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Q9WVC3 (CAV2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 104. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Caveolin-2
Gene names
Name:Cav2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length162 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May act as a scaffolding protein within caveolar membranes. Interacts directly with G-protein alpha subunits and can functionally regulate their activity. Acts as an accessory protein in conjunction with CAV1 in targeting to lipid rafts and driving caveolae formation. The Ser-36 phosphorylated form has a role in modulating mitosis in endothelial cells. Positive regulator of cellular mitogenesis of the MAPK signaling pathway. Required for the insulin-stimulated nuclear translocation and activation of MAPK1 and STAT3, and the subsequent regulation of cell cycle progression By similarity.

Subunit structure

Monomer or homodimer. Interacts with CAV1; the interaction forms a stable heterooligomeric complex that is required for targeting to lipid rafts and for caveolae formation. Tyrosine phosphorylated forms do not form heterooligomers with the Tyr-19-phosphorylated form existing as a monomer or dimer, and the Tyr-27-form as a monomer only. Interacts (tyrosine phosphorylated form) with the SH2 domain-containing proteins, RASA1, NCK1 and SRC. Interacts (tyrosine phosphorylated form) with INSR, the interaction (Tyr-27-phosphorylated form) is increased on insulin stimulation. Interacts (Tyr-19 phosphorylated form) with MAPK1 (phosphorylated form); the interaction, promoted by insulin, leads to nuclear location and MAPK1 activation. Interacts with STAT3; the interaction is increased on insulin-induced tyrosine phosphorylation leading to STAT activation By similarity.

Subcellular location

Nucleus. Cytoplasm. Golgi apparatus membrane; Peripheral membrane protein. Cell membrane; Peripheral membrane protein. Membranecaveola; Peripheral membrane protein. Note: Potential hairpin-like structure in the membrane. Membrane protein of caveolae. Tyr-19-phosphorylated form is enriched at sites of cell-cell contact and is translocated to the nucleus in complex with MAPK1 in response to insulin. Tyr-27-phosphorylated form is located both in the cytoplasm and plasma membrane. CAV1-mediated Ser-23-phosphorylated form locates to the plasma membrane. Ser-36-phosphorylated form resides in intracellular compartments By similarity.

Post-translational modification

Phosphorylated on serine and tyrosine residues. CAV1 promotes phosphorylation on Ser-23 which then targets the complex to the plasma membrane, lipid rafts and caveolae. Phosphorylation on Ser-36 appears to modulate mitosis in endothelial cells. Phosphorylation on both Tyr-19 and Tyr-27 is required for insulin-induced 'Ser-727' phosphorylation of STAT3 and its activation. Phosphorylation on Tyr-19 is required for insulin-induced phosphorylation of MAPK1 and DNA binding of STAT3. Tyrosine phosphorylation is induced by both EGF and insulin By similarity. Ref.5

Sequence similarities

Belongs to the caveolin family.

Ontologies

Keywords
   Cellular componentCell membrane
Cytoplasm
Golgi apparatus
Membrane
Nucleus
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcaveola assembly

Inferred from sequence or structural similarity PubMed 12633858. Source: UniProtKB

endocytosis

Traceable author statement Ref.1. Source: MGI

endoplasmic reticulum organization

Inferred from mutant phenotype PubMed 17200204. Source: MGI

mitochondrion organization

Inferred from mutant phenotype PubMed 17200204. Source: MGI

negative regulation of cell proliferation

Inferred from mutant phenotype PubMed 17200204. Source: MGI

negative regulation of endothelial cell proliferation

Inferred from mutant phenotype PubMed 11884617. Source: MGI

negative regulation of transforming growth factor beta receptor signaling pathway

Inferred from genetic interaction PubMed 21832243. Source: MGI

positive regulation of dopamine receptor signaling pathway

Inferred from sequence or structural similarity PubMed 15569306. Source: UniProtKB

positive regulation of endothelial cell proliferation

Inferred from genetic interaction PubMed 21832243. Source: MGI

protein oligomerization

Inferred from direct assay PubMed 11884617. Source: MGI

regulation of mitosis

Inferred from electronic annotation. Source: Ensembl

skeletal muscle fiber development

Inferred from mutant phenotype PubMed 17200204. Source: MGI

synaptic transmission

Inferred from electronic annotation. Source: Ensembl

vesicle docking

Inferred from sequence or structural similarity PubMed 12743374. Source: UniProtKB

vesicle fusion

Inferred from sequence or structural similarity PubMed 12743374. Source: UniProtKB

   Cellular_componentGolgi membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

acrosomal membrane

Inferred from direct assay PubMed 19144954. Source: MGI

caveola

Inferred from sequence or structural similarity PubMed 15703204. Source: UniProtKB

cell surface

Inferred from electronic annotation. Source: Ensembl

cytoplasmic vesicle

Inferred from sequence orthology PubMed 22792322. Source: MGI

cytosol

Inferred from electronic annotation. Source: Ensembl

extrinsic component of cytoplasmic side of plasma membrane

Inferred from sequence or structural similarity PubMed 15569306. Source: UniProtKB

integral component of plasma membrane

Inferred from electronic annotation. Source: Ensembl

lipid particle

Inferred from electronic annotation. Source: Ensembl

membrane

Inferred from direct assay PubMed 11316799. Source: MGI

membrane raft

Inferred from sequence or structural similarity. Source: HGNC

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

perinuclear region of cytoplasm

Inferred from sequence or structural similarity PubMed 18081315. Source: UniProtKB

plasma membrane

Inferred from direct assay PubMed 12138167. Source: MGI

protein complex

Inferred from sequence orthology PubMed 24013648. Source: MGI

transport vesicle

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionD1 dopamine receptor binding

Inferred from sequence or structural similarity PubMed 15569306. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 162162Caveolin-2
PRO_0000144138

Regions

Topological domain1 – 8686Cytoplasmic Potential
Intramembrane87 – 10721Helical; Potential
Topological domain108 – 16255Cytoplasmic Potential

Amino acid modifications

Modified residue191Phosphotyrosine; by SRC Ref.5
Modified residue231Phosphoserine By similarity
Modified residue271Phosphotyrosine; by SRC By similarity
Modified residue361Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9WVC3 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: 9E2E272FEC169458

FASTA16218,227
        10         20         30         40         50         60 
MGLETEKADV QLFMADDAYS HHSGVDYADP EKYVDSSHDR DPHQLNSHLK LGFEDLIAEP 

        70         80         90        100        110        120 
ETTHSFDKVW ICSHALFEIS KYVMYKFLTV FLAIPLAFIA GILFATLSCL HIWILMPFVK 

       130        140        150        160 
TCLMVLPSVQ TIWKSVTDVV IGPLCTSVGR SFSSVSMQLS HD 

« Hide

References

« Hide 'large scale' references
[1]"The membrane-spanning domains of caveolins-1 and -2 mediate the formation of caveolin hetero-oligomers. Implications for the assembly of caveolae membranes in vivo."
Das K., Lewis R.Y., Scherer P.E., Lisanti M.P.
J. Biol. Chem. 274:18721-18728(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: 3T3-L1.
[2]"Identification of mouse caveolin-2 mRNA variant."
Kogo H., Ishiguro K., Kuwaki S., Fujimoto T.
Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Bone marrow, Inner ear, Lung and Tongue.
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: FVB/N.
Tissue: Mammary gland.
[5]"Src-induced phosphorylation of caveolin-2 on tyrosine 19. Phospho-caveolin-2 (Tyr(P)19) is localized near focal adhesions, remains associated with lipid rafts/caveolae, but no longer forms a high molecular mass hetero-oligomer with caveolin-1."
Lee H., Park D.S., Wang X.B., Scherer P.E., Schwartz P.E., Lisanti M.P.
J. Biol. Chem. 277:34556-34567(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT TYR-19.
[6]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF141322 mRNA. Translation: AAD42349.1.
AB049604 mRNA. Translation: BAB61728.1.
AK004663 mRNA. Translation: BAB23453.1.
AK009913 mRNA. Translation: BAB26582.1.
AK151397 mRNA. Translation: BAE30365.1.
AK158419 mRNA. Translation: BAE34498.1.
BC023095 mRNA. Translation: AAH23095.1.
CCDSCCDS19923.1.
RefSeqNP_058596.1. NM_016900.4.
UniGeneMm.396075.

3D structure databases

ProteinModelPortalQ9WVC3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ9WVC3. 1 interaction.
MINTMINT-4089976.
STRING10090.ENSMUSP00000000058.

PTM databases

PhosphoSiteQ9WVC3.

Proteomic databases

MaxQBQ9WVC3.
PaxDbQ9WVC3.
PRIDEQ9WVC3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000000058; ENSMUSP00000000058; ENSMUSG00000000058.
GeneID12390.
KEGGmmu:12390.
UCSCuc009azm.1. mouse.

Organism-specific databases

CTD858.
MGIMGI:107571. Cav2.

Phylogenomic databases

eggNOGNOG74268.
GeneTreeENSGT00390000014924.
HOGENOMHOG000036550.
HOVERGENHBG003422.
InParanoidQ9WVC3.
KOK12958.
OMASTHSFDK.
OrthoDBEOG7V1FSD.
PhylomeDBQ9WVC3.
TreeFamTF315736.

Gene expression databases

ArrayExpressQ9WVC3.
BgeeQ9WVC3.
CleanExMM_CAV2.
GenevestigatorQ9WVC3.

Family and domain databases

InterProIPR001612. Caveolin.
IPR018361. Caveolin_CS.
[Graphical view]
PANTHERPTHR10844. PTHR10844. 1 hit.
PfamPF01146. Caveolin. 1 hit.
[Graphical view]
PROSITEPS01210. CAVEOLIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio281126.
PROQ9WVC3.
SOURCESearch...

Entry information

Entry nameCAV2_MOUSE
AccessionPrimary (citable) accession number: Q9WVC3
Secondary accession number(s): Q3TYR4
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: November 1, 1999
Last modified: July 9, 2014
This is version 104 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot