ID   CAV2_MUNRE              Reviewed;         162 AA.
AC   Q07DX2;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, sequence version 1.
DT   25-MAY-2022, entry version 45.
DE   RecName: Full=Caveolin-2;
GN   Name=CAV2;
OS   Muntiacus reevesi (Reeves' muntjac) (Cervus reevesi).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Cervidae;
OC   Muntiacinae; Muntiacus.
OX   NCBI_TaxID=9886;
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. Caveolin-2 may function as an accessory
CC       protein in conjunction with caveolin-1 (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer. Caveolin-1 and -2 colocalize and form a stable
CC       hetero-oligomeric complex (By similarity). {ECO:0000250}.
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}.
CC       Note=Potential hairpin-like structure in the membrane. Membrane protein
CC       of caveolae (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the caveolin family. {ECO:0000305}.
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DR   EMBL; DP000195; ABJ08870.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q07DX2; -.
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: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; Golgi apparatus; Membrane; Phosphoprotein.
FT   CHAIN           1..162
FT                   /note="Caveolin-2"
FT                   /id="PRO_0000260380"
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"
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"
FT   MOD_RES         27
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P51636"
SQ   SEQUENCE   162 AA;  18146 MW;  863DAA5EADF48256 CRC64;
     MGLETEKADV QLFMDDDSYS RHSSVDYADP DKFVDPGSDR DPHRLNSHLK VGFEDVIAEP
     VSTHSFDKVW ICSHALFEMS KYVIYKFLTV FLAIPLAFAA GILFATLSCL HIWIIMPFVK
     TCLMVLPSVQ TIWKSVTDVV IAPLCTSVGR SFSSVSLQLS HD