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Protein

Caveolin-2

Gene

Cav2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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).By similarity

GO - Molecular functioni

  1. D1 dopamine receptor binding Source: UniProtKB
  2. protein binding, bridging Source: BHF-UCL
  3. protein complex scaffold Source: BHF-UCL
  4. protein heterodimerization activity Source: BHF-UCL
  5. protein homodimerization activity Source: MGI
  6. protein kinase binding Source: BHF-UCL
  7. scaffold protein binding Source: BHF-UCL

GO - Biological processi

  1. caveola assembly Source: UniProtKB
  2. endocytosis Source: MGI
  3. endoplasmic reticulum organization Source: MGI
  4. insulin receptor signaling pathway Source: MGI
  5. mitochondrion organization Source: MGI
  6. negative regulation of cell proliferation Source: MGI
  7. negative regulation of endothelial cell proliferation Source: MGI
  8. negative regulation of transforming growth factor beta receptor signaling pathway Source: MGI
  9. positive regulation of dopamine receptor signaling pathway Source: UniProtKB
  10. positive regulation of endothelial cell proliferation Source: MGI
  11. positive regulation of GTPase activity Source: MGI
  12. positive regulation of MAPK cascade Source: MGI
  13. protein oligomerization Source: MGI
  14. regulation of mitotic nuclear division Source: Ensembl
  15. skeletal muscle fiber development Source: MGI
  16. vesicle docking Source: UniProtKB
  17. vesicle fusion Source: UniProtKB
  18. vesicle organization Source: MGI
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Caveolin-2
Gene namesi
Name:Cav2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 6

Organism-specific databases

MGIiMGI:107571. Cav2.

Subcellular locationi

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).By similarity

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 8686CytoplasmicSequence AnalysisAdd
BLAST
Intramembranei87 – 10721HelicalSequence AnalysisAdd
BLAST
Topological domaini108 – 16255CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. acrosomal membrane Source: MGI
  2. caveola Source: UniProtKB
  3. cytoplasmic vesicle Source: MGI
  4. extrinsic component of cytoplasmic side of plasma membrane Source: UniProtKB
  5. Golgi membrane Source: UniProtKB-SubCell
  6. integral component of plasma membrane Source: MGI
  7. intracellular Source: MGI
  8. membrane Source: MGI
  9. membrane raft Source: HGNC
  10. nucleus Source: UniProtKB-SubCell
  11. perinuclear region of cytoplasm Source: UniProtKB
  12. plasma membrane Source: MGI
  13. protein complex Source: BHF-UCL
  14. transport vesicle Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Golgi apparatus, Membrane, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 162162Caveolin-2PRO_0000144138Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei19 – 191Phosphotyrosine; by SRC1 Publication
Modified residuei23 – 231PhosphoserineBy similarity
Modified residuei27 – 271Phosphotyrosine; by SRCBy similarity
Modified residuei36 – 361PhosphoserineBy similarity

Post-translational modificationi

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).By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9WVC3.
PaxDbiQ9WVC3.
PRIDEiQ9WVC3.

PTM databases

PhosphoSiteiQ9WVC3.

Expressioni

Gene expression databases

BgeeiQ9WVC3.
CleanExiMM_CAV2.
ExpressionAtlasiQ9WVC3. baseline and differential.
GenevestigatoriQ9WVC3.

Interactioni

Subunit structurei

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).By similarity

Protein-protein interaction databases

IntActiQ9WVC3. 1 interaction.
MINTiMINT-4089976.
STRINGi10090.ENSMUSP00000000058.

Structurei

3D structure databases

ProteinModelPortaliQ9WVC3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the caveolin family.Curated

Phylogenomic databases

eggNOGiNOG74268.
GeneTreeiENSGT00390000014924.
HOGENOMiHOG000036550.
HOVERGENiHBG003422.
InParanoidiQ9WVC3.
KOiK12958.
OMAiSTHSFDK.
OrthoDBiEOG7V1FSD.
PhylomeDBiQ9WVC3.
TreeFamiTF315736.

Family and domain databases

InterProiIPR001612. Caveolin.
IPR018361. Caveolin_CS.
[Graphical view]
PANTHERiPTHR10844. PTHR10844. 1 hit.
PfamiPF01146. Caveolin. 1 hit.
[Graphical view]
PROSITEiPS01210. CAVEOLIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9WVC3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGLETEKADV QLFMADDAYS HHSGVDYADP EKYVDSSHDR DPHQLNSHLK
60 70 80 90 100
LGFEDLIAEP ETTHSFDKVW ICSHALFEIS KYVMYKFLTV FLAIPLAFIA
110 120 130 140 150
GILFATLSCL HIWILMPFVK TCLMVLPSVQ TIWKSVTDVV IGPLCTSVGR
160
SFSSVSMQLS HD
Length:162
Mass (Da):18,227
Last modified:October 31, 1999 - v1
Checksum:i9E2E272FEC169458
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS19923.1.
RefSeqiNP_058596.1. NM_016900.4.
UniGeneiMm.396075.

Genome annotation databases

EnsembliENSMUST00000000058; ENSMUSP00000000058; ENSMUSG00000000058.
GeneIDi12390.
KEGGimmu:12390.
UCSCiuc009azm.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS19923.1.
RefSeqiNP_058596.1. NM_016900.4.
UniGeneiMm.396075.

3D structure databases

ProteinModelPortaliQ9WVC3.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9WVC3. 1 interaction.
MINTiMINT-4089976.
STRINGi10090.ENSMUSP00000000058.

PTM databases

PhosphoSiteiQ9WVC3.

Proteomic databases

MaxQBiQ9WVC3.
PaxDbiQ9WVC3.
PRIDEiQ9WVC3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000000058; ENSMUSP00000000058; ENSMUSG00000000058.
GeneIDi12390.
KEGGimmu:12390.
UCSCiuc009azm.1. mouse.

Organism-specific databases

CTDi858.
MGIiMGI:107571. Cav2.

Phylogenomic databases

eggNOGiNOG74268.
GeneTreeiENSGT00390000014924.
HOGENOMiHOG000036550.
HOVERGENiHBG003422.
InParanoidiQ9WVC3.
KOiK12958.
OMAiSTHSFDK.
OrthoDBiEOG7V1FSD.
PhylomeDBiQ9WVC3.
TreeFamiTF315736.

Miscellaneous databases

NextBioi281126.
PROiQ9WVC3.
SOURCEiSearch...

Gene expression databases

BgeeiQ9WVC3.
CleanExiMM_CAV2.
ExpressionAtlasiQ9WVC3. baseline and differential.
GenevestigatoriQ9WVC3.

Family and domain databases

InterProiIPR001612. Caveolin.
IPR018361. Caveolin_CS.
[Graphical view]
PANTHERiPTHR10844. PTHR10844. 1 hit.
PfamiPF01146. Caveolin. 1 hit.
[Graphical view]
PROSITEiPS01210. CAVEOLIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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(1998) [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 (SEP-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.
    , 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(2004) [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(2003) [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(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT TYR-19.
  6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiCAV2_MOUSE
AccessioniPrimary (citable) accession number: Q9WVC3
Secondary accession number(s): Q3TYR4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 30, 2000
Last sequence update: October 31, 1999
Last modified: March 31, 2015
This is version 110 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.