CAV1_RAT
ID CAV1_RAT Reviewed; 178 AA.
AC P41350; Q8VIK8; Q8VIK9;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 3.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=Caveolin-1;
GN Name=Cav1; Synonyms=Cav;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Adipose tissue;
RA Vinten J., Voldstedlund M., Carlsen J., Christiansen K., Clausen H.,
RA Tranum-Jensen J.;
RT "Immuno-electronmicroscopical identification of caveolin in rat adipocyte
RT plasma membranes.";
RL Submitted (NOV-1994) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), TISSUE SPECIFICITY, AND
RP INTERACTION WITH SNAP25 AND SYNTAXIN.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RX PubMed=11883949; DOI=10.1006/bbrc.2002.6603;
RA Magga J.M., Kay J.G., Davy A., Poulton N.P., Robbins S.M., Braun J.E.A.;
RT "ATP dependence of the SNARE/caveolin 1 interaction in the hippocampus.";
RL Biochem. Biophys. Res. Commun. 291:1232-1238(2002).
RN [3]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INTERACTION WITH SLC7A9.
RX PubMed=16358225;
RA Kwak J.O., Kim H.W., Jung S.M., Song J.H., Hong S.B., Oh K.J., Ko C.B.,
RA Cha S.H.;
RT "Co-localization and interaction of b0,+-type amino acid transporter 1
RT (BAT1) with caveolin-1 in rat kidney.";
RL J. Nephrol. 18:681-689(2005).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2 AND SER-9, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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. Interacts (via the N-terminus) with DPP4; the
CC interaction is direct. Forms a stable heterooligomeric complex with
CC CAV2 that targets to lipid rafts and drives caveolae formation.
CC Interacts with PACSIN2; this interaction induces membrane tubulation
CC (By similarity). Interacts with BMX, BTK, CTNNB1, CDH1, GLIPR2, JUP and
CC NOSTRIN (By similarity). Interacts with SNAP25 and STX1A
CC (PubMed:11883949). Interacts with SLC7A9 (PubMed:16358225). Interacts
CC with TGFBR1. Interacts with CAVIN3 (via leucine-zipper domain) in a
CC cholesterol-sensitive manner. Interacts with CAVIN1. Interacts with
CC EHD2 in a cholesterol-dependent manner (By similarity). Forms a ternary
CC complex with UBXN6 and VCP; mediates CAV1 targeting to lysosomes for
CC degradation (By similarity). Interacts with ABCG1; this interaction
CC regulates ABCG1-mediated cholesterol efflux (By similarity). Interacts
CC with NEU3; this interaction enhances NEU3 sialidase activity within
CC caveola. Interacts (via C-terminus) with SPRY1, SPRY2 (via C-terminus),
CC SPRY3, and SPRY4 (By similarity). {ECO:0000250|UniProtKB:P49817,
CC ECO:0000250|UniProtKB:Q03135, ECO:0000250|UniProtKB:Q2IBA5,
CC ECO:0000269|PubMed:11883949, ECO:0000269|PubMed:16358225}.
CC -!- INTERACTION:
CC P41350-2; P41350-1: Cav1; NbExp=3; IntAct=EBI-1161031, EBI-1161028;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}. Cell membrane
CC {ECO:0000269|PubMed:16358225}; Peripheral membrane protein
CC {ECO:0000269|PubMed:16358225}. Membrane, caveola
CC {ECO:0000250|UniProtKB:P49817}; Peripheral membrane protein
CC {ECO:0000250}. Membrane raft {ECO:0000250|UniProtKB:Q03135}.
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=P41350-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P41350-2; Sequence=VSP_018694;
CC -!- TISSUE SPECIFICITY: Cortex and inner medulla of kidney (at protein
CC level). Expressed in the hippocampus. {ECO:0000269|PubMed:11883949,
CC ECO:0000269|PubMed:16358225}.
CC -!- PTM: Phosphorylated at Tyr-14 by ABL1 in response to oxidative stress.
CC {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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA86587.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; Z46614; CAA86587.1; ALT_FRAME; mRNA.
DR EMBL; AF439778; AAL33579.1; -; mRNA.
DR EMBL; AF439779; AAL33580.1; -; mRNA.
DR AlphaFoldDB; P41350; -.
DR CORUM; P41350; -.
DR IntAct; P41350; 7.
DR MINT; P41350; -.
DR STRING; 10116.ENSRNOP00000009253; -.
DR iPTMnet; P41350; -.
DR PhosphoSitePlus; P41350; -.
DR jPOST; P41350; -.
DR PaxDb; P41350; -.
DR PRIDE; P41350; -.
DR UCSC; RGD:2280; rat. [P41350-1]
DR RGD; 2280; Cav1.
DR eggNOG; ENOG502QUK5; Eukaryota.
DR InParanoid; P41350; -.
DR PhylomeDB; P41350; -.
DR Reactome; R-RNO-203615; eNOS activation.
DR Reactome; R-RNO-203641; NOSTRIN mediated eNOS trafficking.
DR Reactome; R-RNO-210991; Basigin interactions.
DR Reactome; R-RNO-4641262; Disassembly of the destruction complex and recruitment of AXIN to the membrane.
DR Reactome; R-RNO-5218920; VEGFR2 mediated vascular permeability.
DR Reactome; R-RNO-8980692; RHOA GTPase cycle.
DR Reactome; R-RNO-9009391; Extra-nuclear estrogen signaling.
DR Reactome; R-RNO-9013026; RHOB GTPase cycle.
DR Reactome; R-RNO-9013106; RHOC GTPase cycle.
DR Reactome; R-RNO-9013148; CDC42 GTPase cycle.
DR Reactome; R-RNO-9013149; RAC1 GTPase cycle.
DR Reactome; R-RNO-9013404; RAC2 GTPase cycle.
DR Reactome; R-RNO-9013405; RHOD GTPase cycle.
DR Reactome; R-RNO-9013406; RHOQ GTPase cycle.
DR Reactome; R-RNO-9013407; RHOH GTPase cycle.
DR Reactome; R-RNO-9013408; RHOG GTPase cycle.
DR Reactome; R-RNO-9013409; RHOJ GTPase cycle.
DR Reactome; R-RNO-9013423; RAC3 GTPase cycle.
DR Reactome; R-RNO-9035034; RHOF GTPase cycle.
DR Reactome; R-RNO-9696264; RND3 GTPase cycle.
DR Reactome; R-RNO-9696270; RND2 GTPase cycle.
DR Reactome; R-RNO-9696273; RND1 GTPase cycle.
DR PRO; PR:P41350; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0002080; C:acrosomal membrane; ISO:RGD.
DR GO; GO:0009925; C:basal plasma membrane; IDA:RGD.
DR GO; GO:0005901; C:caveola; IDA:UniProtKB.
DR GO; GO:0002095; C:caveolar macromolecular signaling complex; ISO:RGD.
DR GO; GO:0005938; C:cell cortex; ISO:RGD.
DR GO; GO:0009986; C:cell surface; IDA:RGD.
DR GO; GO:0005929; C:cilium; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:RGD.
DR GO; GO:0005829; C:cytosol; IDA:RGD.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:HGNC-UCL.
DR GO; GO:0005768; C:endosome; ISS:UniProtKB.
DR GO; GO:0005925; C:focal adhesion; IDA:RGD.
DR GO; GO:0005794; C:Golgi apparatus; IDA:BHF-UCL.
DR GO; GO:0000139; C:Golgi membrane; ISS:HGNC-UCL.
DR GO; GO:0016021; C:integral component of membrane; ISO:RGD.
DR GO; GO:0005887; C:integral component of plasma membrane; ISO:RGD.
DR GO; GO:0005811; C:lipid droplet; IDA:RGD.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0045121; C:membrane raft; IDA:BHF-UCL.
DR GO; GO:0005739; C:mitochondrion; IDA:RGD.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0005778; C:peroxisomal membrane; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IDA:RGD.
DR GO; GO:0051117; F:ATPase binding; ISO:RGD.
DR GO; GO:0019899; F:enzyme binding; ISO:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0070320; F:inward rectifier potassium channel inhibitor activity; ISO:RGD.
DR GO; GO:0019900; F:kinase binding; IPI:RGD.
DR GO; GO:0060090; F:molecular adaptor activity; ISO:RGD.
DR GO; GO:0050998; F:nitric-oxide synthase binding; IPI:RGD.
DR GO; GO:0016504; F:peptidase activator activity; ISO:RGD.
DR GO; GO:0046982; F:protein heterodimerization activity; ISO:RGD.
DR GO; GO:0019901; F:protein kinase binding; ISO:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:RGD.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; ISO:RGD.
DR GO; GO:0033612; F:receptor serine/threonine kinase binding; IPI:RGD.
DR GO; GO:0005102; F:signaling receptor binding; ISO:RGD.
DR GO; GO:0031267; F:small GTPase binding; ISO:RGD.
DR GO; GO:0000149; F:SNARE binding; IMP:RGD.
DR GO; GO:0019905; F:syntaxin binding; IMP:RGD.
DR GO; GO:0044325; F:transmembrane transporter binding; IPI:BHF-UCL.
DR GO; GO:0001525; P:angiogenesis; ISO:RGD.
DR GO; GO:0086098; P:angiotensin-activated signaling pathway involved in heart process; ISO:RGD.
DR GO; GO:0031100; P:animal organ regeneration; IEP:RGD.
DR GO; GO:0097190; P:apoptotic signaling pathway; ISO:RGD.
DR GO; GO:0071711; P:basement membrane organization; ISO:RGD.
DR GO; GO:0055074; P:calcium ion homeostasis; ISO:RGD.
DR GO; GO:0006816; P:calcium ion transport; ISO:RGD.
DR GO; GO:0070836; P:caveola assembly; ISO:RGD.
DR GO; GO:0072584; P:caveolin-mediated endocytosis; ISO:RGD.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; IMP:RGD.
DR GO; GO:0071360; P:cellular response to exogenous dsRNA; ISO:RGD.
DR GO; GO:0071455; P:cellular response to hyperoxia; ISO:RGD.
DR GO; GO:0071456; P:cellular response to hypoxia; IEP:RGD.
DR GO; GO:0071260; P:cellular response to mechanical stimulus; IDA:RGD.
DR GO; GO:0071375; P:cellular response to peptide hormone stimulus; ISO:RGD.
DR GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; ISO:RGD.
DR GO; GO:0090398; P:cellular senescence; IMP:RGD.
DR GO; GO:0033344; P:cholesterol efflux; IMP:RGD.
DR GO; GO:0042632; P:cholesterol homeostasis; ISO:RGD.
DR GO; GO:0038016; P:insulin receptor internalization; ISO:RGD.
DR GO; GO:0007595; P:lactation; ISO:RGD.
DR GO; GO:0019915; P:lipid storage; ISO:RGD.
DR GO; GO:0032507; P:maintenance of protein location in cell; IMP:BHF-UCL.
DR GO; GO:0030879; P:mammary gland development; ISO:RGD.
DR GO; GO:0060056; P:mammary gland involution; ISO:RGD.
DR GO; GO:0051899; P:membrane depolarization; ISO:RGD.
DR GO; GO:0046785; P:microtubule polymerization; IMP:RGD.
DR GO; GO:2000811; P:negative regulation of anoikis; ISO:RGD.
DR GO; GO:1905949; P:negative regulation of calcium ion import across plasma membrane; IMP:RGD.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; ISS:UniProtKB.
DR GO; GO:2001258; P:negative regulation of cation channel activity; IDA:RGD.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISO:RGD.
DR GO; GO:0001960; P:negative regulation of cytokine-mediated signaling pathway; ISO:RGD.
DR GO; GO:0001937; P:negative regulation of endothelial cell proliferation; IMP:RGD.
DR GO; GO:0030857; P:negative regulation of epithelial cell differentiation; ISO:RGD.
DR GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; IDA:RGD.
DR GO; GO:1903609; P:negative regulation of inward rectifier potassium channel activity; ISO:RGD.
DR GO; GO:0043407; P:negative regulation of MAP kinase activity; ISO:RGD.
DR GO; GO:0043409; P:negative regulation of MAPK cascade; ISO:RGD.
DR GO; GO:0010656; P:negative regulation of muscle cell apoptotic process; IMP:RGD.
DR GO; GO:0060546; P:negative regulation of necroptotic process; ISO:RGD.
DR GO; GO:0045665; P:negative regulation of neuron differentiation; IMP:RGD.
DR GO; GO:0045019; P:negative regulation of nitric oxide biosynthetic process; ISO:RGD.
DR GO; GO:0051001; P:negative regulation of nitric-oxide synthase activity; ISO:RGD.
DR GO; GO:0033137; P:negative regulation of peptidyl-serine phosphorylation; ISO:RGD.
DR GO; GO:1900085; P:negative regulation of peptidyl-tyrosine autophosphorylation; ISO:RGD.
DR GO; GO:0048550; P:negative regulation of pinocytosis; ISO:RGD.
DR GO; GO:1901380; P:negative regulation of potassium ion transmembrane transport; ISO:RGD.
DR GO; GO:0032091; P:negative regulation of protein binding; ISO:RGD.
DR GO; GO:0061099; P:negative regulation of protein tyrosine kinase activity; ISO:RGD.
DR GO; GO:0031397; P:negative regulation of protein ubiquitination; ISO:RGD.
DR GO; GO:0046426; P:negative regulation of receptor signaling pathway via JAK-STAT; ISO:RGD.
DR GO; GO:0009968; P:negative regulation of signal transduction; ISO:RGD.
DR GO; GO:0014912; P:negative regulation of smooth muscle cell migration; IMP:RGD.
DR GO; GO:0048662; P:negative regulation of smooth muscle cell proliferation; IMP:RGD.
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; ISS:UniProtKB.
DR GO; GO:0042532; P:negative regulation of tyrosine phosphorylation of STAT protein; ISO:RGD.
DR GO; GO:1904706; P:negative regulation of vascular associated smooth muscle cell proliferation; IMP:RGD.
DR GO; GO:0033484; P:nitric oxide homeostasis; ISO:RGD.
DR GO; GO:0010524; P:positive regulation of calcium ion transport into cytosol; ISO:RGD.
DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; ISO:RGD.
DR GO; GO:0043085; P:positive regulation of catalytic activity; ISO:RGD.
DR GO; GO:0060355; P:positive regulation of cell adhesion molecule production; ISO:RGD.
DR GO; GO:0030335; P:positive regulation of cell migration; ISO:RGD.
DR GO; GO:0010875; P:positive regulation of cholesterol efflux; ISO:RGD.
DR GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; ISS:YuBioLab.
DR GO; GO:0045807; P:positive regulation of endocytosis; IMP:RGD.
DR GO; GO:0001938; P:positive regulation of endothelial cell proliferation; IMP:RGD.
DR GO; GO:1903071; P:positive regulation of ER-associated ubiquitin-dependent protein catabolic process; ISO:RGD.
DR GO; GO:2001238; P:positive regulation of extrinsic apoptotic signaling pathway; ISO:RGD.
DR GO; GO:1903598; P:positive regulation of gap junction assembly; ISO:RGD.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:RGD.
DR GO; GO:2001244; P:positive regulation of intrinsic apoptotic signaling pathway; ISO:RGD.
DR GO; GO:0031116; P:positive regulation of microtubule polymerization; IMP:RGD.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; ISO:RGD.
DR GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; ISO:RGD.
DR GO; GO:0032092; P:positive regulation of protein binding; ISO:RGD.
DR GO; GO:0031398; P:positive regulation of protein ubiquitination; ISO:RGD.
DR GO; GO:0009967; P:positive regulation of signal transduction; IMP:RGD.
DR GO; GO:0034141; P:positive regulation of toll-like receptor 3 signaling pathway; ISO:RGD.
DR GO; GO:0045907; P:positive regulation of vasoconstriction; IMP:RGD.
DR GO; GO:0010608; P:post-transcriptional regulation of gene expression; ISO:RGD.
DR GO; GO:0008104; P:protein localization; ISO:RGD.
DR GO; GO:0015031; P:protein transport; ISO:RGD.
DR GO; GO:0031623; P:receptor internalization; ISS:UniProtKB.
DR GO; GO:2000286; P:receptor internalization involved in canonical Wnt signaling pathway; ISO:RGD.
DR GO; GO:0019065; P:receptor-mediated endocytosis of virus by host cell; ISO:RGD.
DR GO; GO:0030193; P:regulation of blood coagulation; ISO:RGD.
DR GO; GO:1901844; P:regulation of cell communication by electrical coupling involved in cardiac conduction; ISO:RGD.
DR GO; GO:0051480; P:regulation of cytosolic calcium ion concentration; ISO:RGD.
DR GO; GO:2000535; P:regulation of entry of bacterium into host cell; ISO:RGD.
DR GO; GO:0019217; P:regulation of fatty acid metabolic process; ISO:RGD.
DR GO; GO:0086091; P:regulation of heart rate by cardiac conduction; ISO:RGD.
DR GO; GO:0098903; P:regulation of membrane repolarization during action potential; ISO:RGD.
DR GO; GO:0052547; P:regulation of peptidase activity; ISO:RGD.
DR GO; GO:1900027; P:regulation of ruffle assembly; ISO:RGD.
DR GO; GO:0006940; P:regulation of smooth muscle contraction; ISO:RGD.
DR GO; GO:0002026; P:regulation of the force of heart contraction; ISO:RGD.
DR GO; GO:0003057; P:regulation of the force of heart contraction by chemical signal; ISO:RGD.
DR GO; GO:0098911; P:regulation of ventricular cardiac muscle cell action potential; ISO:RGD.
DR GO; GO:0009617; P:response to bacterium; ISO:RGD.
DR GO; GO:0051592; P:response to calcium ion; ISO:RGD.
DR GO; GO:0043627; P:response to estrogen; ISO:RGD.
DR GO; GO:0010332; P:response to gamma radiation; IEP:RGD.
DR GO; GO:0051384; P:response to glucocorticoid; IEP:RGD.
DR GO; GO:0001666; P:response to hypoxia; ISO:RGD.
DR GO; GO:0002931; P:response to ischemia; ISO:RGD.
DR GO; GO:0009612; P:response to mechanical stimulus; IMP:RGD.
DR GO; GO:0007584; P:response to nutrient; IEP:RGD.
DR GO; GO:0032570; P:response to progesterone; ISO:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
DR GO; GO:0007519; P:skeletal muscle tissue development; ISO:RGD.
DR GO; GO:0031295; P:T cell costimulation; ISS:UniProtKB.
DR GO; GO:0006641; P:triglyceride metabolic process; ISO:RGD.
DR GO; GO:0001570; P:vasculogenesis; ISO:RGD.
DR GO; GO:0042310; P:vasoconstriction; ISO:RGD.
DR GO; GO:0042060; P:wound healing; IMP:RGD.
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; Golgi apparatus;
KW Isopeptide bond; Lipoprotein; Membrane; Palmitate; Phosphoprotein;
KW 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_0000004768"
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:0007744|PubMed:22673903"
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:0007744|PubMed:22673903"
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 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: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 2)"
FT /evidence="ECO:0000303|PubMed:11883949"
FT /id="VSP_018694"
FT CONFLICT 120
FT /note="A -> G (in Ref. 1; CAA86587)"
FT /evidence="ECO:0000305"
FT CONFLICT 154
FT /note="T -> N (in Ref. 1; CAA86587)"
FT /evidence="ECO:0000305"
FT CONFLICT 162
FT /note="A -> G (in Ref. 1; CAA86587)"
FT /evidence="ECO:0000305"
FT CONFLICT 171
FT /note="R -> P (in Ref. 1; CAA86587)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 178 AA; 20553 MW; 55E8F6ABC7514FD2 CRC64;
MSGGKYVDSE GHLYTVPIRE QGNIYKPNNK AMADEVNEKQ VYDAHTKEID LVNRDPKHLN
DDVVKIDFED VIAEPEGTHS FDGIWKASFT TFTVTKYWFY RLLSTIFGIP MALIWGIYFA
ILSFLHIWAV VPCIKSFLIE IQCISRVYSI YVHTFCDPLF EAIGKIFSNI RISTQEEI
