CAV1_HUMAN
ID CAV1_HUMAN Reviewed; 178 AA.
AC Q03135; Q9UGP1; Q9UNG1; Q9UQH6;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 236.
DE RecName: Full=Caveolin-1;
GN Name=CAV1; Synonyms=CAV;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Lung;
RX PubMed=1360410; DOI=10.1016/0014-5793(92)81458-x;
RA Glenney J.R. Jr.;
RT "The sequence of human caveolin reveals identity with VIP21, a component of
RT transport vesicles.";
RL FEBS Lett. 314:45-48(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10086342; DOI=10.1038/sj.onc.1202491;
RA Hurlstone A.F., Reid G., Reeves J.R., Fraser J., Strathdee G., Rahilly M.,
RA Parkinson E.K., Black D.M.;
RT "Analysis of the CAVEOLIN-1 gene at human chromosome 7q31.1 in primary
RT tumours and tumour-derived cell lines.";
RL Oncogene 18:1881-1890(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10218480; DOI=10.1016/s0014-5793(99)00365-8;
RA Engelman J.A., Zhang X.L., Lisanti M.P.;
RT "Sequence and detailed organization of the human caveolin-1 and -2 genes
RT located near the D7S522 locus (7q31.1). Methylation of a CpG island in the
RT 5' promoter region of the caveolin-1 gene in human breast cancer cell
RT lines.";
RL FEBS Lett. 448:221-230(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, and Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP PROTEIN SEQUENCE OF 2-66, SUBCELLULAR LOCATION, CLEAVAGE OF INITIATOR
RP METHIONINE, ACETYLATION AT SER-2, PHOSPHORYLATION AT SER-37, CLEAVAGE OF
RP INITIATOR METHIONINE (ISOFORM 2), ACETYLATION AT ALA-2 (ISOFORM 2), AND
RP PHOSPHORYLATION AT SER-6 (ISOFORM 2).
RC TISSUE=Adipose tissue;
RX PubMed=15219854; DOI=10.1016/j.bbrc.2004.05.196;
RA Vainonen J.P., Aboulaich N., Turkina M.V., Stralfors P., Vener A.V.;
RT "N-terminal processing and modifications of caveolin-1 in caveolae from
RT human adipocytes.";
RL Biochem. Biophys. Res. Commun. 320:480-486(2004).
RN [7]
RP PROTEIN SEQUENCE OF 58-65.
RC TISSUE=Adipocyte;
RX PubMed=15242332; DOI=10.1042/bj20040647;
RA Aboulaich N., Vainonen J.P., Stralfors P., Vener A.V.;
RT "Vectorial proteomics reveal targeting, phosphorylation and specific
RT fragmentation of polymerase I and transcript release factor (PTRF) at the
RT surface of caveolae in human adipocytes.";
RL Biochem. J. 383:237-248(2004).
RN [8]
RP PHOSPHORYLATION AT TYR-6; TYR-14 AND TYR-25.
RX PubMed=8632005; DOI=10.1074/jbc.271.7.3863;
RA Li S., Seitz R., Lisanti M.P.;
RT "Phosphorylation of caveolin by src tyrosine kinases. The alpha-isoform of
RT caveolin is selectively phosphorylated by v-Src in vivo.";
RL J. Biol. Chem. 271:3863-3868(1996).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH BMX AND BTK.
RX PubMed=11751885; DOI=10.1074/jbc.m108537200;
RA Vargas L., Nore B.F., Berglof A., Heinonen J.E., Mattsson P.T., Smith C.I.,
RA Mohamed A.J.;
RT "Functional interaction of caveolin-1 with Bruton's tyrosine kinase and
RT Bmx.";
RL J. Biol. Chem. 277:9351-9357(2002).
RN [10]
RP INTERACTION WITH GLIPR2.
RC TISSUE=Brain;
RX PubMed=11865038; DOI=10.1242/jcs.115.4.827;
RA Eberle H.B., Serrano R.L., Fuellekrug J., Schlosser A., Lehmann W.D.,
RA Lottspeich F., Kaloyanova D., Wieland F.T., Helms J.B.;
RT "Identification and characterization of a novel human plant pathogenesis-
RT related protein that localizes to lipid-enriched microdomains in the Golgi
RT complex.";
RL J. Cell Sci. 115:827-838(2002).
RN [11]
RP PHOSPHORYLATION AT TYR-14.
RX PubMed=12531427; DOI=10.1016/s0898-6568(02)00090-6;
RA Sanguinetti A.R., Mastick C.C.;
RT "c-Abl is required for oxidative stress-induced phosphorylation of
RT caveolin-1 on tyrosine 14.";
RL Cell. Signal. 15:289-298(2003).
RN [12]
RP INTERACTION WITH NOSTRIN.
RX PubMed=16807357; DOI=10.1091/mbc.e05-08-0709;
RA Schilling K., Opitz N., Wiesenthal A., Oess S., Tikkanen R.,
RA Mueller-Esterl W., Icking A.;
RT "Translocation of endothelial nitric-oxide synthase involves a ternary
RT complex with caveolin-1 and NOSTRIN.";
RL Mol. Biol. Cell 17:3870-3880(2006).
RN [13]
RP INTERACTION WITH ROTAVIRUS A NSP4 (MICROBIAL INFECTION).
RX PubMed=16501093; DOI=10.1128/jvi.80.6.2842-2854.2006;
RA Parr R.D., Storey S.M., Mitchell D.M., McIntosh A.L., Zhou M., Mir K.D.,
RA Ball J.M.;
RT "The rotavirus enterotoxin NSP4 directly interacts with the caveolar
RT structural protein caveolin-1.";
RL J. Virol. 80:2842-2854(2006).
RN [14]
RP FUNCTION, INTERACTION WITH DPP4, AND SUBCELLULAR LOCATION.
RX PubMed=17287217; DOI=10.1074/jbc.m609157200;
RA Ohnuma K., Uchiyama M., Yamochi T., Nishibashi K., Hosono O., Takahashi N.,
RA Kina S., Tanaka H., Lin X., Dang N.H., Morimoto C.;
RT "Caveolin-1 triggers T-cell activation via CD26 in association with
RT CARMA1.";
RL J. Biol. Chem. 282:10117-10131(2007).
RN [15]
RP INVOLVEMENT IN CGL3.
RX PubMed=18211975; DOI=10.1210/jc.2007-1328;
RA Kim C.A., Delepine M., Boutet E., El Mourabit H., Le Lay S., Meier M.,
RA Nemani M., Bridel E., Leite C.C., Bertola D.R., Semple R.K., O'Rahilly S.,
RA Dugail I., Capeau J., Lathrop M., Magre J.;
RT "Association of a homozygous nonsense caveolin-1 mutation with
RT Berardinelli-Seip congenital lipodystrophy.";
RL J. Clin. Endocrinol. Metab. 93:1129-1134(2008).
RN [16]
RP INVOLVEMENT IN FPLD7.
RX PubMed=18237401; DOI=10.1186/1476-511x-7-3;
RA Cao H., Alston L., Ruschman J., Hegele R.A.;
RT "Heterozygous CAV1 frameshift mutations (MIM 601047) in patients with
RT atypical partial lipodystrophy and hypertriglyceridemia.";
RL Lipids Health Dis. 7:3-3(2008).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [18]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INTERACTION WITH
RP CAVIN3.
RX PubMed=19262564; DOI=10.1038/emboj.2009.46;
RA McMahon K.A., Zajicek H., Li W.P., Peyton M.J., Minna J.D., Hernandez V.J.,
RA Luby-Phelps K., Anderson R.G.;
RT "SRBC/cavin-3 is a caveolin adapter protein that regulates caveolae
RT function.";
RL EMBO J. 28:1001-1015(2009).
RN [19]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2 (ISOFORM 2), PHOSPHORYLATION
RP [LARGE SCALE ANALYSIS] AT SER-6 (ISOFORM 2), CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS] (ISOFORM 2), AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [20]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-5, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [21]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2 (ISOFORM 2), PHOSPHORYLATION
RP [LARGE SCALE ANALYSIS] AT SER-6 (ISOFORM 2), CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS] (ISOFORM 2), AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [22]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [24]
RP INVOLVEMENT IN PPH3.
RX PubMed=22474227; DOI=10.1161/circgenetics.111.961888;
RA Austin E.D., Ma L., LeDuc C., Berman Rosenzweig E., Borczuk A.,
RA Phillips J.A. III, Palomero T., Sumazin P., Kim H.R., Talati M.H., West J.,
RA Loyd J.E., Chung W.K.;
RT "Whole exome sequencing to identify a novel gene (caveolin-1) associated
RT with human pulmonary arterial hypertension.";
RL Circ. Cardiovasc. Genet. 5:336-343(2012).
RN [25]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, ACETYLATION [LARGE SCALE
RP ANALYSIS] AT ALA-2 (ISOFORM 2), CLEAVAGE OF INITIATOR METHIONINE [LARGE
RP SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS]
RP (ISOFORM 2), AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [26]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [27]
RP INTERACTION WITH ABCG1.
RX PubMed=24576892; DOI=10.1016/j.bbalip.2014.02.002;
RA Gu H.M., Wang F.Q., Zhang D.W.;
RT "Caveolin-1 interacts with ATP binding cassette transporter G1 (ABCG1) and
RT regulates ABCG1-mediated cholesterol efflux.";
RL Biochim. Biophys. Acta 1841:847-858(2014).
RN [28]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [29]
RP INTERACTION WITH CAVIN1; CAVIN3 AND EHD2, SUBCELLULAR LOCATION, AND
RP SUBUNIT.
RX PubMed=25588833; DOI=10.1242/jcs.161463;
RA Mohan J., Moren B., Larsson E., Holst M.R., Lundmark R.;
RT "Cavin3 interacts with cavin1 and caveolin1 to increase surface dynamics of
RT caveolae.";
RL J. Cell Sci. 128:979-991(2015).
RN [30]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH TGFBR1.
RX PubMed=25893292; DOI=10.1038/onc.2015.100;
RA Hwangbo C., Tae N., Lee S., Kim O., Park O.K., Kim J., Kwon S.H., Lee J.H.;
RT "Syntenin regulates TGF-beta1-induced Smad activation and the epithelial-
RT to-mesenchymal transition by inhibiting caveolin-mediated TGF-beta type I
RT receptor internalization.";
RL Oncogene 35:389-401(2016).
RN [31]
RP VARIANT LEU-132, AND CHARACTERIZATION OF VARIANT LEU-132.
RX PubMed=12368209; DOI=10.1016/s0002-9440(10)64412-4;
RA Lee H., Park D.S., Razani B., Russell R.G., Pestell R.G., Lisanti M.P.;
RT "Caveolin-1 mutations (P132L and null) and the pathogenesis of breast
RT cancer: caveolin-1 (P132L) behaves in a dominant-negative manner and
RT caveolin-1 (-/-) null mice show mammary epithelial cell hyperplasia.";
RL Am. J. Pathol. 161:1357-1369(2002).
RN [32]
RP INTERACTION WITH VCP AND UBXN6, UBIQUITINATION, AND CHARACTERIZATION OF
RP VARIANT LEU-132.
RX PubMed=21822278; DOI=10.1038/ncb2301;
RA Ritz D., Vuk M., Kirchner P., Bug M., Schuetz S., Hayer A., Bremer S.,
RA Lusk C., Baloh R.H., Lee H., Glatter T., Gstaiger M., Aebersold R.,
RA Weihl C.C., Meyer H.;
RT "Endolysosomal sorting of ubiquitylated caveolin-1 is regulated by VCP and
RT UBXD1 and impaired by VCP disease mutations.";
RL Nat. Cell Biol. 13:1116-1123(2011).
RN [33]
RP INTERACTION WITH VCP AND UBXN6, AND UBIQUITINATION AT LYS-5; LYS-26;
RP LYS-30; LYS-39; LYS-47 AND LYS-57.
RX PubMed=23335559; DOI=10.1074/jbc.m112.429076;
RA Kirchner P., Bug M., Meyer H.;
RT "Ubiquitination of the N-terminal region of caveolin-1 regulates endosomal
RT sorting by the VCP/p97 AAA-ATPase.";
RL J. Biol. Chem. 288:7363-7372(2013).
RN [34]
RP INTERACTION WITH HRSV MATRIX PROTEIN (MICROBIAL INFECTION).
RX PubMed=25556234; DOI=10.1074/mcp.m114.044107;
RA Kipper S., Hamad S., Caly L., Avrahami D., Bacharach E., Jans D.A.,
RA Gerber D., Bajorek M.;
RT "New host factors important for respiratory syncytial virus (RSV)
RT replication revealed by a novel microfluidics screen for interactors of
RT matrix (M) protein.";
RL Mol. Cell. Proteomics 14:532-543(2015).
CC -!- FUNCTION: May act as a scaffolding protein within caveolar membranes
CC (PubMed:11751885). Forms a stable heterooligomeric complex with CAV2
CC that targets to lipid rafts and drives caveolae formation. Mediates the
CC recruitment of CAVIN proteins (CAVIN1/2/3/4) to the caveolae
CC (PubMed:19262564). Interacts directly with G-protein alpha subunits and
CC can functionally regulate their activity (By similarity). Involved in
CC the costimulatory signal essential for T-cell receptor (TCR)-mediated
CC T-cell activation. Its binding to DPP4 induces T-cell proliferation and
CC NF-kappa-B activation in a T-cell receptor/CD3-dependent manner
CC (PubMed:17287217). Recruits CTNNB1 to caveolar membranes and may
CC regulate CTNNB1-mediated signaling through the Wnt pathway (By
CC similarity). Negatively regulates TGFB1-mediated activation of SMAD2/3
CC by mediating the internalization of TGFBR1 from membrane rafts leading
CC to its subsequent degradation (PubMed:25893292).
CC {ECO:0000250|UniProtKB:P49817, ECO:0000269|PubMed:11751885,
CC ECO:0000269|PubMed:17287217, ECO:0000269|PubMed:19262564,
CC ECO:0000269|PubMed:25893292}.
CC -!- SUBUNIT: Homooligomer (PubMed:25588833). Interacts with GLIPR2
CC (PubMed:11865038). Interacts with NOSTRIN (PubMed:16807357). Interacts
CC with SNAP25 and STX1A (By similarity). Interacts (via the N-terminus)
CC with DPP4; the interaction is direct (PubMed:17287217). Interacts with
CC CTNNB1, CDH1 and JUP. Interacts with PACSIN2; this interaction induces
CC membrane tubulation (By similarity). Interacts with SLC7A9 (By
CC similarity). Interacts with BMX and BTK (PubMed:11751885). Interacts
CC with TGFBR1 (PubMed:25893292). Interacts with CAVIN3 (via leucine-
CC zipper domain) in a cholesterol-sensitive manner (PubMed:25588833,
CC PubMed:19262564). Interacts with CAVIN1 (PubMed:25588833). Interacts
CC with EHD2 in a cholesterol-dependent manner (PubMed:25588833). Forms a
CC ternary complex with UBXN6 and VCP; mediates CAV1 targeting to
CC lysosomes for degradation (PubMed:21822278, PubMed:23335559). Interacts
CC with ABCG1; this interaction regulates ABCG1-mediated cholesterol
CC efflux (PubMed:24576892). Interacts with NEU3; this interaction
CC enhances NEU3 sialidase activity within caveola. Interacts (via C-
CC terminus) with SPRY1, SPRY2 (via C-terminus), SPRY3, and SPRY4 (By
CC similarity). {ECO:0000250|UniProtKB:P41350,
CC ECO:0000250|UniProtKB:P49817, ECO:0000250|UniProtKB:Q2IBA5,
CC ECO:0000269|PubMed:11751885, ECO:0000269|PubMed:11865038,
CC ECO:0000269|PubMed:16807357, ECO:0000269|PubMed:17287217,
CC ECO:0000269|PubMed:19262564, ECO:0000269|PubMed:21822278,
CC ECO:0000269|PubMed:23335559, ECO:0000269|PubMed:24576892,
CC ECO:0000269|PubMed:25588833, ECO:0000269|PubMed:25893292}.
CC -!- SUBUNIT: (Microbial infection) Interacts with rotavirus A NSP4.
CC {ECO:0000269|PubMed:16501093}.
CC -!- SUBUNIT: (Microbial infection) Interacts with human respiratory
CC syncytial virus (HRSV) matrix protein; this interaction probably
CC facilitates viral budding. {ECO:0000269|PubMed:25556234}.
CC -!- INTERACTION:
CC Q03135; P05067: APP; NbExp=3; IntAct=EBI-603614, EBI-77613;
CC Q03135; P55957: BID; NbExp=3; IntAct=EBI-603614, EBI-519672;
CC Q03135; P51636: CAV2; NbExp=4; IntAct=EBI-603614, EBI-603607;
CC Q03135; Q6NZI2: CAVIN1; NbExp=10; IntAct=EBI-603614, EBI-2559016;
CC Q03135; O95810: CAVIN2; NbExp=6; IntAct=EBI-603614, EBI-742141;
CC Q03135; Q969G5: CAVIN3; NbExp=11; IntAct=EBI-603614, EBI-3893101;
CC Q03135; P48730-2: CSNK1D; NbExp=3; IntAct=EBI-603614, EBI-9087876;
CC Q03135; P00533: EGFR; NbExp=7; IntAct=EBI-603614, EBI-297353;
CC Q03135; P25116: F2R; NbExp=3; IntAct=EBI-603614, EBI-2803960;
CC Q03135; P25445: FAS; NbExp=3; IntAct=EBI-603614, EBI-494743;
CC Q03135; P25445-1: FAS; NbExp=3; IntAct=EBI-603614, EBI-15749113;
CC Q03135; P41134: ID1; NbExp=6; IntAct=EBI-603614, EBI-1215527;
CC Q03135; Q12809: KCNH2; NbExp=5; IntAct=EBI-603614, EBI-720643;
CC Q03135; O75581: LRP6; NbExp=3; IntAct=EBI-603614, EBI-910915;
CC Q03135; Q9GZQ8: MAP1LC3B; NbExp=2; IntAct=EBI-603614, EBI-373144;
CC Q03135; Q07820: MCL1; NbExp=3; IntAct=EBI-603614, EBI-1003422;
CC Q03135; O15118: NPC1; NbExp=3; IntAct=EBI-603614, EBI-2368710;
CC Q03135; P19174: PLCG1; NbExp=2; IntAct=EBI-603614, EBI-79387;
CC Q03135; P18031: PTPN1; NbExp=5; IntAct=EBI-603614, EBI-968788;
CC Q03135; O00194: RAB27B; NbExp=2; IntAct=EBI-603614, EBI-10179046;
CC Q03135; P63000: RAC1; NbExp=3; IntAct=EBI-603614, EBI-413628;
CC Q03135; P20936: RASA1; NbExp=2; IntAct=EBI-603614, EBI-1026476;
CC Q03135; P22307: SCP2; NbExp=3; IntAct=EBI-603614, EBI-1050999;
CC Q03135; Q15208: STK38; NbExp=3; IntAct=EBI-603614, EBI-458376;
CC Q03135; P48995: TRPC1; NbExp=7; IntAct=EBI-603614, EBI-929665;
CC Q03135; Q16881: TXNRD1; NbExp=4; IntAct=EBI-603614, EBI-716617;
CC Q03135; P52735: VAV2; NbExp=2; IntAct=EBI-603614, EBI-297549;
CC Q03135; P52735-1: VAV2; NbExp=3; IntAct=EBI-603614, EBI-15875004;
CC Q03135; O70239: Axin1; Xeno; NbExp=5; IntAct=EBI-603614, EBI-6857773;
CC Q03135; Q03160: Grb7; Xeno; NbExp=3; IntAct=EBI-603614, EBI-7100053;
CC Q03135; P0DOE7: M; Xeno; NbExp=2; IntAct=EBI-603614, EBI-10042882;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane; Peripheral membrane
CC protein. Cell membrane; Peripheral membrane protein. Membrane, caveola
CC {ECO:0000269|PubMed:19262564, ECO:0000269|PubMed:25588833}; Peripheral
CC membrane protein. Membrane raft {ECO:0000269|PubMed:25893292}. Golgi
CC apparatus, trans-Golgi network {ECO:0000250|UniProtKB:P33724}.
CC Note=Colocalized with DPP4 in membrane rafts. Potential hairpin-like
CC structure in the membrane. Membrane protein of caveolae.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=1;
CC IsoId=Q03135-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q03135-2; Sequence=VSP_018692;
CC -!- TISSUE SPECIFICITY: Skeletal muscle, liver, stomach, lung, kidney and
CC heart (at protein level). Expressed in the brain.
CC {ECO:0000269|PubMed:19262564}.
CC -!- PTM: Ubiquitinated. Undergo monoubiquitination and multi- and/or
CC polyubiquitination (PubMed:21822278). Monoubiquitination of N-terminal
CC lysines promotes integration in a ternary complex with UBXN6 and VCP
CC which promotes oligomeric CAV1 targeting to lysosomes for degradation
CC (PubMed:23335559). {ECO:0000269|PubMed:21822278,
CC ECO:0000269|PubMed:23335559}.
CC -!- PTM: The initiator methionine for isoform 2 is removed during or just
CC after translation. The new N-terminal amino acid is then N-acetylated.
CC {ECO:0000269|PubMed:15219854}.
CC -!- PTM: Phosphorylated at Tyr-14 by ABL1 in response to oxidative stress.
CC {ECO:0000269|PubMed:12531427, ECO:0000269|PubMed:15219854,
CC ECO:0000269|PubMed:8632005}.
CC -!- DISEASE: Congenital generalized lipodystrophy 3 (CGL3) [MIM:612526]: An
CC autosomal recessive disorder characterized by a near complete absence
CC of adipose tissue, extreme insulin resistance, hypertriglyceridemia,
CC hepatic steatosis and early onset of diabetes.
CC {ECO:0000269|PubMed:18211975}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Pulmonary hypertension, primary, 3 (PPH3) [MIM:615343]: A rare
CC disorder characterized by plexiform lesions of proliferating
CC endothelial cells in pulmonary arterioles. The lesions lead to elevated
CC pulmonary arterial pression, right ventricular failure, and death. The
CC disease can occur from infancy throughout life and it has a mean age at
CC onset of 36 years. Penetrance is reduced. Although familial pulmonary
CC hypertension is rare, cases secondary to known etiologies are more
CC common and include those associated with the appetite-suppressant
CC drugs. {ECO:0000269|PubMed:22474227}. Note=The disease is caused by
CC variants affecting the gene represented in this entry.
CC -!- DISEASE: Lipodystrophy, familial partial, 7 (FPLD7) [MIM:606721]: A
CC form of partial lipodystrophy, a disorder characterized by abnormal
CC subcutaneous fat distribution. Affected individuals manifest a gradual
CC loss of subcutaneous adipose tissue in various parts of the body,
CC accompanied by an accumulation of adipose tissue in the face and neck
CC in some cases causing a double chin, fat neck, or cushingoid
CC appearance. FPLD7 is an autosomal dominant form with a variable
CC phenotype. Some patients manifest congenital cataracts and
CC neurodegeneration leading to cerebellar and spinal cord dysfunction.
CC {ECO:0000269|PubMed:18237401}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the caveolin family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/CAV1ID932ch7q31.html";
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Caveolin entry;
CC URL="https://en.wikipedia.org/wiki/Caveolin";
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; Z18951; CAA79476.1; -; mRNA.
DR EMBL; AF095593; AAD23745.1; -; Genomic_DNA.
DR EMBL; AF095591; AAD23745.1; JOINED; Genomic_DNA.
DR EMBL; AF095592; AAD23745.1; JOINED; Genomic_DNA.
DR EMBL; AJ133269; CAB63654.1; -; Genomic_DNA.
DR EMBL; AF125348; AAD34722.1; -; Genomic_DNA.
DR EMBL; BT007143; AAP35807.1; -; mRNA.
DR EMBL; BC009685; AAH09685.1; -; mRNA.
DR EMBL; BC082246; AAH82246.1; -; mRNA.
DR CCDS; CCDS55156.1; -. [Q03135-2]
DR CCDS; CCDS5767.1; -. [Q03135-1]
DR PIR; S26884; S26884.
DR RefSeq; NP_001744.2; NM_001753.4. [Q03135-1]
DR AlphaFoldDB; Q03135; -.
DR BioGRID; 107305; 703.
DR CORUM; Q03135; -.
DR DIP; DIP-5960N; -.
DR IntAct; Q03135; 178.
DR MINT; Q03135; -.
DR STRING; 9606.ENSP00000339191; -.
DR BindingDB; Q03135; -.
DR ChEMBL; CHEMBL3808270; -.
DR TCDB; 8.A.26.1.1; the caveolin (caveolin) family.
DR GlyGen; Q03135; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q03135; -.
DR MetOSite; Q03135; -.
DR PhosphoSitePlus; Q03135; -.
DR SwissPalm; Q03135; -.
DR BioMuta; CAV1; -.
DR DMDM; 13637934; -.
DR EPD; Q03135; -.
DR jPOST; Q03135; -.
DR MassIVE; Q03135; -.
DR MaxQB; Q03135; -.
DR PaxDb; Q03135; -.
DR PeptideAtlas; Q03135; -.
DR PRIDE; Q03135; -.
DR ProteomicsDB; 58192; -. [Q03135-1]
DR ProteomicsDB; 58193; -. [Q03135-2]
DR TopDownProteomics; Q03135-1; -. [Q03135-1]
DR TopDownProteomics; Q03135-2; -. [Q03135-2]
DR ABCD; Q03135; 3 sequenced antibodies.
DR Antibodypedia; 3530; 1199 antibodies from 47 providers.
DR DNASU; 857; -.
DR Ensembl; ENST00000341049.7; ENSP00000339191.2; ENSG00000105974.13. [Q03135-1]
DR Ensembl; ENST00000393467.1; ENSP00000377110.1; ENSG00000105974.13. [Q03135-2]
DR Ensembl; ENST00000393468.1; ENSP00000377111.1; ENSG00000105974.13. [Q03135-2]
DR Ensembl; ENST00000405348.6; ENSP00000384348.1; ENSG00000105974.13. [Q03135-2]
DR GeneID; 857; -.
DR KEGG; hsa:857; -.
DR MANE-Select; ENST00000341049.7; ENSP00000339191.2; NM_001753.5; NP_001744.2.
DR UCSC; uc003vig.3; human. [Q03135-1]
DR CTD; 857; -.
DR DisGeNET; 857; -.
DR GeneCards; CAV1; -.
DR GeneReviews; CAV1; -.
DR HGNC; HGNC:1527; CAV1.
DR HPA; ENSG00000105974; Tissue enhanced (adipose).
DR MalaCards; CAV1; -.
DR MIM; 601047; gene.
DR MIM; 606721; phenotype.
DR MIM; 612526; phenotype.
DR MIM; 615343; phenotype.
DR neXtProt; NX_Q03135; -.
DR OpenTargets; ENSG00000105974; -.
DR Orphanet; 528; Congenital generalized lipodystrophy.
DR Orphanet; 220393; Diffuse cutaneous systemic sclerosis.
DR Orphanet; 275777; Heritable pulmonary arterial hypertension.
DR Orphanet; 220402; Limited cutaneous systemic sclerosis.
DR PharmGKB; PA26107; -.
DR VEuPathDB; HostDB:ENSG00000105974; -.
DR eggNOG; ENOG502QUK5; Eukaryota.
DR GeneTree; ENSGT00950000183006; -.
DR InParanoid; Q03135; -.
DR OMA; SIRINMQ; -.
DR PhylomeDB; Q03135; -.
DR TreeFam; TF315736; -.
DR PathwayCommons; Q03135; -.
DR Reactome; R-HSA-163560; Triglyceride catabolism.
DR Reactome; R-HSA-203615; eNOS activation.
DR Reactome; R-HSA-203641; NOSTRIN mediated eNOS trafficking.
DR Reactome; R-HSA-210991; Basigin interactions.
DR Reactome; R-HSA-4641262; Disassembly of the destruction complex and recruitment of AXIN to the membrane.
DR Reactome; R-HSA-5218920; VEGFR2 mediated vascular permeability.
DR Reactome; R-HSA-8980692; RHOA GTPase cycle.
DR Reactome; R-HSA-9009391; Extra-nuclear estrogen signaling.
DR Reactome; R-HSA-9013026; RHOB GTPase cycle.
DR Reactome; R-HSA-9013106; RHOC GTPase cycle.
DR Reactome; R-HSA-9013148; CDC42 GTPase cycle.
DR Reactome; R-HSA-9013149; RAC1 GTPase cycle.
DR Reactome; R-HSA-9013404; RAC2 GTPase cycle.
DR Reactome; R-HSA-9013405; RHOD GTPase cycle.
DR Reactome; R-HSA-9013406; RHOQ GTPase cycle.
DR Reactome; R-HSA-9013407; RHOH GTPase cycle.
DR Reactome; R-HSA-9013408; RHOG GTPase cycle.
DR Reactome; R-HSA-9013409; RHOJ GTPase cycle.
DR Reactome; R-HSA-9013423; RAC3 GTPase cycle.
DR Reactome; R-HSA-9035034; RHOF GTPase cycle.
DR Reactome; R-HSA-9617828; FOXO-mediated transcription of cell cycle genes.
DR Reactome; R-HSA-9696264; RND3 GTPase cycle.
DR Reactome; R-HSA-9696270; RND2 GTPase cycle.
DR Reactome; R-HSA-9696273; RND1 GTPase cycle.
DR Reactome; R-HSA-9755779; SARS-CoV-2 targets host intracellular signalling and regulatory pathways.
DR Reactome; R-HSA-9767675; SARS-CoV-1-host interactions.
DR SignaLink; Q03135; -.
DR SIGNOR; Q03135; -.
DR BioGRID-ORCS; 857; 16 hits in 1084 CRISPR screens.
DR ChiTaRS; CAV1; human.
DR GeneWiki; Caveolin_1; -.
DR GenomeRNAi; 857; -.
DR Pharos; Q03135; Tbio.
DR PRO; PR:Q03135; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q03135; protein.
DR Bgee; ENSG00000105974; Expressed in lower lobe of lung and 207 other tissues.
DR ExpressionAtlas; Q03135; baseline and differential.
DR Genevisible; Q03135; HS.
DR GO; GO:0002080; C:acrosomal membrane; IEA:Ensembl.
DR GO; GO:0016324; C:apical plasma membrane; IDA:BHF-UCL.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:BHF-UCL.
DR GO; GO:0005901; C:caveola; IDA:UniProtKB.
DR GO; GO:0002095; C:caveolar macromolecular signaling complex; IEA:Ensembl.
DR GO; GO:0005938; C:cell cortex; IEA:Ensembl.
DR GO; GO:0005929; C:cilium; IEA:Ensembl.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:UniProtKB.
DR GO; GO:0031901; C:early endosome membrane; TAS:Reactome.
DR GO; GO:0030666; C:endocytic vesicle membrane; TAS:Reactome.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:HGNC-UCL.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:ParkinsonsUK-UCL.
DR GO; GO:0005768; C:endosome; IDA:UniProtKB.
DR GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0000139; C:Golgi membrane; IDA:HGNC-UCL.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005811; C:lipid droplet; TAS:Reactome.
DR GO; GO:0016020; C:membrane; IDA:AgBase.
DR GO; GO:0045121; C:membrane raft; IDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR GO; GO:0051117; F:ATPase binding; IPI:ParkinsonsUK-UCL.
DR GO; GO:0015485; F:cholesterol binding; TAS:HGNC-UCL.
DR GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:BHF-UCL.
DR GO; GO:0070320; F:inward rectifier potassium channel inhibitor activity; IDA:BHF-UCL.
DR GO; GO:0060090; F:molecular adaptor activity; IBA:GO_Central.
DR GO; GO:0050998; F:nitric-oxide synthase binding; IPI:BHF-UCL.
DR GO; GO:0005113; F:patched binding; NAS:BHF-UCL.
DR GO; GO:0016504; F:peptidase activator activity; ISS:BHF-UCL.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:Ensembl.
DR GO; GO:0019901; F:protein kinase binding; IPI:BHF-UCL.
DR GO; GO:0044877; F:protein-containing complex binding; IPI:ParkinsonsUK-UCL.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IEA:Ensembl.
DR GO; GO:0005102; F:signaling receptor binding; IPI:BHF-UCL.
DR GO; GO:0031267; F:small GTPase binding; IPI:AgBase.
DR GO; GO:0044325; F:transmembrane transporter binding; IPI:BHF-UCL.
DR GO; GO:0001525; P:angiogenesis; IEA:Ensembl.
DR GO; GO:0086098; P:angiotensin-activated signaling pathway involved in heart process; ISS:BHF-UCL.
DR GO; GO:0097190; P:apoptotic signaling pathway; IMP:UniProtKB.
DR GO; GO:0071711; P:basement membrane organization; IEA:Ensembl.
DR GO; GO:0055074; P:calcium ion homeostasis; ISS:BHF-UCL.
DR GO; GO:0006816; P:calcium ion transport; ISS:BHF-UCL.
DR GO; GO:0070836; P:caveola assembly; IMP:BHF-UCL.
DR GO; GO:0072584; P:caveolin-mediated endocytosis; IDA:UniProtKB.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; ISS:BHF-UCL.
DR GO; GO:0071360; P:cellular response to exogenous dsRNA; IMP:UniProtKB.
DR GO; GO:0071455; P:cellular response to hyperoxia; IMP:UniProtKB.
DR GO; GO:0071375; P:cellular response to peptide hormone stimulus; ISS:BHF-UCL.
DR GO; GO:0009267; P:cellular response to starvation; IEP:BHF-UCL.
DR GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; IEA:Ensembl.
DR GO; GO:0042632; P:cholesterol homeostasis; ISS:BHF-UCL.
DR GO; GO:0030301; P:cholesterol transport; TAS:HGNC-UCL.
DR GO; GO:0019221; P:cytokine-mediated signaling pathway; IEA:Ensembl.
DR GO; GO:0001935; P:endothelial cell proliferation; IEA:Ensembl.
DR GO; GO:0051649; P:establishment of localization in cell; IEA:Ensembl.
DR GO; GO:0048144; P:fibroblast proliferation; IEA:Ensembl.
DR GO; GO:0002067; P:glandular epithelial cell differentiation; IEA:Ensembl.
DR GO; GO:0038016; P:insulin receptor internalization; IEA:Ensembl.
DR GO; GO:0007595; P:lactation; IEA:Ensembl.
DR GO; GO:0019915; P:lipid storage; ISS:BHF-UCL.
DR GO; GO:0032507; P:maintenance of protein location in cell; ISS:BHF-UCL.
DR GO; GO:0030879; P:mammary gland development; ISS:BHF-UCL.
DR GO; GO:0060056; P:mammary gland involution; ISS:BHF-UCL.
DR GO; GO:0000165; P:MAPK cascade; IEA:Ensembl.
DR GO; GO:0051899; P:membrane depolarization; ISS:BHF-UCL.
DR GO; GO:0046716; P:muscle cell cellular homeostasis; IEA:Ensembl.
DR GO; GO:2000811; P:negative regulation of anoikis; IMP:UniProtKB.
DR GO; GO:0030514; P:negative regulation of BMP signaling pathway; IDA:BHF-UCL.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; ISS:UniProtKB.
DR GO; GO:0001960; P:negative regulation of cytokine-mediated signaling pathway; IEA:Ensembl.
DR GO; GO:0001937; P:negative regulation of endothelial cell proliferation; ISS:BHF-UCL.
DR GO; GO:0030857; P:negative regulation of epithelial cell differentiation; ISS:BHF-UCL.
DR GO; GO:0048147; P:negative regulation of fibroblast proliferation; IEA:Ensembl.
DR GO; GO:1903609; P:negative regulation of inward rectifier potassium channel activity; IMP:BHF-UCL.
DR GO; GO:0043407; P:negative regulation of MAP kinase activity; IEA:Ensembl.
DR GO; GO:0043409; P:negative regulation of MAPK cascade; ISS:BHF-UCL.
DR GO; GO:0060546; P:negative regulation of necroptotic process; IEA:Ensembl.
DR GO; GO:0045019; P:negative regulation of nitric oxide biosynthetic process; ISS:BHF-UCL.
DR GO; GO:0051001; P:negative regulation of nitric-oxide synthase activity; IEA:Ensembl.
DR GO; GO:0033137; P:negative regulation of peptidyl-serine phosphorylation; IDA:BHF-UCL.
DR GO; GO:1900085; P:negative regulation of peptidyl-tyrosine autophosphorylation; IMP:BHF-UCL.
DR GO; GO:0048550; P:negative regulation of pinocytosis; IMP:UniProtKB.
DR GO; GO:1901380; P:negative regulation of potassium ion transmembrane transport; IMP:BHF-UCL.
DR GO; GO:0032091; P:negative regulation of protein binding; IDA:BHF-UCL.
DR GO; GO:0061099; P:negative regulation of protein tyrosine kinase activity; IMP:BHF-UCL.
DR GO; GO:0031397; P:negative regulation of protein ubiquitination; IMP:UniProtKB.
DR GO; GO:0046426; P:negative regulation of receptor signaling pathway via JAK-STAT; ISS:BHF-UCL.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0042532; P:negative regulation of tyrosine phosphorylation of STAT protein; IEA:Ensembl.
DR GO; GO:0006809; P:nitric oxide biosynthetic process; IEA:Ensembl.
DR GO; GO:0033484; P:nitric oxide homeostasis; ISS:BHF-UCL.
DR GO; GO:0010524; P:positive regulation of calcium ion transport into cytosol; ISS:BHF-UCL.
DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; IMP:BHF-UCL.
DR GO; GO:0043085; P:positive regulation of catalytic activity; ISS:BHF-UCL.
DR GO; GO:0060355; P:positive regulation of cell adhesion molecule production; IMP:UniProtKB.
DR GO; GO:0030335; P:positive regulation of cell migration; IMP:BHF-UCL.
DR GO; GO:0010875; P:positive regulation of cholesterol efflux; IDA:ARUK-UCL.
DR GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; ISS:YuBioLab.
DR GO; GO:1903071; P:positive regulation of ER-associated ubiquitin-dependent protein catabolic process; IMP:ParkinsonsUK-UCL.
DR GO; GO:2001238; P:positive regulation of extrinsic apoptotic signaling pathway; IMP:UniProtKB.
DR GO; GO:1903598; P:positive regulation of gap junction assembly; ISS:BHF-UCL.
DR GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
DR GO; GO:2001244; P:positive regulation of intrinsic apoptotic signaling pathway; IMP:UniProtKB.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IMP:ARUK-UCL.
DR GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; IDA:BHF-UCL.
DR GO; GO:0032092; P:positive regulation of protein binding; IMP:ParkinsonsUK-UCL.
DR GO; GO:0031398; P:positive regulation of protein ubiquitination; IMP:ParkinsonsUK-UCL.
DR GO; GO:0034141; P:positive regulation of toll-like receptor 3 signaling pathway; IMP:UniProtKB.
DR GO; GO:0045907; P:positive regulation of vasoconstriction; ISS:BHF-UCL.
DR GO; GO:0010608; P:post-transcriptional regulation of gene expression; IEA:Ensembl.
DR GO; GO:0008104; P:protein localization; ISS:BHF-UCL.
DR GO; GO:1903361; P:protein localization to basolateral plasma membrane; ISS:BHF-UCL.
DR GO; GO:0044860; P:protein localization to plasma membrane raft; ISS:BHF-UCL.
DR GO; GO:0015031; P:protein transport; IEA:Ensembl.
DR GO; GO:0031623; P:receptor internalization; IDA:UniProtKB.
DR GO; GO:2000286; P:receptor internalization involved in canonical Wnt signaling pathway; IMP:BHF-UCL.
DR GO; GO:0019065; P:receptor-mediated endocytosis of virus by host cell; IGI:CACAO.
DR GO; GO:0030193; P:regulation of blood coagulation; IMP:BHF-UCL.
DR GO; GO:0098909; P:regulation of cardiac muscle cell action potential involved in regulation of contraction; IC:BHF-UCL.
DR GO; GO:1901844; P:regulation of cell communication by electrical coupling involved in cardiac conduction; ISS:BHF-UCL.
DR GO; GO:0051480; P:regulation of cytosolic calcium ion concentration; IDA:BHF-UCL.
DR GO; GO:2000535; P:regulation of entry of bacterium into host cell; IDA:AgBase.
DR GO; GO:0019217; P:regulation of fatty acid metabolic process; ISS:BHF-UCL.
DR GO; GO:0086091; P:regulation of heart rate by cardiac conduction; ISS:BHF-UCL.
DR GO; GO:0098903; P:regulation of membrane repolarization during action potential; IMP:BHF-UCL.
DR GO; GO:0052547; P:regulation of peptidase activity; ISS:BHF-UCL.
DR GO; GO:1900027; P:regulation of ruffle assembly; IDA:AgBase.
DR GO; GO:0006940; P:regulation of smooth muscle contraction; ISS:BHF-UCL.
DR GO; GO:0003057; P:regulation of the force of heart contraction by chemical signal; IEA:Ensembl.
DR GO; GO:0098911; P:regulation of ventricular cardiac muscle cell action potential; ISS:BHF-UCL.
DR GO; GO:0009617; P:response to bacterium; IDA:AgBase.
DR GO; GO:0051592; P:response to calcium ion; ISS:BHF-UCL.
DR GO; GO:0043627; P:response to estrogen; IDA:MGI.
DR GO; GO:0001666; P:response to hypoxia; ISS:BHF-UCL.
DR GO; GO:0002931; P:response to ischemia; IEA:Ensembl.
DR GO; GO:0032570; P:response to progesterone; IDA:MGI.
DR GO; GO:0007519; P:skeletal muscle tissue development; ISS:BHF-UCL.
DR GO; GO:0031295; P:T cell costimulation; IDA:UniProtKB.
DR GO; GO:0006641; P:triglyceride metabolic process; ISS:BHF-UCL.
DR GO; GO:0007260; P:tyrosine phosphorylation of STAT protein; IEA:Ensembl.
DR GO; GO:0001570; P:vasculogenesis; ISS:BHF-UCL.
DR GO; GO:0042310; P:vasoconstriction; IEA:Ensembl.
DR GO; GO:0016050; P:vesicle organization; ISS:BHF-UCL.
DR InterPro; IPR015504; CAV-1.
DR InterPro; IPR001612; Caveolin.
DR InterPro; IPR018361; Caveolin_CS.
DR PANTHER; PTHR10844; PTHR10844; 1.
DR PANTHER; PTHR10844:SF18; PTHR10844:SF18; 1.
DR Pfam; PF01146; Caveolin; 1.
DR PROSITE; PS01210; CAVEOLIN; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative initiation; Cell membrane;
KW Congenital generalized lipodystrophy; Diabetes mellitus;
KW Direct protein sequencing; Disease variant; Golgi apparatus;
KW Host-virus interaction; Isopeptide bond; Lipoprotein; Membrane; Palmitate;
KW Phosphoprotein; Reference proteome; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:15219854,
FT ECO:0007744|PubMed:22814378"
FT CHAIN 2..178
FT /note="Caveolin-1"
FT /id="PRO_0000004764"
FT TOPO_DOM 2..104
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT INTRAMEM 105..125
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 126..178
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 2..94
FT /note="Required for homooligomerization"
FT /evidence="ECO:0000269|PubMed:25588833"
FT REGION 82..94
FT /note="Interaction with CAVIN3"
FT /evidence="ECO:0000269|PubMed:25588833"
FT REGION 131..142
FT /note="Interacts with SPRY1, SPRY2, SPRY3 and SPRY4"
FT /evidence="ECO:0000250|UniProtKB:P49817"
FT REGION 149..160
FT /note="Interacts with SPRY1, SPRY2, and SPRY4"
FT /evidence="ECO:0000250|UniProtKB:P49817"
FT REGION 167..178
FT /note="Interacts with SPRY1, SPRY2, SPRY3 and SPRY4"
FT /evidence="ECO:0000250|UniProtKB:P49817"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|PubMed:15219854,
FT ECO:0007744|PubMed:22814378"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P41350"
FT MOD_RES 5
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 6
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:8632005"
FT MOD_RES 9
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49817"
FT MOD_RES 14
FT /note="Phosphotyrosine; by ABL1"
FT /evidence="ECO:0000269|PubMed:12531427,
FT ECO:0000269|PubMed:8632005"
FT MOD_RES 25
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:8632005"
FT MOD_RES 37
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:15219854,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT LIPID 133
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 143
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 156
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT CROSSLNK 5
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin); alternate"
FT /evidence="ECO:0000269|PubMed:23335559"
FT CROSSLNK 26
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:23335559"
FT CROSSLNK 30
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:23335559"
FT CROSSLNK 39
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:23335559"
FT CROSSLNK 47
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:23335559"
FT CROSSLNK 57
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:23335559"
FT VAR_SEQ 1..31
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_018692"
FT VARIANT 132
FT /note="P -> L (in breast cancer; seems to form misfolded
FT oligomers that are retained within the Golgi complex and
FT are not targeted to caveolae or the plasma membrane; loss
FT of interaction with VCP; dbSNP:rs1213469537)"
FT /evidence="ECO:0000269|PubMed:12368209,
FT ECO:0000269|PubMed:21822278"
FT /id="VAR_015103"
FT CONFLICT 82
FT /note="D -> H (in Ref. 1; CAA79476)"
FT /evidence="ECO:0000305"
FT CONFLICT 144
FT /note="I -> T (in Ref. 1; CAA79476)"
FT /evidence="ECO:0000305"
FT INIT_MET Q03135-2:1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:15219854,
FT ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:22814378"
FT MOD_RES Q03135-2:2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|PubMed:15219854,
FT ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:22814378"
FT MOD_RES Q03135-2:6
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:15219854,
FT ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:20068231"
SQ SEQUENCE 178 AA; 20472 MW; 2424DE9B5E6521D5 CRC64;
MSGGKYVDSE GHLYTVPIRE QGNIYKPNNK AMADELSEKQ VYDAHTKEID LVNRDPKHLN
DDVVKIDFED VIAEPEGTHS FDGIWKASFT TFTVTKYWFY RLLSALFGIP MALIWGIYFA
ILSFLHIWAV VPCIKSFLIE IQCISRVYSI YVHTVCDPLF EAVGKIFSNV RINLQKEI
