CAV1_CANLF
ID CAV1_CANLF Reviewed; 178 AA.
AC P33724; A0M8U8;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 188.
DE RecName: Full=Caveolin-1;
DE AltName: Full=Vesicular integral-membrane protein VIP21;
GN Name=CAV1; Synonyms=CAV;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 48-74 AND
RP 166-176.
RC TISSUE=Epithelium;
RX PubMed=1512286; DOI=10.1083/jcb.118.5.1003;
RA Kurzchalia T.V., Dupree P., Parton R.G., Kellner R., Virta H., Lehnert M.,
RA Simons K.;
RT "VIP21, a 21-kD membrane protein is an integral component of trans-Golgi-
RT network-derived transport vesicles.";
RL J. Cell Biol. 118:1003-1014(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Cocker spaniel; TISSUE=Kidney;
RX PubMed=8349730; DOI=10.1083/jcb.122.4.789;
RA Sargiacomo M., Sudol M., Tang Z., Lisanti M.P.;
RT "Signal transducing molecules and glycosyl-phosphatidylinositol-linked
RT proteins form a caveolin-rich insoluble complex in MDCK cells.";
RL J. Cell Biol. 122:789-807(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12917688; DOI=10.1038/nature01858;
RA Thomas J.W., Touchman J.W., Blakesley R.W., Bouffard G.G.,
RA Beckstrom-Sternberg S.M., Margulies E.H., Blanchette M., Siepel A.C.,
RA Thomas P.J., McDowell J.C., Maskeri B., Hansen N.F., Schwartz M.S.,
RA Weber R.J., Kent W.J., Karolchik D., Bruen T.C., Bevan R., Cutler D.J.,
RA Schwartz S., Elnitski L., Idol J.R., Prasad A.B., Lee-Lin S.-Q.,
RA Maduro V.V.B., Summers T.J., Portnoy M.E., Dietrich N.L., Akhter N.,
RA Ayele K., Benjamin B., Cariaga K., Brinkley C.P., Brooks S.Y., Granite S.,
RA Guan X., Gupta J., Haghighi P., Ho S.-L., Huang M.C., Karlins E.,
RA Laric P.L., Legaspi R., Lim M.J., Maduro Q.L., Masiello C.A.,
RA Mastrian S.D., McCloskey J.C., Pearson R., Stantripop S., Tiongson E.E.,
RA Tran J.T., Tsurgeon C., Vogt J.L., Walker M.A., Wetherby K.D.,
RA Wiggins L.S., Young A.C., Zhang L.-H., Osoegawa K., Zhu B., Zhao B.,
RA Shu C.L., De Jong P.J., Lawrence C.E., Smit A.F., Chakravarti A.,
RA Haussler D., Green P., Miller W., Green E.D.;
RT "Comparative analyses of multi-species sequences from targeted genomic
RT regions.";
RL Nature 424:788-793(2003).
RN [4]
RP SUBCELLULAR LOCATION.
RX PubMed=8385608; DOI=10.1002/j.1460-2075.1993.tb05804.x;
RA Dupree P., Parton R.G., Raposo G., Kurzchalia T.V., Simons K.;
RT "Caveolae and sorting in the trans-Golgi network of epithelial cells.";
RL EMBO J. 12:1597-1605(1993).
RN [5]
RP SUBUNIT.
RX PubMed=7568142; DOI=10.1073/pnas.92.20.9407;
RA Sargiacomo M., Scherer P.E., Tang Z., Kubler E., Song K.S., Sanders M.C.,
RA Lisanti M.P.;
RT "Oligomeric structure of caveolin: implications for caveolae membrane
RT organization.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:9407-9411(1995).
RN [6]
RP PALMITOYLATION AT CYS-133; CYS-143 AND CYS-156.
RX PubMed=7896831; DOI=10.1074/jbc.270.12.6838;
RA Dietzen D.J., Hastings W.R., Lublin D.M.;
RT "Caveolin is palmitoylated on multiple cysteine residues. Palmitoylation is
RT not necessary for localization of caveolin to caveolae.";
RL J. Biol. Chem. 270:6838-6842(1995).
RN [7]
RP ALTERNATIVE INITIATION.
RX PubMed=7608210; DOI=10.1074/jbc.270.27.16395;
RA Scherer P.E., Tang Z., Chun M., Sargiacomo M., Lodish H.F., Lisanti M.P.;
RT "Caveolin isoforms differ in their N-terminal protein sequence and
RT subcellular distribution. Identification and epitope mapping of an isoform-
RT specific monoclonal antibody probe.";
RL J. Biol. Chem. 270:16395-16401(1995).
RN [8]
RP INTERACTION WITH CTNNB1; CDH1 AND JUP, AND SUBCELLULAR LOCATION.
RX PubMed=10816572; DOI=10.1074/jbc.m002020200;
RA Galbiati F., Volonte D., Brown A.M., Weinstein D.E., Ben-Ze'ev A.,
RA Pestell R.G., Lisanti M.P.;
RT "Caveolin-1 expression inhibits Wnt/beta-catenin/Lef-1 signaling by
RT recruiting beta-catenin to caveolae membrane domains.";
RL J. Biol. Chem. 275:23368-23377(2000).
CC -!- FUNCTION: May act as a scaffolding protein within caveolar membranes.
CC Forms a stable heterooligomeric complex with CAV2 that targets to lipid
CC rafts and drives caveolae formation. Mediates the recruitment of CAVIN
CC proteins (CAVIN1/2/3/4) to the caveolae (By similarity). Interacts
CC directly with G-protein alpha subunits and can functionally regulate
CC their activity (By similarity). Involved in the costimulatory signal
CC essential for T-cell receptor (TCR)-mediated T-cell activation. Its
CC binding to DPP4 induces T-cell proliferation and NF-kappa-B activation
CC in a T-cell receptor/CD3-dependent manner (By similarity). Recruits
CC CTNNB1 to caveolar membranes and may regulate CTNNB1-mediated signaling
CC through the Wnt pathway (By similarity). Negatively regulates TGFB1-
CC mediated activation of SMAD2/3 by mediating the internalization of
CC TGFBR1 from membrane rafts leading to its subsequent degradation (By
CC similarity). {ECO:0000250|UniProtKB:P49817,
CC ECO:0000250|UniProtKB:Q03135}.
CC -!- SUBUNIT: Homooligomer (PubMed:7568142). Interacts with BMX, BTK,
CC GLIPR2, NOSTRIN, SNAP25 and STX1A. Interacts with PACSIN2; this
CC interaction induces membrane tubulation (By similarity). Interacts (via
CC the N-terminus) with DPP4; the interaction is direct. Interacts with
CC SLC7A9 (By similarity). Interacts with CTNNB1, CDH1 and JUP
CC (PubMed:10816572). Interacts with TGFBR1. Interacts with CAVIN3 (via
CC leucine-zipper domain) in a cholesterol-sensitive manner. Interacts
CC with CAVIN1. Interacts with EHD2 in a cholesterol-dependent manner (By
CC similarity). Forms a ternary complex with UBXN6 and VCP; mediates CAV1
CC targeting to lysosomes for degradation (By similarity). Interacts with
CC ABCG1; this interaction regulates ABCG1-mediated cholesterol efflux (By
CC similarity). Interacts with NEU3; this interaction enhances NEU3
CC sialidase activity within caveola. Interacts (via C-terminus) with
CC SPRY1, SPRY2 (via C-terminus), SPRY3, and SPRY4 (By similarity).
CC {ECO:0000250|UniProtKB:P41350, ECO:0000250|UniProtKB:P49817,
CC ECO:0000250|UniProtKB:Q03135, ECO:0000250|UniProtKB:Q2IBA5,
CC ECO:0000269|PubMed:10816572, ECO:0000269|PubMed:7568142}.
CC -!- INTERACTION:
CC P33724; P59632: 3a; Xeno; NbExp=5; IntAct=EBI-79998, EBI-15595051;
CC P33724; P35222: CTNNB1; Xeno; NbExp=5; IntAct=EBI-79998, EBI-491549;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}. Cell membrane {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}. Membrane, caveola
CC {ECO:0000269|PubMed:10816572, ECO:0000269|PubMed:8385608}; Peripheral
CC membrane protein {ECO:0000250}. Membrane raft
CC {ECO:0000250|UniProtKB:Q03135}. Golgi apparatus, trans-Golgi network
CC {ECO:0000269|PubMed:8385608}. Note=Colocalized with DPP4 in membrane
CC rafts. Potential hairpin-like structure in the membrane. Membrane
CC protein of caveolae. {ECO:0000250|UniProtKB:P49817,
CC ECO:0000250|UniProtKB:Q03135}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=Alpha;
CC IsoId=P33724-1; Sequence=Displayed;
CC Name=Beta;
CC IsoId=P33724-2; Sequence=VSP_018691;
CC -!- PTM: Phosphorylation of isoform Beta on serine residues is
CC constitutive. Phosphorylated at Tyr-14 by ABL1 in response to oxidative
CC stress (By similarity). {ECO:0000250|UniProtKB:Q03135}.
CC -!- PTM: Ubiquitinated. Undergo monoubiquitination and multi- and/or
CC polyubiquitination. Monoubiquitination of N-terminal lysines promotes
CC integration in a ternary complex with UBXN6 and VCP which promotes
CC oligomeric CAV1 targeting to lysosomes for degradation.
CC {ECO:0000250|UniProtKB:Q03135}.
CC -!- SIMILARITY: Belongs to the caveolin family. {ECO:0000305}.
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DR EMBL; Z12161; CAA78151.1; -; Genomic_DNA.
DR EMBL; U47060; AAA87050.1; -; mRNA.
DR EMBL; DP000236; AAR16266.1; -; Genomic_DNA.
DR PIR; A43419; A43419.
DR RefSeq; NP_001003296.1; NM_001003296.1. [P33724-1]
DR RefSeq; XP_005628404.1; XM_005628347.2. [P33724-2]
DR RefSeq; XP_013974350.1; XM_014118875.1. [P33724-2]
DR AlphaFoldDB; P33724; -.
DR BioGRID; 139896; 3.
DR IntAct; P33724; 6.
DR MINT; P33724; -.
DR STRING; 9612.ENSCAFP00000005060; -.
DR iPTMnet; P33724; -.
DR SwissPalm; P33724; -.
DR PaxDb; P33724; -.
DR PRIDE; P33724; -.
DR Ensembl; ENSCAFT00000098661; ENSCAFP00000074453; ENSCAFG00000055058. [P33724-1]
DR Ensembl; ENSCAFT00030014054; ENSCAFP00030012265; ENSCAFG00030007606. [P33724-1]
DR Ensembl; ENSCAFT00040030547; ENSCAFP00040026553; ENSCAFG00040016536. [P33724-1]
DR Ensembl; ENSCAFT00845012174; ENSCAFP00845009515; ENSCAFG00845006847. [P33724-1]
DR GeneID; 403980; -.
DR KEGG; cfa:403980; -.
DR CTD; 857; -.
DR VEuPathDB; HostDB:ENSCAFG00845006847; -.
DR eggNOG; ENOG502QUK5; Eukaryota.
DR GeneTree; ENSGT00950000183006; -.
DR HOGENOM; CLU_102582_0_0_1; -.
DR InParanoid; P33724; -.
DR OMA; SIRINMQ; -.
DR OrthoDB; 1468974at2759; -.
DR TreeFam; TF315736; -.
DR Reactome; R-CFA-203641; NOSTRIN mediated eNOS trafficking.
DR Reactome; R-CFA-210991; Basigin interactions.
DR Reactome; R-CFA-4641262; Disassembly of the destruction complex and recruitment of AXIN to the membrane.
DR Reactome; R-CFA-8980692; RHOA GTPase cycle.
DR Reactome; R-CFA-9009391; Extra-nuclear estrogen signaling.
DR Reactome; R-CFA-9013026; RHOB GTPase cycle.
DR Reactome; R-CFA-9013106; RHOC GTPase cycle.
DR Reactome; R-CFA-9013148; CDC42 GTPase cycle.
DR Reactome; R-CFA-9013149; RAC1 GTPase cycle.
DR Reactome; R-CFA-9013404; RAC2 GTPase cycle.
DR Reactome; R-CFA-9013405; RHOD GTPase cycle.
DR Reactome; R-CFA-9013407; RHOH GTPase cycle.
DR Reactome; R-CFA-9013408; RHOG GTPase cycle.
DR Reactome; R-CFA-9013409; RHOJ GTPase cycle.
DR Reactome; R-CFA-9035034; RHOF GTPase cycle.
DR Reactome; R-CFA-9696264; RND3 GTPase cycle.
DR Reactome; R-CFA-9696270; RND2 GTPase cycle.
DR Reactome; R-CFA-9696273; RND1 GTPase cycle.
DR Proteomes; UP000002254; Chromosome 14.
DR Bgee; ENSCAFG00000003404; Expressed in adipose tissue and 46 other tissues.
DR GO; GO:0002080; C:acrosomal membrane; IEA:Ensembl.
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; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:Ensembl.
DR GO; GO:0005768; C:endosome; ISS:UniProtKB.
DR GO; GO:0070382; C:exocytic vesicle; IDA:CAFA.
DR GO; GO:0005925; C:focal adhesion; IEA:Ensembl.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IBA:GO_Central.
DR GO; GO:0051117; F:ATPase binding; IEA:Ensembl.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0070320; F:inward rectifier potassium channel inhibitor activity; IEA:Ensembl.
DR GO; GO:0060090; F:molecular adaptor activity; IBA:GO_Central.
DR GO; GO:0050998; F:nitric-oxide synthase binding; IEA:Ensembl.
DR GO; GO:0016504; F:peptidase activator activity; IEA:Ensembl.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:Ensembl.
DR GO; GO:0019901; F:protein kinase binding; IBA:GO_Central.
DR GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IEA:Ensembl.
DR GO; GO:0005102; F:signaling receptor binding; IEA:Ensembl.
DR GO; GO:0031267; F:small GTPase binding; IEA:Ensembl.
DR GO; GO:0044325; F:transmembrane transporter binding; IBA:GO_Central.
DR GO; GO:0001525; P:angiogenesis; IEA:Ensembl.
DR GO; GO:0086098; P:angiotensin-activated signaling pathway involved in heart process; IEA:Ensembl.
DR GO; GO:0097190; P:apoptotic signaling pathway; IEA:Ensembl.
DR GO; GO:0071711; P:basement membrane organization; IEA:Ensembl.
DR GO; GO:0006816; P:calcium ion transport; IEA:Ensembl.
DR GO; GO:0070836; P:caveola assembly; IDA:BHF-UCL.
DR GO; GO:0072584; P:caveolin-mediated endocytosis; IEA:Ensembl.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0071360; P:cellular response to exogenous dsRNA; IEA:Ensembl.
DR GO; GO:0071455; P:cellular response to hyperoxia; IEA:Ensembl.
DR GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; IEA:Ensembl.
DR GO; GO:0042632; P:cholesterol homeostasis; IEA:Ensembl.
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; IEA:Ensembl.
DR GO; GO:0060056; P:mammary gland involution; IEA:Ensembl.
DR GO; GO:0000165; P:MAPK cascade; IEA:Ensembl.
DR GO; GO:0051899; P:membrane depolarization; IEA:Ensembl.
DR GO; GO:0046716; P:muscle cell cellular homeostasis; IEA:Ensembl.
DR GO; GO:2000811; P:negative regulation of anoikis; IEA:Ensembl.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IEA:Ensembl.
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; IBA:GO_Central.
DR GO; GO:0030857; P:negative regulation of epithelial cell differentiation; IEA:Ensembl.
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; IEA:Ensembl.
DR GO; GO:0043407; P:negative regulation of MAP kinase activity; IEA:Ensembl.
DR GO; GO:0060546; P:negative regulation of necroptotic process; IEA:Ensembl.
DR GO; GO:0045019; P:negative regulation of nitric oxide biosynthetic process; IEA:Ensembl.
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; IEA:Ensembl.
DR GO; GO:1900085; P:negative regulation of peptidyl-tyrosine autophosphorylation; IEA:Ensembl.
DR GO; GO:0048550; P:negative regulation of pinocytosis; IEA:Ensembl.
DR GO; GO:0032091; P:negative regulation of protein binding; IEA:Ensembl.
DR GO; GO:0061099; P:negative regulation of protein tyrosine kinase activity; IBA:GO_Central.
DR GO; GO:0031397; P:negative regulation of protein ubiquitination; IEA:Ensembl.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; ISS: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; IEA:Ensembl.
DR GO; GO:0010524; P:positive regulation of calcium ion transport into cytosol; IEA:Ensembl.
DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; IEA:Ensembl.
DR GO; GO:0060355; P:positive regulation of cell adhesion molecule production; IEA:Ensembl.
DR GO; GO:0030335; P:positive regulation of cell migration; IEA:Ensembl.
DR GO; GO:0010875; P:positive regulation of cholesterol efflux; IEA:Ensembl.
DR GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; IEA:Ensembl.
DR GO; GO:1903071; P:positive regulation of ER-associated ubiquitin-dependent protein catabolic process; IEA:Ensembl.
DR GO; GO:2001238; P:positive regulation of extrinsic apoptotic signaling pathway; IEA:Ensembl.
DR GO; GO:1903598; P:positive regulation of gap junction assembly; IEA:Ensembl.
DR GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
DR GO; GO:2001244; P:positive regulation of intrinsic apoptotic signaling pathway; IEA:Ensembl.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IEA:Ensembl.
DR GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; IEA:Ensembl.
DR GO; GO:0032092; P:positive regulation of protein binding; IEA:Ensembl.
DR GO; GO:0031398; P:positive regulation of protein ubiquitination; IEA:Ensembl.
DR GO; GO:0034141; P:positive regulation of toll-like receptor 3 signaling pathway; IEA:Ensembl.
DR GO; GO:0045907; P:positive regulation of vasoconstriction; IEA:Ensembl.
DR GO; GO:0010608; P:post-transcriptional regulation of gene expression; IEA:Ensembl.
DR GO; GO:1903361; P:protein localization to basolateral plasma membrane; IDA:BHF-UCL.
DR GO; GO:0044860; P:protein localization to plasma membrane raft; IDA:BHF-UCL.
DR GO; GO:0015031; P:protein transport; IEA:Ensembl.
DR GO; GO:0031623; P:receptor internalization; ISS:UniProtKB.
DR GO; GO:2000286; P:receptor internalization involved in canonical Wnt signaling pathway; IEA:Ensembl.
DR GO; GO:0019065; P:receptor-mediated endocytosis of virus by host cell; IEA:Ensembl.
DR GO; GO:0030193; P:regulation of blood coagulation; IEA:Ensembl.
DR GO; GO:1901844; P:regulation of cell communication by electrical coupling involved in cardiac conduction; IEA:Ensembl.
DR GO; GO:0051480; P:regulation of cytosolic calcium ion concentration; IBA:GO_Central.
DR GO; GO:2000535; P:regulation of entry of bacterium into host cell; IEA:Ensembl.
DR GO; GO:0019217; P:regulation of fatty acid metabolic process; IEA:Ensembl.
DR GO; GO:0086091; P:regulation of heart rate by cardiac conduction; IEA:Ensembl.
DR GO; GO:0098903; P:regulation of membrane repolarization during action potential; IEA:Ensembl.
DR GO; GO:1900027; P:regulation of ruffle assembly; IEA:Ensembl.
DR GO; GO:0006940; P:regulation of smooth muscle contraction; IEA:Ensembl.
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; IEA:Ensembl.
DR GO; GO:0009617; P:response to bacterium; IEA:Ensembl.
DR GO; GO:0051592; P:response to calcium ion; IEA:Ensembl.
DR GO; GO:0043627; P:response to estrogen; IEA:Ensembl.
DR GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
DR GO; GO:0002931; P:response to ischemia; IEA:Ensembl.
DR GO; GO:0032570; P:response to progesterone; IEA:Ensembl.
DR GO; GO:0007519; P:skeletal muscle tissue development; IEA:Ensembl.
DR GO; GO:0031295; P:T cell costimulation; ISS:UniProtKB.
DR GO; GO:0006641; P:triglyceride metabolic process; IEA:Ensembl.
DR GO; GO:0007260; P:tyrosine phosphorylation of STAT protein; IEA:Ensembl.
DR GO; GO:0001570; P:vasculogenesis; IEA:Ensembl.
DR GO; GO:0042310; P:vasoconstriction; IEA:Ensembl.
DR GO; GO:0016050; P:vesicle organization; IDA: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 Direct protein sequencing; Golgi apparatus; Isopeptide bond; Lipoprotein;
KW Membrane; Palmitate; Phosphoprotein; Reference proteome; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q03135"
FT CHAIN 2..178
FT /note="Caveolin-1"
FT /id="PRO_0000004762"
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:0000250|UniProtKB:Q03135"
FT REGION 82..94
FT /note="Interaction with CAVIN3"
FT /evidence="ECO:0000250|UniProtKB:Q03135"
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:0000250|UniProtKB:Q03135"
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:0000250|UniProtKB:Q03135"
FT MOD_RES 6
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q03135"
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:0000250|UniProtKB:P49817"
FT MOD_RES 25
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q03135"
FT MOD_RES 37
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q03135"
FT LIPID 133
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000269|PubMed:7896831"
FT LIPID 143
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000269|PubMed:7896831"
FT LIPID 156
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000269|PubMed:7896831"
FT CROSSLNK 5
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q03135"
FT CROSSLNK 26
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q03135"
FT CROSSLNK 30
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q03135"
FT CROSSLNK 39
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q03135"
FT CROSSLNK 47
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q03135"
FT CROSSLNK 57
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q03135"
FT VAR_SEQ 1..31
FT /note="Missing (in isoform Beta)"
FT /evidence="ECO:0000305"
FT /id="VSP_018691"
SQ SEQUENCE 178 AA; 20606 MW; DD77CE4D436E508D CRC64;
MSGGKYVDSE GHLYTVPIRE QGNIYKPNNK AMAEEMSEKQ VYDAHTKEID LVNRDPKHLN
DDVVKIDFED VIAEPEGTHS FDGIWKASFT TFTVTKYWFY RLLSALFGIP MALIWGIYFA
ILSFLHIWAV VPCIKSFLIE IQCISRVYSI YVHTFCDPFF EAVGKIFSNI RINMQKET