LOCUS       NP_001744                178 aa            linear   PRI 28-APR-2025
DEFINITION  caveolin-1 isoform alpha [Homo sapiens].
ACCESSION   NP_001744
VERSION     NP_001744.2
DBSOURCE    REFSEQ: accession NM_001753.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 178)
  AUTHORS   da Silva Correia,A., Schmitz,M., Fischer,A.L., da Silva Correia,S.,
            Simonetti,F.L., Saher,G., Goya-Maldonado,R., Arora,A.S.,
            Fischer,A., Outeiro,T.F. and Zerr,I.
  TITLE     Cellular prion protein acts as mediator of amyloid beta uptake by
            caveolin-1 causing cellular dysfunctions in vitro and in vivo
  JOURNAL   Alzheimers Dement 20 (10), 6776-6792 (2024)
   PUBMED   39212313
  REMARK    GeneRIF: Cellular prion protein acts as mediator of amyloid beta
            uptake by caveolin-1 causing cellular dysfunctions in vitro and in
            vivo.
REFERENCE   2  (residues 1 to 178)
  AUTHORS   Sakaguchi,R., Takahashi,N., Yoshida,T., Ogawa,N., Ueda,Y.,
            Hamano,S., Yamaguchi,K., Sawamura,S., Yamamoto,S., Hara,Y.,
            Kawamoto,T., Suzuki,R., Nakao,A., Mori,M.X., Furukawa,T.,
            Shimizu,S., Inoue,R. and Mori,Y.
  TITLE     Dynamic remodeling of TRPC5 channel-caveolin-1-eNOS protein
            assembly potentiates the positive feedback interaction between Ca2+
            and NO signals
  JOURNAL   J Biol Chem 300 (9), 107705 (2024)
   PUBMED   39178948
  REMARK    GeneRIF: Dynamic remodeling of TRPC5 channel-caveolin-1-eNOS
            protein assembly potentiates the positive feedback interaction
            between Ca[2+] and NO signals.
REFERENCE   3  (residues 1 to 178)
  AUTHORS   Hu,X., Jiang,C., Gu,Y. and Xue,X.
  TITLE     Exploring the conformational dynamics and key amino acids in the
            CD26-caveolin-1 interaction and potential therapeutic interventions
  JOURNAL   Medicine (Baltimore) 103 (22), e38367 (2024)
   PUBMED   39259075
  REMARK    GeneRIF: Exploring the conformational dynamics and key amino acids
            in the CD26-caveolin-1 interaction and potential therapeutic
            interventions.
REFERENCE   4  (residues 1 to 178)
  AUTHORS   Kim,C.A., Delepine,M., Boutet,E., El Mourabit,H., Le Lay,S.,
            Meier,M., Nemani,M., Bridel,E., Leite,C.C., Bertola,D.R.,
            Semple,R.K., O'Rahilly,S., Dugail,I., Capeau,J., Lathrop,M. and
            Magre,J.
  TITLE     Association of a homozygous nonsense caveolin-1 mutation with
            Berardinelli-Seip congenital lipodystrophy
  JOURNAL   J Clin Endocrinol Metab 93 (4), 1129-1134 (2008)
   PUBMED   18211975
  REMARK    GeneRIF: CAV1 as a new Berardinelli-Seip congenital lipodystrophy
            (BSCL)-related gene and support a critical role for caveolins in
            human adipocyte function.
REFERENCE   5  (residues 1 to 178)
  AUTHORS   Engelman,J.A., Zhang,X.L. and Lisanti,M.P.
  TITLE     Genes encoding human caveolin-1 and -2 are co-localized to the
            D7S522 locus (7q31.1), a known fragile site (FRA7G) that is
            frequently deleted in human cancers
  JOURNAL   FEBS Lett 436 (3), 403-410 (1998)
   PUBMED   9801158
REFERENCE   6  (residues 1 to 178)
  AUTHORS   Song,K.S., Li,Shengwen., Okamoto,T., Quilliam,L.A., Sargiacomo,M.
            and Lisanti,M.P.
  TITLE     Co-purification and direct interaction of Ras with caveolin, an
            integral membrane protein of caveolae microdomains. Detergent-free
            purification of caveolae microdomains
  JOURNAL   J Biol Chem 271 (16), 9690-9697 (1996)
   PUBMED   8621645
REFERENCE   7  (residues 1 to 178)
  AUTHORS   Li,S., Seitz,R. and Lisanti,M.P.
  TITLE     Phosphorylation of caveolin by src tyrosine kinases. The
            alpha-isoform of caveolin is selectively phosphorylated by v-Src in
            vivo
  JOURNAL   J Biol Chem 271 (7), 3863-3868 (1996)
   PUBMED   8632005
REFERENCE   8  (residues 1 to 178)
  AUTHORS   Sargiacomo,M., Scherer,P.E., Tang,Z.L., Casanova,J.E. and
            Lisanti,M.P.
  TITLE     In vitro phosphorylation of caveolin-rich membrane domains:
            identification of an associated serine kinase activity as a casein
            kinase II-like enzyme
  JOURNAL   Oncogene 9 (9), 2589-2595 (1994)
   PUBMED   8058322
REFERENCE   9  (residues 1 to 178)
  AUTHORS   Austin,E.D., Phillips,J.A. III and Loyd,J.E.
  TITLE     Heritable Pulmonary Arterial Hypertension Overview
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301658
REFERENCE   10 (residues 1 to 178)
  AUTHORS   Glenney,J.R. Jr.
  TITLE     The sequence of human caveolin reveals identity with VIP21, a
            component of transport vesicles
  JOURNAL   FEBS Lett 314 (1), 45-48 (1992)
   PUBMED   1360410
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AK290871.1, AB209926.1,
            AC006159.3 and BG170208.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Sep 6, 2001 this sequence version replaced NP_001744.1.
            
            Summary: The scaffolding protein encoded by this gene is the main
            component of the caveolae plasma membranes found in most cell
            types. The protein links integrin subunits to the tyrosine kinase
            FYN, an initiating step in coupling integrins to the Ras-ERK
            pathway and promoting cell cycle progression. The gene is a tumor
            suppressor gene candidate and a negative regulator of the
            Ras-p42/44 mitogen-activated kinase cascade. Caveolin 1 and
            caveolin 2 are located next to each other on chromosome 7 and
            express colocalizing proteins that form a stable hetero-oligomeric
            complex. Mutations in this gene have been associated with
            Berardinelli-Seip congenital lipodystrophy. Alternatively spliced
            transcripts encode alpha and beta isoforms of caveolin 1.[provided
            by RefSeq, Mar 2010].
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (alpha).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.273460.1,
                                           SRR3476690.1034034.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000341049.7/ ENSP00000339191.2
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..178
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="7"
                     /map="7q31.2"
     Protein         1..178
                     /product="caveolin-1 isoform alpha"
                     /note="cell growth-inhibiting protein 32; caveolin 1,
                     caveolae protein, 22kDa"
                     /calculated_mol_wt=20341
     Region          2..94
                     /region_name="Required for homooligomerization.
                     /evidence=ECO:0000269|PubMed:25588833"
                     /note="propagated from UniProtKB/Swiss-Prot (Q03135.4)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000269|PubMed:15219854,
                     ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:20068231,
                     ECO:0007744|PubMed:22814378; N-acetylserine.
                     /evidence=ECO:0000269|PubMed:15219854,
                     ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q03135.4)"
     Site            2
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P41350; propagated from
                     UniProtKB/Swiss-Prot (Q03135.4)"
     Site            5
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q03135.4)"
     Site            6
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:15219854,
                     ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:20068231;
                     Phosphotyrosine. /evidence=ECO:0000269|PubMed:8632005;
                     propagated from UniProtKB/Swiss-Prot (Q03135.4)"
     Site            9
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P49817; propagated from
                     UniProtKB/Swiss-Prot (Q03135.4)"
     Site            14
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine, by ABL1.
                     /evidence=ECO:0000269|PubMed:12531427,
                     ECO:0000269|PubMed:8632005; propagated from
                     UniProtKB/Swiss-Prot (Q03135.4)"
     Site            25
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000269|PubMed:8632005; propagated from
                     UniProtKB/Swiss-Prot (Q03135.4)"
     Site            37
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:15219854,
                     ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:21406692,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q03135.4)"
     Region          43..174
                     /region_name="Caveolin"
                     /note="pfam01146"
                     /db_xref="CDD:460081"
     Region          82..94
                     /region_name="Interaction with CAVIN3.
                     /evidence=ECO:0000269|PubMed:25588833"
                     /note="propagated from UniProtKB/Swiss-Prot (Q03135.4)"
     Region          131..142
                     /region_name="Interacts with SPRY1, SPRY2, SPRY3 and
                     SPRY4. /evidence=ECO:0000250|UniProtKB:P49817"
                     /note="propagated from UniProtKB/Swiss-Prot (Q03135.4)"
     Region          149..160
                     /region_name="Interacts with SPRY1, SPRY2, and SPRY4.
                     /evidence=ECO:0000250|UniProtKB:P49817"
                     /note="propagated from UniProtKB/Swiss-Prot (Q03135.4)"
     Region          167..178
                     /region_name="Interacts with SPRY1, SPRY2, SPRY3 and
                     SPRY4. /evidence=ECO:0000250|UniProtKB:P49817"
                     /note="propagated from UniProtKB/Swiss-Prot (Q03135.4)"
     CDS             1..178
                     /gene="CAV1"
                     /gene_synonym="BSCL3; CGL3; LCCNS; MSTP085; PPH3; VIP21"
                     /coded_by="NM_001753.5:28..564"
                     /note="isoform alpha is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS5767.1"
                     /db_xref="GeneID:857"
                     /db_xref="HGNC:HGNC:1527"
                     /db_xref="MIM:601047"
ORIGIN      
        1 msggkyvdse ghlytvpire qgniykpnnk amadelsekq vydahtkeid lvnrdpkhln
       61 ddvvkidfed viaepegths fdgiwkasft tftvtkywfy rllsalfgip maliwgiyfa
      121 ilsflhiwav vpciksflie iqcisrvysi yvhtvcdplf eavgkifsnv rinlqkei
//
