ID A0A1S3WF52_ERIEU Unreviewed; 147 AA.
AC A0A1S3WF52;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Caveolin {ECO:0000256|RuleBase:RU000680};
GN Name=CAV1 {ECO:0000313|RefSeq:XP_016044759.1};
OS Erinaceus europaeus (Western European hedgehog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Eulipotyphla; Erinaceidae; Erinaceinae;
OC Erinaceus.
OX NCBI_TaxID=9365 {ECO:0000313|Proteomes:UP000079721, ECO:0000313|RefSeq:XP_016044759.1};
RN [1] {ECO:0000313|RefSeq:XP_016044759.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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.
CC {ECO:0000256|ARBA:ARBA00024950}.
CC -!- FUNCTION: May act as a scaffolding protein within caveolar membranes.
CC Interacts directly with G-protein alpha subunits and can functionally
CC regulate their activity. {ECO:0000256|RuleBase:RU000680}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004202,
CC ECO:0000256|RuleBase:RU000680}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004202, ECO:0000256|RuleBase:RU000680}. Golgi
CC apparatus membrane {ECO:0000256|RuleBase:RU000680}; Peripheral membrane
CC protein {ECO:0000256|RuleBase:RU000680}. Membrane, caveola
CC {ECO:0000256|RuleBase:RU000680}; Peripheral membrane protein
CC {ECO:0000256|RuleBase:RU000680}. Membrane raft
CC {ECO:0000256|ARBA:ARBA00004285}. Membrane
CC {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004170}.
CC -!- SIMILARITY: Belongs to the caveolin family.
CC {ECO:0000256|ARBA:ARBA00010988, ECO:0000256|RuleBase:RU000680}.
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DR RefSeq; XP_016044759.1; XM_016189273.1.
DR AlphaFoldDB; A0A1S3WF52; -.
DR GeneID; 103115649; -.
DR CTD; 857; -.
DR OrthoDB; 3740765at2759; -.
DR Proteomes; UP000079721; Unplaced.
DR GO; GO:0005901; C:caveola; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0070836; P:caveola assembly; IEA:InterPro.
DR InterPro; IPR001612; Caveolin.
DR InterPro; IPR018361; Caveolin_CS.
DR PANTHER; PTHR10844; CAVEOLIN; 1.
DR PANTHER; PTHR10844:SF18; CAVEOLIN-1; 1.
DR Pfam; PF01146; Caveolin; 1.
DR PROSITE; PS01210; CAVEOLIN; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|RuleBase:RU000680};
KW Golgi apparatus {ECO:0000256|ARBA:ARBA00023034,
KW ECO:0000256|RuleBase:RU000680};
KW Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW Membrane {ECO:0000256|RuleBase:RU000680, ECO:0000256|SAM:Phobius};
KW Palmitate {ECO:0000256|ARBA:ARBA00023139};
KW Reference proteome {ECO:0000313|Proteomes:UP000079721};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 75..98
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 147 AA; 17112 MW; AA315D2F25AFED97 CRC64;
MAEEMNEKQM YDAHTKEIDL VNRDPKHLND DVVKIDFEDV IAEPEGTHSF DGVWKASFTT
FTVTKYWFYR LLSSLVGIPV ALIWGIYFAI LSFLYIWAVV PCIKSFLIKI QCISRIYSIC
IHTFCDPLYE AIGKIFSNIR ISMQKEI
//
