CAV2_MOUSE
ID CAV2_MOUSE Reviewed; 162 AA.
AC Q9WVC3; Q3TYR4;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Caveolin-2;
GN Name=Cav2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=3T3-L1;
RX PubMed=10373486; DOI=10.1074/jbc.274.26.18721;
RA Das K., Lewis R.Y., Scherer P.E., Lisanti M.P.;
RT "The membrane-spanning domains of caveolins-1 and -2 mediate the formation
RT of caveolin hetero-oligomers. Implications for the assembly of caveolae
RT membranes in vivo.";
RL J. Biol. Chem. 274:18721-18728(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Kogo H., Ishiguro K., Kuwaki S., Fujimoto T.;
RT "Identification of mouse caveolin-2 mRNA variant.";
RL Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Bone marrow, Inner ear, Lung, and Tongue;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary gland;
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 [5]
RP PHOSPHORYLATION AT TYR-19.
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 [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-19; SER-20; SER-23 AND
RP TYR-27, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Pancreas, Spleen,
RC and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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, 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. 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. Tyr-27-phosphorylated form is located both in the cytoplasm
CC and plasma membrane. CAV1-mediated Ser-23-phosphorylated form locates
CC to the plasma membrane. Ser-36-phosphorylated form resides in
CC intracellular 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 both Tyr-
CC 19 and Tyr-27 is required for insulin-induced 'Ser-727' phosphorylation
CC of 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; AF141322; AAD42349.1; -; mRNA.
DR EMBL; AB049604; BAB61728.1; -; mRNA.
DR EMBL; AK004663; BAB23453.1; -; mRNA.
DR EMBL; AK009913; BAB26582.1; -; mRNA.
DR EMBL; AK151397; BAE30365.1; -; mRNA.
DR EMBL; AK158419; BAE34498.1; -; mRNA.
DR EMBL; BC023095; AAH23095.1; -; mRNA.
DR CCDS; CCDS19923.1; -.
DR RefSeq; NP_058596.1; NM_016900.4.
DR AlphaFoldDB; Q9WVC3; -.
DR SMR; Q9WVC3; -.
DR IntAct; Q9WVC3; 1.
DR STRING; 10090.ENSMUSP00000000058; -.
DR iPTMnet; Q9WVC3; -.
DR PhosphoSitePlus; Q9WVC3; -.
DR SwissPalm; Q9WVC3; -.
DR jPOST; Q9WVC3; -.
DR MaxQB; Q9WVC3; -.
DR PaxDb; Q9WVC3; -.
DR PeptideAtlas; Q9WVC3; -.
DR PRIDE; Q9WVC3; -.
DR ProteomicsDB; 265336; -.
DR Antibodypedia; 4606; 431 antibodies from 38 providers.
DR DNASU; 12390; -.
DR Ensembl; ENSMUST00000000058; ENSMUSP00000000058; ENSMUSG00000000058.
DR GeneID; 12390; -.
DR KEGG; mmu:12390; -.
DR UCSC; uc009azm.2; mouse.
DR CTD; 858; -.
DR MGI; MGI:107571; Cav2.
DR VEuPathDB; HostDB:ENSMUSG00000000058; -.
DR eggNOG; ENOG502RZYX; Eukaryota.
DR GeneTree; ENSGT00950000183006; -.
DR InParanoid; Q9WVC3; -.
DR OMA; FMDDDAY; -.
DR OrthoDB; 1468974at2759; -.
DR PhylomeDB; Q9WVC3; -.
DR TreeFam; TF315736; -.
DR Reactome; R-MMU-9009391; Extra-nuclear estrogen signaling.
DR BioGRID-ORCS; 12390; 3 hits in 77 CRISPR screens.
DR ChiTaRS; Cav2; mouse.
DR PRO; PR:Q9WVC3; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q9WVC3; protein.
DR Bgee; ENSMUSG00000000058; Expressed in epididymal fat pad and 236 other tissues.
DR ExpressionAtlas; Q9WVC3; baseline and differential.
DR Genevisible; Q9WVC3; MM.
DR GO; GO:0002080; C:acrosomal membrane; IDA:MGI.
DR GO; GO:0005901; C:caveola; IDA:MGI.
DR GO; GO:0002095; C:caveolar macromolecular signaling complex; IDA:MGI.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0031410; C:cytoplasmic vesicle; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; ISS:UniProtKB.
DR GO; GO:0005925; C:focal adhesion; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005887; C:integral component of plasma membrane; ISO:MGI.
DR GO; GO:0005811; C:lipid droplet; ISO:MGI.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0045121; C:membrane raft; ISS:HGNC-UCL.
DR GO; GO:0005635; C:nuclear envelope; ISO:MGI.
DR GO; GO:0005637; C:nuclear inner membrane; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0032991; C:protein-containing complex; IDA:BHF-UCL.
DR GO; GO:0045202; C:synapse; IEA:GOC.
DR GO; GO:0030133; C:transport vesicle; ISO:MGI.
DR GO; GO:0031748; F:D1 dopamine receptor binding; ISS:UniProtKB.
DR GO; GO:0031435; F:mitogen-activated protein kinase kinase kinase binding; ISO:MGI.
DR GO; GO:0060090; F:molecular adaptor activity; IDA:BHF-UCL.
DR GO; GO:0051219; F:phosphoprotein binding; ISO:MGI.
DR GO; GO:0046982; F:protein heterodimerization activity; IPI:BHF-UCL.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0019901; F:protein kinase binding; IDA:BHF-UCL.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IDA:BHF-UCL.
DR GO; GO:0097110; F:scaffold protein binding; IPI:BHF-UCL.
DR GO; GO:0000149; F:SNARE binding; ISO:MGI.
DR GO; GO:0019905; F:syntaxin binding; ISO:MGI.
DR GO; GO:0071711; P:basement membrane organization; IMP:MGI.
DR GO; GO:0070836; P:caveola assembly; ISS:UniProtKB.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0008283; P:cell population proliferation; IMP:MGI.
DR GO; GO:0007268; P:chemical synaptic transmission; ISO:MGI.
DR GO; GO:0006897; P:endocytosis; TAS:MGI.
DR GO; GO:0007029; P:endoplasmic reticulum organization; IMP:MGI.
DR GO; GO:0001935; P:endothelial cell proliferation; IMP:MGI.
DR GO; GO:0008286; P:insulin receptor signaling pathway; ISO:MGI.
DR GO; GO:0007005; P:mitochondrion organization; IMP:MGI.
DR GO; GO:0001937; P:negative regulation of endothelial cell proliferation; IMP:MGI.
DR GO; GO:0014859; P:negative regulation of skeletal muscle cell proliferation; IMP:MGI.
DR GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; IGI:MGI.
DR GO; GO:0044794; P:positive regulation by host of viral process; ISO:MGI.
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; IGI:MGI.
DR GO; GO:0043547; P:positive regulation of GTPase activity; ISO:MGI.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; ISO:MGI.
DR GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; ISO:MGI.
DR GO; GO:1900182; P:positive regulation of protein localization to nucleus; ISO:MGI.
DR GO; GO:0019065; P:receptor-mediated endocytosis of virus by host cell; ISO:MGI.
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; IMP:MGI.
DR GO; GO:0048741; P:skeletal muscle fiber development; IMP:MGI.
DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IGI:MGI.
DR GO; GO:0048278; P:vesicle docking; ISS:UniProtKB.
DR GO; GO:0006906; P:vesicle fusion; ISS:UniProtKB.
DR GO; GO:0016050; P:vesicle organization; ISO:MGI.
DR GO; GO:0019076; P:viral release from host cell; ISO:MGI.
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_0000144138"
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:0007744|PubMed:21183079"
FT MOD_RES 20
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 23
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 27
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 36
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P51636"
SQ SEQUENCE 162 AA; 18227 MW; 9E2E272FEC169458 CRC64;
MGLETEKADV QLFMADDAYS HHSGVDYADP EKYVDSSHDR DPHQLNSHLK LGFEDLIAEP
ETTHSFDKVW ICSHALFEIS KYVMYKFLTV FLAIPLAFIA GILFATLSCL HIWILMPFVK
TCLMVLPSVQ TIWKSVTDVV IGPLCTSVGR SFSSVSMQLS HD
