CAV2_RABIT
ID CAV2_RABIT Reviewed; 162 AA.
AC Q09YN7;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 25-MAY-2022, entry version 66.
DE RecName: Full=Caveolin-2;
GN Name=CAV2;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
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 (SEP-2006) to the EMBL/GenBank/DDBJ databases.
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. Acts as an accessory protein in conjunction
CC with CAV1 in targeting to lipid rafts and driving caveolae formation.
CC Positive regulator of cellular mitogenesis of the MAPK signaling
CC pathway. Required for the insulin-stimulated nuclear translocation and
CC activation of MAPK1 and STAT3, and the subsequent regulation of cell
CC cycle progression (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Monomer or homodimer. Interacts with CAV1; the interaction
CC forms a stable heterooligomeric complex that is required for targeting
CC to lipid rafts and for caveolae formation. Tyrosine phosphorylated
CC forms do not form heterooligomers with the Tyr-19-phosphorylated form
CC existing as a monomer or dimer. Interacts (tyrosine phosphorylated
CC form) with the SH2 domain-containing proteins, RASA1, NCK1 and SRC.
CC Interacts (tyrosine phosphorylated form) with INSR. Interacts (Tyr-19
CC phosphorylated form) with MAPK1 (phosphorylated form); the interaction,
CC promoted by insulin, leads to nuclear location and MAPK1 activation.
CC Interacts with STAT3; the interaction is increased on insulin-induced
CC tyrosine phosphorylation leading to STAT activation (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC Golgi apparatus membrane; Peripheral membrane protein. Cell membrane;
CC Peripheral membrane protein. Membrane, caveola; Peripheral membrane
CC protein. Note=Potential hairpin-like structure in the membrane.
CC Membrane protein of caveolae. Tyr-19-phosphorylated form is enriched at
CC sites of cell-cell contact and is translocated to the nucleus in
CC complex with MAPK1 in response to insulin. CAV1-mediated Ser-23-
CC phosphorylated form locates to the plasma membrane (By similarity).
CC {ECO:0000250}.
CC -!- PTM: Phosphorylated on serine and tyrosine residues. CAV1 promotes
CC phosphorylation on Ser-23 which then targets the complex to the plasma
CC membrane, lipid rafts and caveolae. Phosphorylation on Tyr-19 is
CC required for insulin-induced phosphorylation of MAPK1 and DNA binding
CC of STAT3. Tyrosine phosphorylation is induced by both EGF and insulin
CC (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the caveolin family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DP000006; AAY89010.1; -; Genomic_DNA.
DR RefSeq; NP_001164493.1; NM_001171022.1.
DR AlphaFoldDB; Q09YN7; -.
DR STRING; 9986.ENSOCUP00000012478; -.
DR GeneID; 100126563; -.
DR KEGG; ocu:100126563; -.
DR CTD; 858; -.
DR eggNOG; ENOG502RZYX; Eukaryota.
DR InParanoid; Q09YN7; -.
DR OrthoDB; 1468974at2759; -.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0005901; C:caveola; ISS:UniProtKB.
DR GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; ISS:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR GO; GO:0031748; F:D1 dopamine receptor binding; ISS:UniProtKB.
DR GO; GO:0070836; P:caveola assembly; ISS:UniProtKB.
DR GO; GO:0007029; P:endoplasmic reticulum organization; ISS:UniProtKB.
DR GO; GO:0007005; P:mitochondrion organization; ISS:UniProtKB.
DR GO; GO:0001937; P:negative regulation of endothelial cell proliferation; ISS:UniProtKB.
DR GO; GO:0060161; P:positive regulation of dopamine receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0048741; P:skeletal muscle fiber development; ISS:UniProtKB.
DR GO; GO:0048278; P:vesicle docking; ISS:UniProtKB.
DR GO; GO:0006906; P:vesicle fusion; ISS:UniProtKB.
DR InterPro; IPR033306; CAV-2.
DR InterPro; IPR001612; Caveolin.
DR InterPro; IPR018361; Caveolin_CS.
DR PANTHER; PTHR10844; PTHR10844; 1.
DR PANTHER; PTHR10844:SF3; PTHR10844:SF3; 1.
DR Pfam; PF01146; Caveolin; 1.
DR PROSITE; PS01210; CAVEOLIN; 1.
PE 3: Inferred from homology;
KW Cell membrane; Cytoplasm; Golgi apparatus; Membrane; Nucleus;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..162
FT /note="Caveolin-2"
FT /id="PRO_0000260383"
FT TOPO_DOM 1..86
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT INTRAMEM 87..107
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 108..162
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOD_RES 19
FT /note="Phosphotyrosine; by SRC"
FT /evidence="ECO:0000250|UniProtKB:P51636"
FT MOD_RES 20
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9WVC3"
FT MOD_RES 23
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P51636"
SQ SEQUENCE 162 AA; 17968 MW; 8F2797A21704EB80 CRC64;
MGLETEKADV QLFMDDDAYS HHSGVDFADP EKFPDTGPDR DPHGLNSHLK LGFEDVIAEP
VTTHSFDKVW ICSHALFEIS KYVLYKFLTV FLAIPLAFAA GVLFAVLSCL HIWILMPFVK
TCLMVLPSVQ TIWRSVTDVV IAPLCASIGR SFSSVGLQLS HD
