CAV1_EULMM
ID CAV1_EULMM Reviewed; 179 AA.
AC Q2IBG8;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 1.
DT 25-MAY-2022, entry version 61.
DE RecName: Full=Caveolin-1;
GN Name=CAV1;
OS Eulemur macaco macaco (Black lemur).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Strepsirrhini; Lemuriformes;
OC Lemuridae; Eulemur.
OX NCBI_TaxID=30603;
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 (NOV-2005) 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; DP000024; ABC87434.1; -; Genomic_DNA.
DR AlphaFoldDB; Q2IBG8; -.
DR GO; GO:0005901; C:caveola; ISS:UniProtKB.
DR GO; GO:0005768; C:endosome; ISS:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0045121; C:membrane raft; ISS:UniProtKB.
DR GO; GO:0070836; P:caveola assembly; IEA:InterPro.
DR GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0031623; P:receptor internalization; ISS:UniProtKB.
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..179
FT /note="Caveolin-1"
FT /id="PRO_0000251904"
FT TOPO_DOM 2..105
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT INTRAMEM 106..126
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 127..179
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 2..95
FT /note="Required for homooligomerization"
FT /evidence="ECO:0000250|UniProtKB:Q03135"
FT REGION 83..95
FT /note="Interaction with CAVIN3"
FT /evidence="ECO:0000250|UniProtKB:Q03135"
FT REGION 132..143
FT /note="Interacts with SPRY1, SPRY2, SPRY3 and SPRY4"
FT /evidence="ECO:0000250|UniProtKB:P49817"
FT REGION 150..161
FT /note="Interacts with SPRY1, SPRY2, and SPRY4"
FT /evidence="ECO:0000250|UniProtKB:P49817"
FT REGION 168..179
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 134
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 144
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 157
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 48
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q03135"
FT CROSSLNK 58
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q03135"
SQ SEQUENCE 179 AA; 20666 MW; 0CA4983C20EEB176 CRC64;
MSGGKYVDSE GHLYTVPIRE QGNIYKPNNK AMADEVSEKQ QVYDAHTKEI DLVNRDPKHL
NDDVVKIDFE DVIAEPEGTH SFDGIWKASF TTFTVTKYWF YRLLSALFGI PMALIWGIYF
AILSFLHIWA VVPCIKSFLI EIQCISRVYS IYVHTFCDPL FEAIGKVFSN IRINMQKEI
