CAV1_PIG
ID CAV1_PIG Reviewed; 178 AA.
AC Q6RVA9; Q0PHA2; Q2QLE1;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Caveolin-1;
GN Name=CAV1 {ECO:0000312|EMBL:AAR92481.1};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1] {ECO:0000312|EMBL:AAR92481.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Muscle;
RA Tian X., Li J., Wang C., Chen Y.;
RT "Cloning and expression of cav-1 in pig.";
RL Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000312|EMBL:AAR92481.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Mei Y., Li J., Wang C., Chen Y., Tian X.;
RT "Cloning and expression analysis of pig caveolin 1 gene.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
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).
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:0000255}.
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DR EMBL; AY490204; AAR92481.1; -; mRNA.
DR EMBL; DQ835010; ABH03043.1; -; mRNA.
DR EMBL; DP000017; AAR16300.1; -; Genomic_DNA.
DR RefSeq; NP_999603.1; NM_214438.2.
DR AlphaFoldDB; Q6RVA9; -.
DR IntAct; Q6RVA9; 1.
DR STRING; 9823.ENSSSCP00000017622; -.
DR PaxDb; Q6RVA9; -.
DR PeptideAtlas; Q6RVA9; -.
DR PRIDE; Q6RVA9; -.
DR GeneID; 404693; -.
DR KEGG; ssc:404693; -.
DR CTD; 857; -.
DR eggNOG; ENOG502QUK5; Eukaryota.
DR HOGENOM; CLU_102582_0_0_1; -.
DR InParanoid; Q6RVA9; -.
DR OrthoDB; 1468974at2759; -.
DR TreeFam; TF315736; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR Genevisible; Q6RVA9; SS.
DR GO; GO:0005901; C:caveola; IDA:AgBase.
DR GO; GO:0031410; C:cytoplasmic vesicle; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:HGNC-UCL.
DR GO; GO:0005768; C:endosome; ISS:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0000139; C:Golgi membrane; ISS:HGNC-UCL.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0045121; C:membrane raft; ISS:HGNC-UCL.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:AgBase.
DR GO; GO:0060090; F:molecular adaptor activity; IBA:GO_Central.
DR GO; GO:0019901; F:protein kinase binding; IBA:GO_Central.
DR GO; GO:0044325; F:transmembrane transporter binding; IBA:GO_Central.
DR GO; GO:0070836; P:caveola assembly; IBA:GO_Central.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0001937; P:negative regulation of endothelial cell proliferation; IBA:GO_Central.
DR GO; GO:0061099; P:negative regulation of protein tyrosine kinase activity; IBA:GO_Central.
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:0051480; P:regulation of cytosolic calcium ion concentration; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Acetylation; Cell membrane; 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_0000144134"
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|UniProtKB:P33724"
FT LIPID 143
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P33724"
FT LIPID 156
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P33724"
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; 20625 MW; 1A67CE55F431A3BF CRC64;
MSGGKYVDSE GHLYTVPIRE QGNIYKPNNK AMAEEMNEKQ VYDAHTKEID LVNRDPKHLN
DDVVKIDFED VIAEPEGTHS FDGIWKASFT TFTVTKYWFY RLLSALFGIP MALIWGIYFA
ILSFLHIWAV VPCIKSFLIE IQCISRVYSI YVHTFCDPLF EAIGKIFSNI RINMQKEI
