CAV1_CHICK
ID CAV1_CHICK Reviewed; 178 AA.
AC P35431;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Caveolin-1;
GN Name=CAV1;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1279683; DOI=10.1073/pnas.89.21.10517;
RA Glenney J.R. Jr., Soppet D.;
RT "Sequence and expression of caveolin, a protein component of caveolae
RT plasma membrane domains phosphorylated on tyrosine in Rous sarcoma virus-
RT transformed fibroblasts.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:10517-10521(1992).
CC -!- FUNCTION: May act as a positive regulator of T-cell coactivation. May
CC act as a scaffolding protein within caveolar membranes. Interacts
CC directly with G-protein alpha subunits and can functionally regulate
CC their activity (By similarity). {ECO:0000250|UniProtKB:Q03135}.
CC -!- SUBUNIT: Homooligomer. {ECO:0000250|UniProtKB:Q03135}.
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}; Peripheral membrane protein {ECO:0000250}. Membrane raft
CC {ECO:0000250|UniProtKB:Q03135}. Note=Potential hairpin-like structure
CC in the membrane. Membrane protein of caveolae (By similarity).
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=Alpha;
CC IsoId=P35431-1; Sequence=Displayed;
CC Name=Beta;
CC IsoId=P35431-2; Sequence=VSP_018695;
CC -!- PTM: Phosphorylated on tyrosine residue(s).
CC {ECO:0000250|UniProtKB:Q03135}.
CC -!- SIMILARITY: Belongs to the caveolin family. {ECO:0000305}.
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DR EMBL; L01582; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; NP_001099134.1; NM_001105664.2. [P35431-1]
DR AlphaFoldDB; P35431; -.
DR STRING; 9031.ENSGALP00000015287; -.
DR PaxDb; P35431; -.
DR GeneID; 373996; -.
DR KEGG; gga:373996; -.
DR CTD; 857; -.
DR VEuPathDB; HostDB:geneid_373996; -.
DR eggNOG; ENOG502QUK5; Eukaryota.
DR InParanoid; P35431; -.
DR OrthoDB; 1468974at2759; -.
DR PhylomeDB; P35431; -.
DR PRO; PR:P35431; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005901; C:caveola; IDA:AgBase.
DR GO; GO:0031410; C:cytoplasmic vesicle; IBA:GO_Central.
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; 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: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: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 Alternative initiation; Cell membrane; Golgi apparatus; Lipoprotein;
KW Membrane; Palmitate; Phosphoprotein; Reference proteome.
FT CHAIN 1..178
FT /note="Caveolin-1"
FT /id="PRO_0000004770"
FT TOPO_DOM 1..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 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 VAR_SEQ 1..31
FT /note="Missing (in isoform Beta)"
FT /evidence="ECO:0000305"
FT /id="VSP_018695"
SQ SEQUENCE 178 AA; 20447 MW; B5DF7F94ED68B948 CRC64;
MSGTKYVDSE GFLYAAPVRE QGNIYKPNNK MMADELSEKA VHDVDTKEID LVNRDPKHLN
DDVVKIDFED VIAEPEGTHS FDGIWKASFT TFTVTKYWFY RLLSAIFGIP MALIWGIYFA
ILSFLHIWAV VPCIRSYLIE IQCISRVYSI CIHTFCDPLF EAMGKVFSSI RATVRKEI
