ID L5KSM1_PTEAL Unreviewed; 178 AA.
AC L5KSM1;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=Caveolin {ECO:0000256|RuleBase:RU000680};
GN ORFNames=PAL_GLEAN10019219 {ECO:0000313|EMBL:ELK13931.1};
OS Pteropus alecto (Black flying fox).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Megachiroptera; Pteropodidae;
OC Pteropodinae; Pteropus.
OX NCBI_TaxID=9402 {ECO:0000313|EMBL:ELK13931.1, ECO:0000313|Proteomes:UP000010552};
RN [1] {ECO:0000313|Proteomes:UP000010552}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23258410; DOI=10.1126/science.1230835;
RA Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X.,
RA Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., Zhou P.,
RA Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., Sun X.,
RA Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., Wang L.F.,
RA Wang J.;
RT "Comparative analysis of bat genomes provides insight into the evolution of
RT flight and immunity.";
RL Science 339:456-460(2013).
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 EMBL; KB030581; ELK13931.1; -; Genomic_DNA.
DR RefSeq; XP_006910649.1; XM_006910587.2.
DR AlphaFoldDB; L5KSM1; -.
DR STRING; 9402.L5KSM1; -.
DR GeneID; 102886570; -.
DR KEGG; pale:102886570; -.
DR CTD; 857; -.
DR eggNOG; ENOG502QUK5; Eukaryota.
DR InParanoid; L5KSM1; -.
DR OrthoDB; 3740765at2759; -.
DR Proteomes; UP000010552; Unassembled WGS sequence.
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:UP000010552};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 98..131
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 178 AA; 20641 MW; C573145607D40D16 CRC64;
MSGGKYVDSE GHLYTVPIRE QGNIYKPNNK AMADEMNEKQ VYDVHTKEID LVNRDPKHLN
DDVVKIDFED VIAEPEGTHS FDGIWKASFT TFTVTKYWFY RLLSGLFGIP MALIWGIYFA
IVSFLHIWVV VPYIKSFLIE IQCISRVYSI CIHTFCDPLF EATGKIFSNI RINMQKEI
//
