CAV2_PIG
ID CAV2_PIG Reviewed; 162 AA.
AC Q2QLE2;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Caveolin-2;
GN Name=CAV2;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12917688; DOI=10.1038/nature01858;
RA Thomas J.W., Touchman J.W., Blakesley R.W., Bouffard G.G.,
RA Beckstrom-Sternberg S.M., Margulies E.H., Blanchette M., Siepel A.C.,
RA Thomas P.J., McDowell J.C., Maskeri B., Hansen N.F., Schwartz M.S.,
RA Weber R.J., Kent W.J., Karolchik D., Bruen T.C., Bevan R., Cutler D.J.,
RA Schwartz S., Elnitski L., Idol J.R., Prasad A.B., Lee-Lin S.-Q.,
RA Maduro V.V.B., Summers T.J., Portnoy M.E., Dietrich N.L., Akhter N.,
RA Ayele K., Benjamin B., Cariaga K., Brinkley C.P., Brooks S.Y., Granite S.,
RA Guan X., Gupta J., Haghighi P., Ho S.-L., Huang M.C., Karlins E.,
RA Laric P.L., Legaspi R., Lim M.J., Maduro Q.L., Masiello C.A.,
RA Mastrian S.D., McCloskey J.C., Pearson R., Stantripop S., Tiongson E.E.,
RA Tran J.T., Tsurgeon C., Vogt J.L., Walker M.A., Wetherby K.D.,
RA Wiggins L.S., Young A.C., Zhang L.-H., Osoegawa K., Zhu B., Zhao B.,
RA Shu C.L., De Jong P.J., Lawrence C.E., Smit A.F., Chakravarti A.,
RA Haussler D., Green P., Miller W., Green E.D.;
RT "Comparative analyses of multi-species sequences from targeted genomic
RT regions.";
RL Nature 424:788-793(2003).
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 (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. Tyr-27-phosphorylated form
CC is located both in the cytoplasm and plasma membrane. CAV1-mediated
CC Ser-23-phosphorylated form locates to the plasma membrane (By
CC 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 both Tyr-19 and
CC Tyr-27 is required for insulin-induced 'Ser-727' phosphorylation of
CC STAT3 and its activation. Phosphorylation on Tyr-19 is required for
CC insulin-induced phosphorylation of MAPK1 and DNA binding of STAT3.
CC Tyrosine phosphorylation is induced by both EGF and insulin (By
CC similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the caveolin family. {ECO:0000305}.
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DR EMBL; DP000017; AAR16299.1; -; Genomic_DNA.
DR RefSeq; NP_001116563.1; NM_001123091.1.
DR AlphaFoldDB; Q2QLE2; -.
DR STRING; 9823.ENSSSCP00000017623; -.
DR PaxDb; Q2QLE2; -.
DR PeptideAtlas; Q2QLE2; -.
DR PRIDE; Q2QLE2; -.
DR Ensembl; ENSSSCT00000018113; ENSSSCP00000017623; ENSSSCG00000016635.
DR Ensembl; ENSSSCT00015004158; ENSSSCP00015001465; ENSSSCG00015003281.
DR Ensembl; ENSSSCT00025099599; ENSSSCP00025043875; ENSSSCG00025072445.
DR Ensembl; ENSSSCT00030073638; ENSSSCP00030033702; ENSSSCG00030052782.
DR Ensembl; ENSSSCT00035045855; ENSSSCP00035018316; ENSSSCG00035034615.
DR Ensembl; ENSSSCT00040055981; ENSSSCP00040023274; ENSSSCG00040041830.
DR Ensembl; ENSSSCT00045002037; ENSSSCP00045001301; ENSSSCG00045001291.
DR Ensembl; ENSSSCT00050061509; ENSSSCP00050026443; ENSSSCG00050045186.
DR Ensembl; ENSSSCT00055037612; ENSSSCP00055029893; ENSSSCG00055019204.
DR Ensembl; ENSSSCT00060098831; ENSSSCP00060042888; ENSSSCG00060072306.
DR Ensembl; ENSSSCT00065000436; ENSSSCP00065000063; ENSSSCG00065000398.
DR Ensembl; ENSSSCT00070057619; ENSSSCP00070048989; ENSSSCG00070028713.
DR GeneID; 100125375; -.
DR KEGG; ssc:100125375; -.
DR CTD; 858; -.
DR VGNC; VGNC:103914; CAV2.
DR eggNOG; ENOG502RZYX; Eukaryota.
DR GeneTree; ENSGT00950000183006; -.
DR HOGENOM; CLU_102582_2_0_1; -.
DR InParanoid; Q2QLE2; -.
DR OMA; FMDDDAY; -.
DR OrthoDB; 1468974at2759; -.
DR TreeFam; TF315736; -.
DR Proteomes; UP000008227; Chromosome 18.
DR Proteomes; UP000314985; Chromosome 18.
DR Bgee; ENSSSCG00000016635; Expressed in lung and 42 other tissues.
DR Genevisible; Q2QLE2; SS.
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:0031410; C:cytoplasmic vesicle; IBA:GO_Central.
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:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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:0060090; F:molecular adaptor activity; IBA:GO_Central.
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; IBA:GO_Central.
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:0030154; P:cell differentiation; IBA:GO_Central.
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; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0019065; P:receptor-mediated endocytosis of virus by host cell; IEA:Ensembl.
DR GO; GO:0051480; P:regulation of cytosolic calcium ion concentration; IBA:GO_Central.
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; Cytoplasm; Golgi apparatus; Membrane; Nucleus;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..162
FT /note="Caveolin-2"
FT /id="PRO_0000226059"
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"
SQ SEQUENCE 162 AA; 18056 MW; 931E54403BB21E9F CRC64;
MGLETEKADV QLFMDDDSYS RHSGVDYADP KKFVDPGTDR DPHRLNSNLK VGFEDVIAEP
VSTHSFDKVW ICSHALFEIS KYVIYKFLTV FLAIPLAFAA GILFATLSCL HIWIIIPFVK
TCLMVLPSVQ TIWKSVTDVV IAPLCTSAGR SFSSVSLQLS HD
