LOCUS       NP_031642                178 aa            linear   ROD 18-MAR-2025
DEFINITION  caveolin-1 isoform 1 [Mus musculus].
ACCESSION   NP_031642
VERSION     NP_031642.1
DBSOURCE    REFSEQ: accession NM_007616.5
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 178)
  AUTHORS   Aboy-Pardal,M.C.M., Guadamillas,M.C., Guerrero,C.R.,
            Catala-Montoro,M., Toledano-Donado,M., Terres-Dominguez,S.,
            Pavon,D.M., Jimenez-Jimenez,V., Jimenez-Carretero,D., Zamai,M.,
            Folgueira,C., Cerezo,A., Lolo,F.N., Nogueiras,R., Sabio,G.,
            Sanchez-Alvarez,M., Echarri,A., Garcia,R. and Del Pozo,M.A.
  TITLE     Plasma membrane remodeling determines adipocyte expansion and
            mechanical adaptability
  JOURNAL   Nat Commun 15 (1), 10102 (2024)
   PUBMED   39609408
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 178)
  AUTHORS   Zhang,L., Chu,W., Feng,X., Li,J., Ren,Y., Yang,Y., Zheng,Z. and
            Li,H.
  TITLE     Caveolin-1 protects retinal ganglion cells in glaucoma by reducing
            TLR4 and activating the Akt/PTEN signaling pathway
  JOURNAL   Pathol Res Pract 262, 155552 (2024)
   PUBMED   39180803
  REMARK    GeneRIF: Caveolin-1 protects retinal ganglion cells in glaucoma by
            reducing TLR4 and activating the Akt/PTEN signaling pathway.
REFERENCE   3  (residues 1 to 178)
  AUTHORS   Liu,S., Zhao,L., Peng,Y., Liu,X., Yan,W., Zhang,L. and Zhang,J.
  TITLE     Obesity induced caveolin-1 impairs osteogenesis via activating
            mitophagy and inhibiting Sirt1 signaling
  JOURNAL   Bone 186, 117146 (2024)
   PUBMED   38844017
  REMARK    GeneRIF: Obesity induced caveolin-1 impairs osteogenesis via
            activating mitophagy and inhibiting Sirt1 signaling.
REFERENCE   4  (residues 1 to 178)
  AUTHORS   Huang,M., Wang,X., Chen,Y., Pessoa,M.T., Terrell,K.C., Zhang,J.,
            Tian,J., Xie,Z., Pierre,S.V. and Cai,L.
  TITLE     Role of Na/K-ATPase alpha1 caveolin-binding motif in adipogenesis
  JOURNAL   Am J Physiol Cell Physiol 327 (1), C48-C64 (2024)
   PUBMED   38708522
  REMARK    GeneRIF: Role of Na/K-ATPase alpha1 caveolin-binding motif in
            adipogenesis.
REFERENCE   5  (residues 1 to 178)
  AUTHORS   Islam,M. and Behura,S.K.
  TITLE     Molecular Regulation of Fetal Brain Development in Inbred and
            Congenic Mouse Strains Differing in Longevity
  JOURNAL   Genes (Basel) 15 (5), 604 (2024)
   PUBMED   38790233
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 178)
  AUTHORS   Tang,Z., Scherer,P.E., Okamoto,T., Song,K., Chu,C., Kohtz,D.S.,
            Nishimoto,I., Lodish,H.F. and Lisanti,M.P.
  TITLE     Molecular cloning of caveolin-3, a novel member of the caveolin
            gene family expressed predominantly in muscle
  JOURNAL   J Biol Chem 271 (4), 2255-2261 (1996)
   PUBMED   8567687
REFERENCE   7  (residues 1 to 178)
  AUTHORS   Scherer,P.E., Okamoto,T., Chun,M., Nishimoto,I., Lodish,H.F. and
            Lisanti,M.P.
  TITLE     Identification, sequence, and expression of caveolin-2 defines a
            caveolin gene family
  JOURNAL   Proc Natl Acad Sci U S A 93 (1), 131-135 (1996)
   PUBMED   8552590
REFERENCE   8  (residues 1 to 178)
  AUTHORS   Way,M. and Parton,R.G.
  TITLE     M-caveolin, a muscle-specific caveolin-related protein
  JOURNAL   FEBS Lett 376 (1-2), 108-112 (1995)
   PUBMED   8521953
REFERENCE   9  (residues 1 to 178)
  AUTHORS   Scherer,P.E., Tang,Z., Chun,M., Sargiacomo,M., Lodish,H.F. and
            Lisanti,M.P.
  TITLE     Caveolin isoforms differ in their N-terminal protein sequence and
            subcellular distribution. Identification and epitope mapping of an
            isoform-specific monoclonal antibody probe
  JOURNAL   J Biol Chem 270 (27), 16395-16401 (1995)
   PUBMED   7608210
REFERENCE   10 (residues 1 to 178)
  AUTHORS   Tang,Z.L., Scherer,P.E. and Lisanti,M.P.
  TITLE     The primary sequence of murine caveolin reveals a conserved
            consensus site for phosphorylation by protein kinase C
  JOURNAL   Gene 147 (2), 299-300 (1994)
   PUBMED   7926819
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC023173.3.
            
            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 :: AK003489.1, BC038280.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849375
                                           [ECO: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="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="6"
                     /map="6 7.73 cM"
     Protein         1..178
                     /product="caveolin-1 isoform 1"
                     /note="caveolin, caveolae protein 1; caveolin-1; caveolin,
                     caveolae protein, 22 kDa"
                     /calculated_mol_wt=20408
     Region          2..94
                     /region_name="Required for homooligomerization.
                     /evidence=ECO:0000250|UniProtKB:Q03135"
                     /note="propagated from UniProtKB/Swiss-Prot (P49817.1)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0007744|PubMed:23806337; propagated from
                     UniProtKB/Swiss-Prot (P49817.1)"
     Site            2
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P41350; propagated from
                     UniProtKB/Swiss-Prot (P49817.1)"
     Site            5
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:23806337; propagated from
                     UniProtKB/Swiss-Prot (P49817.1)"
     Site            6
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q03135; propagated from
                     UniProtKB/Swiss-Prot (P49817.1)"
     Site            9
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (P49817.1)"
     Site            14
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by ABL1 and INSR.
                     /evidence=ECO:0000269|PubMed:12036959,
                     ECO:0000269|PubMed:12531427, ECO:0007744|PubMed:21183079;
                     propagated from UniProtKB/Swiss-Prot (P49817.1)"
     Site            25
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q03135; propagated from
                     UniProtKB/Swiss-Prot (P49817.1)"
     Region          43..174
                     /region_name="Caveolin"
                     /note="pfam01146"
                     /db_xref="CDD:460081"
     Region          82..94
                     /region_name="Interaction with CAVIN3.
                     /evidence=ECO:0000250|UniProtKB:Q03135"
                     /note="propagated from UniProtKB/Swiss-Prot (P49817.1)"
     Region          131..142
                     /region_name="Interacts with SPRY1, SPRY2, SPRY3 and
                     SPRY4. /evidence=ECO:0000269|PubMed:16877379"
                     /note="propagated from UniProtKB/Swiss-Prot (P49817.1)"
     Region          149..160
                     /region_name="Interacts with SPRY1, SPRY2, and SPRY4.
                     /evidence=ECO:0000269|PubMed:16877379"
                     /note="propagated from UniProtKB/Swiss-Prot (P49817.1)"
     Region          167..178
                     /region_name="Interacts with SPRY1, SPRY2, SPRY3 and
                     SPRY4. /evidence=ECO:0000269|PubMed:16877379"
                     /note="propagated from UniProtKB/Swiss-Prot (P49817.1)"
     CDS             1..178
                     /gene="Cav1"
                     /gene_synonym="Cav; Cav-1"
                     /coded_by="NM_007616.5:63..599"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS19924.1"
                     /db_xref="GeneID:12389"
                     /db_xref="MGI:MGI:102709"
ORIGIN      
        1 msggkyvdse ghlytvpire qgniykpnnk amadevtekq vydahtkeid lvnrdpkhln
       61 ddvvkidfed viaepegths fdgiwkasft tftvtkywfy rllstifgip maliwgiyfa
      121 ilsflhiwav vpciksflie iqcisrvysi yvhtfcdplf eaigkifsni ristqkei
//
