ID   CAV2_OTOGA              Reviewed;         162 AA.
AC   Q2QLH8;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   25-MAY-2022, entry version 64.
DE   RecName: Full=Caveolin-2;
GN   Name=CAV2;
OS   Otolemur garnettii (Small-eared galago) (Garnett's greater bushbaby).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Strepsirrhini; Lorisiformes;
OC   Galagidae; Otolemur.
OX   NCBI_TaxID=30611;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   The Broad Institute Genome Sequencing Platform;
RA   Di Palma F., Johnson J., Lander E.S., Lindblad-Toh K., Jaffe D.B.,
RA   Gnerre S., MacCallum I., Przybylski D., Ribeiro F.J., Burton J.N.,
RA   Walker B.J., Sharpe T., Hall G.;
RT   "Version 3 of the genome sequence of Otolemur garnettii(Bushbaby).";
RL   Submitted (MAR-2011) 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       The Ser-36 phosphorylated form has a role in modulating mitosis in
CC       endothelial cells. Positive regulator of cellular mitogenesis of the
CC       MAPK signaling pathway. Required for the insulin-stimulated nuclear
CC       translocation and activation of MAPK1 and STAT3, and the subsequent
CC       regulation of cell cycle progression (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Monomer or homodimer (By similarity). Interacts with CAV1; the
CC       interaction forms a stable heterooligomeric complex that is required
CC       for targeting to lipid rafts and for caveolae formation. Tyrosine
CC       phosphorylated forms do not form heterooligomers with the Tyr-19-
CC       phosphorylated form existing as a monomer or dimer, and the Tyr-27-form
CC       as a monomer only. Interacts (tyrosine phosphorylated form) with the
CC       SH2 domain-containing proteins, RASA1, NCK1 and SRC. Interacts
CC       (tyrosine phosphorylated form) with INSR, the interaction (Tyr-27-
CC       phosphorylated form) is increased on insulin stimulation. Interacts
CC       (Tyr-19 phosphorylated form) with MAPK1 (phosphorylated form); the
CC       interaction, promoted by insulin, leads to nuclear location and MAPK1
CC       activation. Interacts with STAT3; the interaction is increased on
CC       insulin-induced tyrosine phosphorylation leading to STAT activation (By
CC       similarity). {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 (By similarity). Tyr-27-
CC       phosphorylated form is located both in the cytoplasm and plasma
CC       membrane. CAV1-mediated Ser-23-phosphorylated form locates to the
CC       plasma membrane. Ser-36-phosphorylated form resides in intracellular
CC       compartments. {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 Ser-36 appears
CC       to modulate mitosis in endothelial cells (By similarity).
CC       Phosphorylation on both Tyr-19 and Tyr-27 is required for insulin-
CC       induced 'Ser-727' phosphorylation of STAT3 and its activation.
CC       Phosphorylation on Tyr-19 is required for insulin-induced
CC       phosphorylation of MAPK1 and DNA binding of STAT3. Tyrosine
CC       phosphorylation is induced by both EGF and insulin (By. similarity).
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the caveolin family. {ECO:0000305}.
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DR   EMBL; DP000013; ABA90400.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q2QLH8; -.
DR   STRING; 30611.ENSOGAP00000018222; -.
DR   eggNOG; ENOG502RZYX; Eukaryota.
DR   InParanoid; Q2QLH8; -.
DR   Proteomes; UP000005225; Unassembled WGS sequence.
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_0000226342"
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"
FT   MOD_RES         27
FT                   /note="Phosphotyrosine; by SRC"
FT                   /evidence="ECO:0000250|UniProtKB:P51636"
FT   MOD_RES         36
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P51636"
SQ   SEQUENCE   162 AA;  18190 MW;  C050025BB0B66C18 CRC64;
     MGLETEKADV QLFMDDDSYS HHSGVDYGDP EKFVDSGQDR DPHRLNSQLK VGFEDVIAEP
     VTTHSFDKVW ICSHALFEIS KYVLYKFLTV FLAIPLAFVA GILFATLSCL HIWIIMPFVK
     TCLMVLPSVQ TIWKSVTDVI IAPLCTSVGR SFSSISLRLS QD