CAV2_CANLF
ID CAV2_CANLF Reviewed; 162 AA.
AC O46550; A0M8U7;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 2.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Caveolin-2;
GN Name=CAV2; Synonyms=CAV-2;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ALPHA AND BETA), PROTEIN SEQUENCE OF
RP 24-32 AND 152-159, PHOSPHORYLATION, INTERACTION WITH CAV1, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=Cocker spaniel; TISSUE=Kidney;
RX PubMed=9472032; DOI=10.1083/jcb.140.4.795;
RA Scheiffele P., Verkade P., Fra A.M., Sweet-Virta H., Simons K., Ikonen E.;
RT "Caveolin-1 and -2 in the exocytic pathway of MDCK cells.";
RL J. Cell Biol. 140:795-806(1998).
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).
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}. Cytoplasm {ECO:0000250}.
CC Golgi apparatus membrane {ECO:0000269|PubMed:9472032}; Peripheral
CC membrane protein {ECO:0000269|PubMed:9472032}. Cell membrane
CC {ECO:0000269|PubMed:9472032}; Peripheral membrane protein
CC {ECO:0000269|PubMed:9472032}. Membrane, caveola
CC {ECO:0000269|PubMed:9472032}; Peripheral membrane protein
CC {ECO:0000269|PubMed:9472032}. 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. CAV1-mediated
CC Ser-23-phosphorylated form locates to the plasma membrane. Ser-36-
CC phosphorylated form resides in intracellular compartments (By
CC similarity). {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=Alpha;
CC IsoId=O46550-1; Sequence=Displayed;
CC Name=Beta;
CC IsoId=O46550-2; Sequence=VSP_038113;
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 -!- MISCELLANEOUS: [Isoform Alpha]: Most abundant form.
CC -!- SIMILARITY: Belongs to the caveolin family. {ECO:0000305}.
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DR EMBL; AF039223; AAB92672.1; -; mRNA.
DR EMBL; DP000236; AAR16265.1; -; Genomic_DNA.
DR RefSeq; NP_001010997.2; NM_001010997.3. [O46550-1]
DR AlphaFoldDB; O46550; -.
DR BioGRID; 141021; 1.
DR STRING; 9615.ENSCAFP00000038932; -.
DR PaxDb; O46550; -.
DR PRIDE; O46550; -.
DR Ensembl; ENSCAFT00030013808; ENSCAFP00030012051; ENSCAFG00030007499. [O46550-1]
DR Ensembl; ENSCAFT00040030363; ENSCAFP00040026462; ENSCAFG00040016417. [O46550-1]
DR Ensembl; ENSCAFT00845012023; ENSCAFP00845009384; ENSCAFG00845006745. [O46550-1]
DR GeneID; 475294; -.
DR KEGG; cfa:475294; -.
DR CTD; 858; -.
DR VEuPathDB; HostDB:ENSCAFG00845006745; -.
DR eggNOG; ENOG502RZYX; Eukaryota.
DR GeneTree; ENSGT00950000183006; -.
DR HOGENOM; CLU_102582_2_0_1; -.
DR InParanoid; O46550; -.
DR OrthoDB; 1468974at2759; -.
DR Reactome; R-CFA-9009391; Extra-nuclear estrogen signaling.
DR Proteomes; UP000002254; Chromosome 14.
DR Bgee; ENSCAFG00000003402; Expressed in keratinocyte and 46 other tissues.
DR GO; GO:0005901; C:caveola; ISS:UniProtKB.
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: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:0031748; F:D1 dopamine receptor binding; ISS:UniProtKB.
DR GO; GO:0060090; F:molecular adaptor activity; IBA:GO_Central.
DR GO; GO:0019901; F:protein kinase binding; IBA:GO_Central.
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: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:0060161; P:positive regulation of dopamine receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; IBA:GO_Central.
DR GO; GO:0051480; P:regulation of cytosolic calcium ion concentration; IBA:GO_Central.
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 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; Cell membrane; Cytoplasm;
KW Direct protein sequencing; Golgi apparatus; Membrane; Nucleus;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..162
FT /note="Caveolin-2"
FT /id="PRO_0000144137"
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 36
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P51636"
FT VAR_SEQ 1..13
FT /note="Missing (in isoform Beta)"
FT /evidence="ECO:0000303|PubMed:9472032"
FT /id="VSP_038113"
FT CONFLICT 21
FT /note="R -> H (in Ref. 1; AAB92672)"
FT /evidence="ECO:0000305"
FT CONFLICT 59..60
FT /note="EP -> DA (in Ref. 1; AAB92672)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 162 AA; 17931 MW; 7E7881542BAFB2B6 CRC64;
MGLETEKADV QLCMDDDAYS RHSAVDFGDL EQLADSGSDR DPRRLNSHLQ VGFEDVIAEP
VSTHSFDKVW ICSHALFEVS KYVIYKFLTL LLAMPMAFAA GVLFATLSCL HIWIIMPFVK
TCLMVLPSVQ TIWKSVTDAV IAPLCSSVGR SFSSVSLQVS HD
