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Protein

Caveolin-2

Gene

Cav2

Organism
Rattus norvegicus (Rat)
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.2 Publications

GO - Molecular functioni

  • D1 dopamine receptor binding Source: UniProtKB
  • mitogen-activated protein kinase kinase kinase binding Source: BHF-UCL
  • phosphoprotein binding Source: RGD
  • SNARE binding Source: RGD
  • syntaxin binding Source: RGD

GO - Biological processi

  • caveola assembly Source: UniProtKB
  • endoplasmic reticulum organization Source: UniProtKB
  • insulin receptor signaling pathway Source: BHF-UCL
  • mitochondrion organization Source: UniProtKB
  • negative regulation of endothelial cell proliferation Source: UniProtKB
  • positive regulation of dopamine receptor signaling pathway Source: UniProtKB
  • positive regulation of MAPK cascade Source: BHF-UCL
  • positive regulation of peptidyl-tyrosine phosphorylation Source: BHF-UCL
  • positive regulation of protein localization to nucleus Source: BHF-UCL
  • skeletal muscle fiber development Source: UniProtKB
  • synaptic transmission Source: RGD
  • vesicle docking Source: UniProtKB
  • vesicle fusion Source: UniProtKB
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Caveolin-2
Gene namesi
Name:Cav2
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi620348. Cav2.

Subcellular locationi

Topology

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

GO - Cellular componenti

  • caveola Source: UniProtKB
  • cell surface Source: RGD
  • cytoplasm Source: RGD
  • cytosol Source: RGD
  • endoplasmic reticulum Source: RGD
  • extrinsic component of cytoplasmic side of plasma membrane Source: UniProtKB
  • Golgi apparatus Source: BHF-UCL
  • Golgi membrane Source: UniProtKB-SubCell
  • lipid particle Source: RGD
  • membrane raft Source: BHF-UCL
  • nuclear envelope Source: BHF-UCL
  • nuclear inner membrane Source: BHF-UCL
  • perinuclear region of cytoplasm Source: UniProtKB
  • plasma membrane Source: BHF-UCL
  • protein complex Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Golgi apparatus, Membrane, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi19 – 191Y → A: Abolishes phosphorylation, insulin-stimulated interaction with phosphorylated MAPK1, MAPK1 nuclear translocation and activation, reduction of insulin-induced DNA binding of STAT3 but no effect on 'S-727' phosphorylation of STAT3. Completely abolishes phosphorylation, decreases insulin-induced DNA binding and impairs nuclear location of STAT3, inhibits insulin-induced 'S-727' phosphorylation of STAT3, and eliminates binding to RASA1, SRC and NCK1; when associated with A-27. 2 Publications
Mutagenesisi27 – 271Y → A: Abolishes phosphorylation and insulin-induced nuclear location, but no effect on insulin-induced 'S-727' phosphorylation of STAT3 nor on MAPK1 phosphorylation. Completely abolishes insulin-induced phosphorylation, nuclear location, nuclear translocation of MAPK1 and STAT3 and 'S-727' phosphorylation of STAT3 and MAPK1 phosphorylation; when associated with A-19. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 162162Caveolin-2PRO_0000385179Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei19 – 191Phosphotyrosine; by SRC2 Publications
Modified residuei20 – 201PhosphoserineBy similarity
Modified residuei23 – 231PhosphoserineBy similarity
Modified residuei27 – 271Phosphotyrosine; by SRC1 Publication
Modified residuei36 – 361PhosphoserineBy similarity

Post-translational modificationi

Phosphorylated on serine and tyrosine residues. CAV1 promotes phosphorylation on Ser-23 which targets the complex to the plasma membrane, lipid rafts and caveolae. Phosphorylation on Ser-36 appears to modulate mitosis in endothelial cells (By similarity). 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 similarity2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ2IBC5.

PTM databases

iPTMnetiQ2IBC5.

Expressioni

Tissue specificityi

In the retina, mainly expressed in vessels, but also diffuse expression in the inner and outer plexiform layers and in the inner nuclear layer.1 Publication

Interactioni

Subunit structurei

Monomer or homodimer (By similarity). 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 similarity2 Publications

GO - Molecular functioni

  • D1 dopamine receptor binding Source: UniProtKB
  • mitogen-activated protein kinase kinase kinase binding Source: BHF-UCL
  • phosphoprotein binding Source: RGD
  • SNARE binding Source: RGD
  • syntaxin binding Source: RGD

Protein-protein interaction databases

BioGridi264175. 2 interactions.
IntActiQ2IBC5. 1 interaction.
STRINGi10116.ENSRNOP00000008722.

Family & Domainsi

Sequence similaritiesi

Belongs to the caveolin family.Curated

Phylogenomic databases

eggNOGiENOG410IFFB. Eukaryota.
ENOG4111STF. LUCA.
HOGENOMiHOG000036550.
InParanoidiQ2IBC5.
KOiK12958.
OrthoDBiEOG7V1FSD.
PhylomeDBiQ2IBC5.
TreeFamiTF315736.

Family and domain databases

InterProiIPR033306. CAV-2.
IPR001612. Caveolin.
IPR018361. Caveolin_CS.
[Graphical view]
PANTHERiPTHR10844. PTHR10844. 1 hit.
PTHR10844:SF3. PTHR10844:SF3. 1 hit.
PfamiPF01146. Caveolin. 1 hit.
[Graphical view]
PROSITEiPS01210. CAVEOLIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q2IBC5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGLETEKADV QLFMADDAYS HHSVVDYTDP EKYVDSSQDR DPHQLNSHLK
60 70 80 90 100
LGFEDLIAEP PTTHSFDKVW ICSHALFEIS KYVIYKFLTV FLAIPLAFIA
110 120 130 140 150
GILFATLSCL HIWILMPFVK TCLMVLPSVQ TIWKSVTDVV IGPLCTSVGR
160
IFSSVSMQLS HD
Length:162
Mass (Da):18,266
Last modified:September 22, 2009 - v2
Checksum:i7F8423C6B42F2F55
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti28 – 281T → A in AAR16307 (PubMed:12917688).Curated
Sequence conflicti29 – 291D → G in AAL33581 (PubMed:11883949).Curated
Sequence conflicti124 – 1241M → V in AAL33581 (PubMed:11883949).Curated
Sequence conflicti162 – 1621D → N in AAL33581 (PubMed:11883949).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF439780 mRNA. Translation: AAL33581.1.
DP000027 Genomic DNA. Translation: AAR16307.1.
BC062059 mRNA. Translation: AAH62059.1.
RefSeqiNP_571989.2. NM_131914.2.
UniGeneiRn.81070.

Genome annotation databases

GeneIDi363425.
KEGGirno:363425.
UCSCiRGD:620348. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF439780 mRNA. Translation: AAL33581.1.
DP000027 Genomic DNA. Translation: AAR16307.1.
BC062059 mRNA. Translation: AAH62059.1.
RefSeqiNP_571989.2. NM_131914.2.
UniGeneiRn.81070.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi264175. 2 interactions.
IntActiQ2IBC5. 1 interaction.
STRINGi10116.ENSRNOP00000008722.

PTM databases

iPTMnetiQ2IBC5.

Proteomic databases

PaxDbiQ2IBC5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi363425.
KEGGirno:363425.
UCSCiRGD:620348. rat.

Organism-specific databases

CTDi858.
RGDi620348. Cav2.

Phylogenomic databases

eggNOGiENOG410IFFB. Eukaryota.
ENOG4111STF. LUCA.
HOGENOMiHOG000036550.
InParanoidiQ2IBC5.
KOiK12958.
OrthoDBiEOG7V1FSD.
PhylomeDBiQ2IBC5.
TreeFamiTF315736.

Miscellaneous databases

NextBioi683298.
PROiQ2IBC5.

Family and domain databases

InterProiIPR033306. CAV-2.
IPR001612. Caveolin.
IPR018361. Caveolin_CS.
[Graphical view]
PANTHERiPTHR10844. PTHR10844. 1 hit.
PTHR10844:SF3. PTHR10844:SF3. 1 hit.
PfamiPF01146. Caveolin. 1 hit.
[Graphical view]
PROSITEiPS01210. CAVEOLIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "ATP dependence of the SNARE/caveolin 1 interaction in the hippocampus."
    Magga J.M., Kay J.G., Davy A., Poulton N.P., Robbins S.M., Braun J.E.A.
    Biochem. Biophys. Res. Commun. 291:1232-1238(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Sprague-Dawley.
  2. "Comparative analyses of multi-species sequences from targeted genomic regions."
    Thomas J.W., Touchman J.W., Blakesley R.W., Bouffard G.G., Beckstrom-Sternberg S.M., Margulies E.H., Blanchette M., Siepel A.C., Thomas P.J., McDowell J.C., Maskeri B., Hansen N.F., Schwartz M.S., Weber R.J., Kent W.J., Karolchik D., Bruen T.C., Bevan R.
    , Cutler D.J., Schwartz S., Elnitski L., Idol J.R., Prasad A.B., Lee-Lin S.-Q., Maduro V.V.B., Summers T.J., Portnoy M.E., Dietrich N.L., Akhter N., Ayele K., Benjamin B., Cariaga K., Brinkley C.P., Brooks S.Y., Granite S., Guan X., Gupta J., Haghighi P., Ho S.-L., Huang M.C., Karlins E., Laric P.L., Legaspi R., Lim M.J., Maduro Q.L., Masiello C.A., Mastrian S.D., McCloskey J.C., Pearson R., Stantripop S., Tiongson E.E., Tran J.T., Tsurgeon C., Vogt J.L., Walker M.A., Wetherby K.D., Wiggins L.S., Young A.C., Zhang L.-H., Osoegawa K., Zhu B., Zhao B., Shu C.L., De Jong P.J., Lawrence C.E., Smit A.F., Chakravarti A., Haussler D., Green P., Miller W., Green E.D.
    Nature 424:788-793(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "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].
    Tissue: Prostate.
  4. "Immunohistochemical study of caveolin-1 and -2 in the rat retina."
    Kim H., Lee T., Lee J., Ahn M., Moon C., Wie M.B., Shin T.
    J. Vet. Sci. 7:101-104(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  5. "Identification of pY19-caveolin-2 as a positive regulator of insulin-stimulated actin cytoskeleton-dependent mitogenesis."
    Kwon H., Jeong K., Pak Y.
    J. Cell. Mol. Med. 13:1549-1564(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT TYR-19, INTERACTION WITH MAPK1 AND INSR, FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF TYR-19.
  6. "Caveolin-2 regulation of STAT3 transcriptional activation in response to insulin."
    Kwon H., Jeong K., Hwang E.M., Park J.-Y., Hong S.-G., Choi W.-S., Pak Y.
    Biochim. Biophys. Acta 1793:1325-1333(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT TYR-19 AND TYR-27, INTERACTION WITH MAPK1 AND STAT3, FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF TYR-19 AND TYR-27.

Entry informationi

Entry nameiCAV2_RAT
AccessioniPrimary (citable) accession number: Q2IBC5
Secondary accession number(s): Q6P6R8, Q8VIK7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: September 22, 2009
Last modified: May 11, 2016
This is version 72 of the entry and version 2 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. SIMILARITY comments
    Index of protein domains and families

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 one 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.