CAV2_DIDVI
ID CAV2_DIDVI Reviewed; 162 AA.
AC Q2QL80;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 25-MAY-2022, entry version 50.
DE RecName: Full=Caveolin-2;
GN Name=CAV2;
OS Didelphis virginiana (North American opossum) (Didelphis marsupialis
OS virginiana).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Metatheria; Didelphimorphia; Didelphidae; Didelphis.
OX NCBI_TaxID=9267;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Antonellis A., Ayele K., Benjamin B., Blakesley R.W., Boakye A.,
RA Bouffard G.G., Brinkley C., Brooks S., Chu G., Coleman H., Engle J.,
RA Gestole M., Greene A., Guan X., Gupta J., Haghighi P., Han J., Hansen N.,
RA Ho S.-L., Hu P., Hunter G., Hurle B., Idol J.R., Kwong P., Laric P.,
RA Larson S., Lee-Lin S.-Q., Legaspi R., Madden M., Maduro Q.L., Maduro V.B.,
RA Margulies E.H., Masiello C., Maskeri B., McDowell J., Mojidi H.A.,
RA Mullikin J.C., Oestreicher J.S., Park M., Portnoy M.E., Prasad A., Puri O.,
RA Reddix-Dugue N., Schandler K., Schueler M.G., Sison C., Stantripop S.,
RA Stephen E., Taye A., Thomas J.W., Thomas P.J., Tsipouri V., Ung L.,
RA Vogt J.L., Wetherby K.D., Young A., Green E.D.;
RT "NISC comparative sequencing initiative.";
RL Submitted (NOV-2005) 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 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 (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 (By similarity). 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. {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 (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 -!- SIMILARITY: Belongs to the caveolin family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DP000023; ABB89829.1; -; Genomic_DNA.
DR AlphaFoldDB; Q2QL80; -.
DR GO; GO:0005901; C:caveola; ISS:UniProtKB.
DR GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; ISS:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
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:0070836; P:caveola assembly; ISS:UniProtKB.
DR GO; GO:0007029; P:endoplasmic reticulum organization; ISS:UniProtKB.
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: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 PANTHER; PTHR10844; PTHR10844; 1.
DR PANTHER; PTHR10844:SF3; PTHR10844:SF3; 1.
DR Pfam; PF01146; Caveolin; 1.
PE 3: Inferred from homology;
KW Cell membrane; Cytoplasm; Golgi apparatus; Membrane; Nucleus;
KW Phosphoprotein.
FT CHAIN 1..162
FT /note="Caveolin-2"
FT /id="PRO_0000226339"
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 REGION 19..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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"
FT MOD_RES 36
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P51636"
SQ SEQUENCE 162 AA; 18141 MW; 3EC4AB8B9367A58C CRC64;
MGLETEKADA QIYMDEDSYS RHSGLGYPEP EKCAKSTQDR DPRGLNTHLK MGFEDVIGEP
ESTHSFDKVW ICSHALFEVS KYLIYKVLTV LLAIPLAFVA GILFATLSCL HIWIVVPFVK
TCLMVLPSVQ TVWHSITDGF IAPLYKSMGL IFSSISLRLS PE
