ID   CAV2_ECHTE              Reviewed;         162 AA.
AC   A1X148;
DT   06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   25-MAY-2022, entry version 50.
DE   RecName: Full=Caveolin-2;
GN   Name=CAV2;
OS   Echinops telfairi (Lesser hedgehog tenrec).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Afrotheria; Tenrecidae; Tenrecinae; Echinops.
OX   NCBI_TaxID=9371;
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 (DEC-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       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. 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}. Golgi apparatus membrane;
CC       Peripheral membrane protein. Cell membrane; Peripheral membrane
CC       protein. Membrane, caveola; Peripheral membrane protein. Note=Potential
CC       hairpin-like structure in the membrane. Membrane protein of caveolae.
CC       Tyr-19-phosphorylated form is enriched at sites of cell-cell contact
CC       and is translocated to the nucleus in complex with MAPK1 in response to
CC       insulin. CAV1-mediated Ser-23-phosphorylated form locates to the plasma
CC       membrane. Ser-36-phosphorylated form resides in intracellular
CC       compartments (By similarity). {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. 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}.
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DR   EMBL; DP000274; ABL76164.1; -; Genomic_DNA.
DR   AlphaFoldDB; A1X148; -.
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   PANTHER; PTHR10844; PTHR10844; 1.
DR   PANTHER; PTHR10844:SF3; PTHR10844:SF3; 1.
DR   Pfam; PF01146; Caveolin; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Golgi apparatus; Membrane; Nucleus; Phosphoprotein.
FT   CHAIN           1..162
FT                   /note="Caveolin-2"
FT                   /id="PRO_0000279732"
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         36
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P51636"
SQ   SEQUENCE   162 AA;  18134 MW;  41DE3438EDFD0576 CRC64;
     MGLESEKADV QLFMDDDAYS RHSGVDFVEA EKFSASGPDR DPHRLNSHLQ LGFQDVIAEP
     ETTHSFDKVW ICSHALFEIS KYVLYKFLTF FLAIPLAFAA GILFAILSCL HIWIIMPFVK
     TCLMVLPSVQ TIWKSVTDVV IAPLCTSVGR SFSSVSLQLS QD