CAV2_BOVIN
ID CAV2_BOVIN Reviewed; 162 AA.
AC Q66WT7; A4D7R4; A7YWJ5;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Caveolin-2;
GN Name=CAV2;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH CAV1, TISSUE SPECIFICITY, AND
RP SUBCELLULAR LOCATION.
RX PubMed=15370296; DOI=10.1080/10623320490512282;
RA Boyd N., Park H., Sun W.P., Coleman S., Cherukuri R., Jo H.;
RT "Bovine caveolin-2 cloning and effects of shear stress on its localization
RT in bovine aortic endothelial cells.";
RL Endothelium 11:189-198(2004).
RN [2]
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).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal skin;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (MAR-2007) 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 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. 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, and the Tyr-27-form as a monomer only.
CC Interacts (tyrosine phosphorylated form) with the SH2 domain-containing
CC proteins, RASA1, NCK1 and SRC. Interacts (tyrosine phosphorylated form)
CC with INSR, the interaction (Tyr-27-phosphorylated form) is increased on
CC insulin stimulation. Interacts (Tyr-19 phosphorylated form) with MAPK1
CC (phosphorylated form); the interaction, promoted by insulin, leads to
CC nuclear location and MAPK1 activation. Interacts with STAT3; the
CC interaction is increased on insulin-induced tyrosine phosphorylation
CC leading to STAT activation (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15370296}. Cytoplasm
CC {ECO:0000269|PubMed:15370296}. Golgi apparatus membrane
CC {ECO:0000269|PubMed:15370296}; Peripheral membrane protein
CC {ECO:0000269|PubMed:15370296}. Cell membrane
CC {ECO:0000269|PubMed:15370296}; Peripheral membrane protein
CC {ECO:0000269|PubMed:15370296}. Membrane, caveola
CC {ECO:0000269|PubMed:15370296}; Peripheral membrane protein
CC {ECO:0000269|PubMed:15370296}. Note=Potential hairpin-like structure in
CC the membrane. Membrane protein of caveolae. Tyr-19-phosphorylated form
CC is enriched at sites of cell-cell contact and is translocated to the
CC nucleus in complex with MAPK1 in response to insulin. 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 (By similarity). {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in aortic endothelial cells.
CC {ECO:0000269|PubMed:15370296}.
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; AY699947; AAU05317.1; -; mRNA.
DR EMBL; DP000008; AAR16255.1; -; Genomic_DNA.
DR EMBL; BC134620; AAI34621.1; -; mRNA.
DR RefSeq; NP_001007809.1; NM_001007808.1.
DR AlphaFoldDB; Q66WT7; -.
DR STRING; 9913.ENSBTAP00000054207; -.
DR PaxDb; Q66WT7; -.
DR Ensembl; ENSBTAT00000077494; ENSBTAP00000058170; ENSBTAG00000049397.
DR GeneID; 493642; -.
DR KEGG; bta:493642; -.
DR CTD; 858; -.
DR VEuPathDB; HostDB:ENSBTAG00000049397; -.
DR VGNC; VGNC:26800; CAV2.
DR eggNOG; ENOG502RZYX; Eukaryota.
DR GeneTree; ENSGT00950000183006; -.
DR HOGENOM; CLU_102582_2_0_1; -.
DR InParanoid; Q66WT7; -.
DR OMA; FMDDDAY; -.
DR OrthoDB; 1468974at2759; -.
DR TreeFam; TF315736; -.
DR Proteomes; UP000009136; Chromosome 4.
DR Bgee; ENSBTAG00000049397; Expressed in omental fat pad and 103 other tissues.
DR GO; GO:0002080; C:acrosomal membrane; IEA:Ensembl.
DR GO; GO:0005901; C:caveola; IDA:BHF-UCL.
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:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR GO; GO:0042383; C:sarcolemma; IDA:BHF-UCL.
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 1: Evidence at protein level;
KW Cell membrane; Cytoplasm; Golgi apparatus; Membrane; Nucleus;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..162
FT /note="Caveolin-2"
FT /id="PRO_0000144136"
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; 18160 MW; 863DAA5EADF49AF5 CRC64;
MGLETEKADV QLFMDDDSYS RHSSVDYADP DKFVDPGSDR DPHRLNSHLK VGFEDVIAEP
VSTHSFDKVW ICSHALFEMS KYVIYKFLTV FLAIPLAFAA GILFATLSCL HIWIIMPFVK
TCLMVLPSVQ TIWKSVTDVV IAPLCTSIGR SFSSVSLQLS HD
