ID   CAV2_MICMU              Reviewed;         162 AA.
AC   Q2QL91;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Caveolin-2;
GN   Name=CAV2;
OS   Microcebus murinus (Gray mouse lemur) (Lemur murinus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Strepsirrhini; Lemuriformes;
OC   Cheirogaleidae; Microcebus.
OX   NCBI_TaxID=30608;
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 (NOV-2005) 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; DP000022; ABB89818.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q2QL91; -.
DR   Ensembl; ENSMICT00000058158; ENSMICP00000045129; ENSMICG00000045272.
DR   GeneTree; ENSGT00950000183006; -.
DR   HOGENOM; CLU_102582_2_0_1; -.
DR   OMA; FMDDDAY; -.
DR   OrthoDB; 1468974at2759; -.
DR   TreeFam; TF315736; -.
DR   Proteomes; UP000694394; Chromosome 11.
DR   GO; GO:0002080; C:acrosomal membrane; IEA:Ensembl.
DR   GO; GO:0005901; C:caveola; ISS:UniProtKB.
DR   GO; GO:0002095; C:caveolar macromolecular signaling complex; IEA:Ensembl.
DR   GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; ISS:UniProtKB.
DR   GO; GO:0005925; C:focal adhesion; IEA:Ensembl.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005887; C:integral component of plasma membrane; IEA:Ensembl.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR   GO; GO:0030133; C:transport vesicle; IEA:Ensembl.
DR   GO; GO:0031748; F:D1 dopamine receptor binding; ISS:UniProtKB.
DR   GO; GO:0046982; F:protein heterodimerization activity; IEA:Ensembl.
DR   GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
DR   GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
DR   GO; GO:0030674; F:protein-macromolecule adaptor activity; IEA:Ensembl.
DR   GO; GO:0097110; F:scaffold protein binding; IEA:Ensembl.
DR   GO; GO:0071711; P:basement membrane organization; IEA:Ensembl.
DR   GO; GO:0070836; P:caveola assembly; ISS:UniProtKB.
DR   GO; GO:0007029; P:endoplasmic reticulum organization; ISS:UniProtKB.
DR   GO; GO:0001935; P:endothelial cell proliferation; IEA:Ensembl.
DR   GO; GO:0008286; P:insulin receptor signaling pathway; IEA:Ensembl.
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:0014859; P:negative regulation of skeletal muscle cell proliferation; IEA:Ensembl.
DR   GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; IEA:Ensembl.
DR   GO; GO:0044794; P:positive regulation by host of viral process; IEA:Ensembl.
DR   GO; GO:0060161; P:positive regulation of dopamine receptor signaling pathway; ISS:UniProtKB.
DR   GO; GO:0001938; P:positive regulation of endothelial cell proliferation; IEA:Ensembl.
DR   GO; GO:0043547; P:positive regulation of GTPase activity; IEA:Ensembl.
DR   GO; GO:0043410; P:positive regulation of MAPK cascade; IEA:Ensembl.
DR   GO; GO:0019065; P:receptor-mediated endocytosis of virus by host cell; IEA:Ensembl.
DR   GO; GO:0007088; P:regulation of mitotic nuclear division; IEA:Ensembl.
DR   GO; GO:0014856; P:skeletal muscle cell proliferation; IEA:Ensembl.
DR   GO; GO:0048741; P:skeletal muscle fiber development; ISS:UniProtKB.
DR   GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IEA:Ensembl.
DR   GO; GO:0048278; P:vesicle docking; ISS:UniProtKB.
DR   GO; GO:0006906; P:vesicle fusion; ISS:UniProtKB.
DR   GO; GO:0019076; P:viral release from host cell; IEA:Ensembl.
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;
KW   Reference proteome.
FT   CHAIN           1..162
FT                   /note="Caveolin-2"
FT                   /id="PRO_0000226341"
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         36
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P51636"
SQ   SEQUENCE   162 AA;  18233 MW;  9E3AAF539B0B894E CRC64;
     MGLETEKADV QLFLDDDSYS HHGDVDFADP EKFADSDHDR DPHRLNSHLK VGFEDVIAEP
     MTTHSCDKVW ICSHALFEIS KYVMYKFLTV FLAIPLAFVA GILFATLSCL HIWIIMPFVK
     TCLMVLPSVQ TIWKSVTDVI IAPLCTSVGR SFSSISLQLS HD