CAV1_ECHTE
ID CAV1_ECHTE Reviewed; 178 AA.
AC A1X149;
DT 06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 25-MAY-2022, entry version 98.
DE RecName: Full=Caveolin-1;
GN Name=CAV1;
OS Echinops telfairi (Lesser hedgehog tenrec).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Afrotheria; Tenrecidae; Tenrecinae; Echinops.
OX NCBI_TaxID=9371;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Antonellis A., Ayele K., Benjamin B., Blakesley R.W., Boakye A.,
RA Bouffard G.G., Brinkley C., Brooks S., Chu G., Coleman H., Engle J.,
RA Gestole M., Greene A., Guan X., Gupta J., Haghighi P., Han J., Hansen N.,
RA Ho S.-L., Hu P., Hunter G., Hurle B., Idol J.R., Kwong P., Laric P.,
RA Larson S., Lee-Lin S.-Q., Legaspi R., Madden M., Maduro Q.L., Maduro V.B.,
RA Margulies E.H., Masiello C., Maskeri B., McDowell J., Mojidi H.A.,
RA Mullikin J.C., Oestreicher J.S., Park M., Portnoy M.E., Prasad A., Puri O.,
RA Reddix-Dugue N., Schandler K., Schueler M.G., Sison C., Stantripop S.,
RA Stephen E., Taye A., Thomas J.W., Thomas P.J., Tsipouri V., Ung L.,
RA Vogt J.L., Wetherby K.D., Young A., Green E.D.;
RT "NISC comparative sequencing initiative.";
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
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,
CC NOSTRIN, SNAP25 and STX1A. Interacts with SLC7A9. Interacts with
CC 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. Forms a ternary complex with
CC UBXN6 and VCP; mediates CAV1 targeting to lysosomes for degradation.
CC Interacts with ABCG1; this interaction regulates ABCG1-mediated
CC cholesterol efflux (By similarity). Interacts with NEU3; this
CC interaction enhances NEU3 sialidase activity within caveola. Interacts
CC (via C-terminus) with SPRY1, SPRY2 (via C-terminus), SPRY3, and SPRY4
CC (By similarity). {ECO:0000250|UniProtKB:P41350,
CC ECO:0000250|UniProtKB:P49817, ECO:0000250|UniProtKB:Q03135,
CC ECO:0000250|UniProtKB:Q2IBA5}.
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: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 (By
CC similarity). {ECO:0000250}.
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}.
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DR EMBL; DP000274; ABL76165.1; -; Genomic_DNA.
DR AlphaFoldDB; A1X149; -.
DR HOGENOM; CLU_102582_0_0_1; -.
DR OMA; SIRINMQ; -.
DR TreeFam; TF315736; -.
DR GO; GO:0005901; C:caveola; ISS:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:Ensembl.
DR GO; GO:0005768; C:endosome; ISS:UniProtKB.
DR GO; GO:0005925; C:focal adhesion; IEA:Ensembl.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0045121; C:membrane raft; ISS:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR GO; GO:0032991; C:protein-containing complex; IEA:Ensembl.
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:0050998; F:nitric-oxide synthase binding; IEA:Ensembl.
DR GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
DR GO; GO:0044877; F:protein-containing complex binding; 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; IEA:Ensembl.
DR GO; GO:0097190; P:apoptotic signaling pathway; IEA:Ensembl.
DR GO; GO:0070836; P:caveola assembly; IEA:Ensembl.
DR GO; GO:0072584; P:caveolin-mediated endocytosis; IEA:Ensembl.
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:2000811; P:negative regulation of anoikis; IEA:Ensembl.
DR GO; GO:1903609; P:negative regulation of inward rectifier potassium channel 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; IEA:Ensembl.
DR GO; GO:0031397; P:negative regulation of protein ubiquitination; IEA:Ensembl.
DR GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; ISS:UniProtKB.
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: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: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: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:0051480; P:regulation of cytosolic calcium ion concentration; IEA:Ensembl.
DR GO; GO:2000535; P:regulation of entry of bacterium into host cell; 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:0009617; P:response to bacterium; IEA:Ensembl.
DR GO; GO:0043627; P:response to estrogen; IEA:Ensembl.
DR GO; GO:0032570; P:response to progesterone; IEA:Ensembl.
DR GO; GO:0031295; P:T cell costimulation; ISS:UniProtKB.
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 3: Inferred from homology;
KW Acetylation; Cell membrane; Golgi apparatus; Isopeptide bond; Lipoprotein;
KW Membrane; Palmitate; Phosphoprotein; 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_0000279728"
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 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"
SQ SEQUENCE 178 AA; 20540 MW; DAEBB7EE1D4B422F CRC64;
MSGGKYVDSE GHLYTLPIRE QGNIYKPNNK AMAEDMNEKQ VYDAHTKEID LVNRDPKHLN
DDVVKIDFED VIAEPEGTHS FDGIWKASFT TFTVTKYWFY RLLSGIFGIP MALIWGVYFA
ILSFLHIWAV VPCIKSFLIE IQCISRVYSI YVHTFCDPLF EAIGKIFSNI RISTQKEI
