CAV2_HUMAN
ID CAV2_HUMAN Reviewed; 162 AA.
AC P51636; A4D0U2; Q9UGM7;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1999, sequence version 2.
DT 03-AUG-2022, entry version 201.
DE RecName: Full=Caveolin-2;
GN Name=CAV2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA).
RX PubMed=8552590; DOI=10.1073/pnas.93.1.131;
RA Scherer P.E., Okamoto T., Chun M., Nishimoto I., Lodish H.F., Lisanti M.P.;
RT "Identification, sequence, and expression of caveolin-2 defines a caveolin
RT gene family.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:131-135(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA), INTERACTION WITH CAV1,
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=9361015; DOI=10.1074/jbc.272.46.29337;
RA Scherer P.E., Lewis R.Y., Volonte D., Engelman J.A., Galbiati F., Couet J.,
RA Kohtz D.S., van Donselaar E., Peters P., Lisanti M.P.;
RT "Cell-type and tissue-specific expression of caveolin-2. Caveolins 1 and 2
RT co-localize and form a stable hetero-oligomeric complex in vivo.";
RL J. Biol. Chem. 272:29337-29346(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10218480; DOI=10.1016/s0014-5793(99)00365-8;
RA Engelman J.A., Zhang X.L., Lisanti M.P.;
RT "Sequence and detailed organization of the human caveolin-1 and -2 genes
RT located near the D7S522 locus (7q31.1). Methylation of a CpG island in the
RT 5' promoter region of the caveolin-1 gene in human breast cancer cell
RT lines.";
RL FEBS Lett. 448:221-230(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM C).
RC TISSUE=Hepatoma;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12690205; DOI=10.1126/science.1083423;
RA Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
RA Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
RA Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
RA Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D.,
RA Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S.,
RA Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R.,
RA Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N.,
RA Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E.,
RA Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R.,
RA Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T.,
RA Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W.,
RA Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A.,
RA Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X.,
RA Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E.,
RA Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
RA Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J.,
RA Adams M.D., Tsui L.-C.;
RT "Human chromosome 7: DNA sequence and biology.";
RL Science 300:767-772(2003).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA).
RC TISSUE=Kidney;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP INTERACTION WITH CAV1, ALTERNATIVE PRODUCTS, AND SUBCELLULAR LOCATION.
RX PubMed=9738464; DOI=10.1016/s0014-5793(98)00945-4;
RA Li S., Galbiati F., Volonte D., Sargiacomo M., Engelman J.A., Das K.,
RA Scherer P.E., Lisanti M.P.;
RT "Mutational analysis of caveolin-induced vesicle formation. Expression of
RT caveolin-1 recruits caveolin-2 to caveolae membranes.";
RL FEBS Lett. 434:127-134(1998).
RN [9]
RP PHOSPHORYLATION AT TYR-19, SUBCELLULAR LOCATION, AND INTERACTION WITH CAV1;
RP SRC; RASA1 AND NCK1.
RX PubMed=12091389; DOI=10.1074/jbc.m204367200;
RA Lee H., Park D.S., Wang X.B., Scherer P.E., Schwartz P.E., Lisanti M.P.;
RT "Src-induced phosphorylation of caveolin-2 on tyrosine 19. Phospho-
RT caveolin-2 (Tyr(P)19) is localized near focal adhesions, remains associated
RT with lipid rafts/caveolae, but no longer forms a high molecular mass
RT hetero-oligomer with caveolin-1.";
RL J. Biol. Chem. 277:34556-34567(2002).
RN [10]
RP PHOSPHORYLATION AT TYR-19 AND TYR-27, SUBCELLULAR LOCATION, INTERACTION
RP WITH CAV1; NCK1; RASA1 AND SRC, FUNCTION, AND MUTAGENESIS OF TYR-19 AND
RP TYR-27.
RX PubMed=15504032; DOI=10.1021/bi049295+;
RA Wang X.B., Lee H., Capozza F., Marmon S., Sotgia F., Brooks J.W.,
RA Campos-Gonzalez R., Lisanti M.P.;
RT "Tyrosine phosphorylation of caveolin-2 at residue 27: differences in the
RT spatial and temporal behavior of phospho-Cav-2 (pY19 and pY27).";
RL Biochemistry 43:13694-13706(2004).
RN [11]
RP PHOSPHORYLATION AT SER-23 AND SER-36, FUNCTION, SUBCELLULAR LOCATION, AND
RP MUTAGENESIS OF SER-23 AND SER-36.
RX PubMed=18081315; DOI=10.1021/bi701709s;
RA Sowa G., Xie L., Xu L., Sessa W.C.;
RT "Serine 23 and 36 phosphorylation of caveolin-2 is differentially regulated
RT by targeting to lipid raft/caveolae and in mitotic endothelial cells.";
RL Biochemistry 47:101-111(2008).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
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 ECO:0000269|PubMed:15504032, ECO:0000269|PubMed:18081315}.
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 -!- INTERACTION:
CC P51636; Q03135: CAV1; NbExp=4; IntAct=EBI-603607, EBI-603614;
CC P51636; P00533: EGFR; NbExp=3; IntAct=EBI-603607, EBI-297353;
CC P51636; O00560: SDCBP; NbExp=3; IntAct=EBI-603607, EBI-727004;
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. 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 (By similarity). Tyr-27-phosphorylated form is located both in
CC the cytoplasm and plasma membrane. CAV1-mediated Ser-23-phosphorylated
CC form locates to the plasma membrane. Ser-36-phosphorylated form resides
CC in intracellular compartments. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing, Alternative initiation; Named isoforms=3;
CC Name=Alpha;
CC IsoId=P51636-1; Sequence=Displayed;
CC Name=Beta;
CC IsoId=P51636-2; Sequence=VSP_018696;
CC Name=C;
CC IsoId=P51636-3; Sequence=VSP_038114, VSP_038115;
CC -!- TISSUE SPECIFICITY: Expressed in endothelial cells, smooth muscle
CC cells, skeletal myoblasts and fibroblasts.
CC {ECO:0000269|PubMed:9361015}.
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 -!- MISCELLANEOUS: [Isoform Beta]: Produced by alternative initiation.
CC {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform C]: Produced by alternative splicing.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the caveolin family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Caveolin entry;
CC URL="https://en.wikipedia.org/wiki/Caveolin";
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DR EMBL; AF035752; AAB88492.1; -; mRNA.
DR EMBL; AJ133269; CAB63653.1; -; Genomic_DNA.
DR EMBL; BT007051; AAP35700.1; -; mRNA.
DR EMBL; BC005256; AAH05256.1; -; mRNA.
DR EMBL; AJ242718; CAB65090.1; -; Genomic_DNA.
DR EMBL; AK310786; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; CH236947; EAL24361.1; -; Genomic_DNA.
DR CCDS; CCDS5765.1; -. [P51636-3]
DR CCDS; CCDS5766.1; -. [P51636-1]
DR RefSeq; NP_001193676.1; NM_001206747.1. [P51636-2]
DR RefSeq; NP_001193677.1; NM_001206748.1.
DR RefSeq; NP_001224.1; NM_001233.4. [P51636-1]
DR RefSeq; NP_937855.1; NM_198212.2. [P51636-3]
DR AlphaFoldDB; P51636; -.
DR BioGRID; 107306; 130.
DR DIP; DIP-34929N; -.
DR IntAct; P51636; 70.
DR MINT; P51636; -.
DR STRING; 9606.ENSP00000222693; -.
DR TCDB; 8.A.104.1.11; the 5'-amp-activated protein kinase (ampk) family.
DR iPTMnet; P51636; -.
DR PhosphoSitePlus; P51636; -.
DR SwissPalm; P51636; -.
DR BioMuta; CAV2; -.
DR EPD; P51636; -.
DR jPOST; P51636; -.
DR MassIVE; P51636; -.
DR MaxQB; P51636; -.
DR PaxDb; P51636; -.
DR PeptideAtlas; P51636; -.
DR PRIDE; P51636; -.
DR ProteomicsDB; 56353; -. [P51636-1]
DR ProteomicsDB; 56354; -. [P51636-2]
DR ProteomicsDB; 56355; -. [P51636-3]
DR Antibodypedia; 4606; 431 antibodies from 38 providers.
DR DNASU; 858; -.
DR Ensembl; ENST00000222693.5; ENSP00000222693.4; ENSG00000105971.15. [P51636-1]
DR Ensembl; ENST00000343213.2; ENSP00000345679.2; ENSG00000105971.15. [P51636-3]
DR GeneID; 858; -.
DR KEGG; hsa:858; -.
DR MANE-Select; ENST00000222693.5; ENSP00000222693.4; NM_001233.5; NP_001224.1.
DR UCSC; uc003vie.4; human. [P51636-1]
DR CTD; 858; -.
DR DisGeNET; 858; -.
DR GeneCards; CAV2; -.
DR HGNC; HGNC:1528; CAV2.
DR HPA; ENSG00000105971; Tissue enhanced (adipose).
DR MIM; 601048; gene.
DR neXtProt; NX_P51636; -.
DR OpenTargets; ENSG00000105971; -.
DR PharmGKB; PA26108; -.
DR VEuPathDB; HostDB:ENSG00000105971; -.
DR eggNOG; ENOG502RZYX; Eukaryota.
DR GeneTree; ENSGT00950000183006; -.
DR HOGENOM; CLU_2145024_0_0_1; -.
DR InParanoid; P51636; -.
DR OMA; FMDDDAY; -.
DR PhylomeDB; P51636; -.
DR TreeFam; TF315736; -.
DR PathwayCommons; P51636; -.
DR Reactome; R-HSA-9009391; Extra-nuclear estrogen signaling.
DR SignaLink; P51636; -.
DR SIGNOR; P51636; -.
DR BioGRID-ORCS; 858; 10 hits in 1080 CRISPR screens.
DR ChiTaRS; CAV2; human.
DR GeneWiki; Caveolin_2; -.
DR GenomeRNAi; 858; -.
DR Pharos; P51636; Tbio.
DR PRO; PR:P51636; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; P51636; protein.
DR Bgee; ENSG00000105971; Expressed in lower lobe of lung and 210 other tissues.
DR ExpressionAtlas; P51636; baseline and differential.
DR Genevisible; P51636; HS.
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:0031410; C:cytoplasmic vesicle; IDA:MGI.
DR GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; IDA:BHF-UCL.
DR GO; GO:0005925; C:focal adhesion; IEA:Ensembl.
DR GO; GO:0005794; C:Golgi apparatus; ISS:BHF-UCL.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:MGI.
DR GO; GO:0016020; C:membrane; IDA:BHF-UCL.
DR GO; GO:0045121; C:membrane raft; IDA:HGNC-UCL.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:BHF-UCL.
DR GO; GO:0005886; C:plasma membrane; IDA:BHF-UCL.
DR GO; GO:0032991; C:protein-containing complex; IDA:MGI.
DR GO; GO:0030133; C:transport vesicle; IDA:LIFEdb.
DR GO; GO:0031748; F:D1 dopamine receptor binding; IPI:BHF-UCL.
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; IDA:MGI.
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; IDA:BHF-UCL.
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; IDA:BHF-UCL.
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; IMP:AgBase.
DR GO; GO:0060161; P:positive regulation of dopamine receptor signaling pathway; IMP:BHF-UCL.
DR GO; GO:0001938; P:positive regulation of endothelial cell proliferation; IEA:Ensembl.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IDA:BHF-UCL.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; IDA:BHF-UCL.
DR GO; GO:0019065; P:receptor-mediated endocytosis of virus by host cell; IGI:CACAO.
DR GO; GO:0051480; P:regulation of cytosolic calcium ion concentration; IBA:GO_Central.
DR GO; GO:0007088; P:regulation of mitotic nuclear division; IEP:BHF-UCL.
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; IDA:BHF-UCL.
DR GO; GO:0006906; P:vesicle fusion; IDA:BHF-UCL.
DR GO; GO:0016050; P:vesicle organization; IDA:BHF-UCL.
DR GO; GO:0019076; P:viral release from host cell; IMP:AgBase.
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 Alternative initiation; Alternative splicing; Cell membrane; Cytoplasm;
KW Golgi apparatus; Membrane; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..162
FT /note="Caveolin-2"
FT /id="PRO_0000004772"
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:0000269|PubMed:12091389,
FT ECO:0000269|PubMed:15504032"
FT MOD_RES 20
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9WVC3"
FT MOD_RES 23
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18081315"
FT MOD_RES 27
FT /note="Phosphotyrosine; by SRC"
FT /evidence="ECO:0000269|PubMed:15504032"
FT MOD_RES 36
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18081315"
FT VAR_SEQ 1..13
FT /note="Missing (in isoform Beta)"
FT /evidence="ECO:0000305"
FT /id="VSP_018696"
FT VAR_SEQ 51..112
FT /note="LGFEDVIAEPVTTHSFDKVWICSHALFEISKYVMYKFLTVFLAIPLAFIAGI
FT LFATLSCLHI -> DFNAFCKDLPNGSAFSADNMEECDRCYHCSIVYERRTMLLFCQPA
FT TEPGLNTWTPGLEIGIL (in isoform C)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_038114"
FT VAR_SEQ 113..162
FT /note="Missing (in isoform C)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_038115"
FT VARIANT 130
FT /note="Q -> E (in dbSNP:rs8940)"
FT /id="VAR_012071"
FT MUTAGEN 19
FT /note="Y->A: Greatly reduced Src-mediated phosphorylation
FT and binding of RASA1, SRC and NCK1. Completely eliminates
FT Src-mediated tyrosine phosphorylation and binding to RASA1,
FT SRC and NCK1; when associated with A-27."
FT /evidence="ECO:0000269|PubMed:15504032"
FT MUTAGEN 23
FT /note="S->A: Abolishes phosphorylation."
FT /evidence="ECO:0000269|PubMed:18081315"
FT MUTAGEN 27
FT /note="Y->A: Greatly reduced Src-mediated phosphorylation
FT and binding of RASA1, SRC and NCK1. Completely eliminates
FT Src-mediated phosphorylation and binding of RASA1, SRC and
FT NCK1; when associated with A-19."
FT /evidence="ECO:0000269|PubMed:15504032"
FT MUTAGEN 36
FT /note="S->A: Abolishes phosphorylation."
FT /evidence="ECO:0000269|PubMed:18081315"
SQ SEQUENCE 162 AA; 18291 MW; 89FDEDA861330B87 CRC64;
MGLETEKADV QLFMDDDSYS HHSGLEYADP EKFADSDQDR DPHRLNSHLK LGFEDVIAEP
VTTHSFDKVW ICSHALFEIS KYVMYKFLTV FLAIPLAFIA GILFATLSCL HIWILMPFVK
TCLMVLPSVQ TIWKSVTDVI IAPLCTSVGR CFSSVSLQLS QD
