Q9WVC3 (CAV2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Caveolin-2

Gene names

Name:

Cav2

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	162 AA.
Sequence status	Complete.
Protein existence	Evidence 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. Membrane › caveola; 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 component	Cell membrane Cytoplasm Golgi apparatus Membrane Nucleus
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	caveola 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 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: Compara skeletal muscle fiber development Inferred from mutant phenotype PubMed 17200204. Source: MGI synaptic transmission Inferred from electronic annotation. Source: Compara 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_component	Golgi 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: Compara cytosol Inferred from electronic annotation. Source: Compara endoplasmic reticulum part Inferred from sequence orthology PubMed 22792322. Source: MGI extrinsic to internal side of plasma membrane Inferred from sequence or structural similarity PubMed 15569306. Source: UniProtKB integral to plasma membrane Inferred from electronic annotation. Source: Compara lipid particle Inferred from electronic annotation. Source: Compara nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell perinuclear region of cytoplasm Inferred from sequence or structural similarity PubMed 18081315. Source: UniProtKB protein complex Inferred from electronic annotation. Source: Compara transport vesicle Inferred from electronic annotation. Source: Compara
Molecular_function	D1 dopamine receptor binding Inferred from sequence or structural similarity PubMed 15569306. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 162	162	Caveolin-2		PRO_0000144138
Regions
	Topological domain	1 – 86	86	Cytoplasmic Potential
	Intramembrane	87 – 107	21	Helical; Potential
	Topological domain	108 – 162	55	Cytoplasmic Potential
Amino acid modifications
	Modified residue	19	1	Phosphotyrosine; by SRC Ref.5
	Modified residue	23	1	Phosphoserine By similarity
	Modified residue	27	1	Phosphotyrosine; by SRC By similarity
	Modified residue	36	1	Phosphoserine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9WVC3 [UniParc]. Last modified November 1, 1999. Version 1. Checksum: 9E2E272FEC169458	FASTA	162	18,227
	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

References

	« Hide 'large scale' referencesShow '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. , 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.
+	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.
IPI	IPI00125832.
RefSeq	NP_058596.1. NM_016900.3.
UniGene	Mm.396075.
3D structure databases
ProteinModelPortal	Q9WVC3.
ModBase	Search...
Protein-protein interaction databases
STRING	10090.ENSMUSP00000000058.
PTM databases
PhosphoSite	Q9WVC3.
Proteomic databases
PaxDb	Q9WVC3.
PRIDE	Q9WVC3.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000000058; ENSMUSP00000000058; ENSMUSG00000000058.
GeneID	12390.
KEGG	mmu:12390.
UCSC	uc009azn.1. mouse.
Organism-specific databases
CTD	858.
MGI	MGI:107571. Cav2.
Phylogenomic databases
eggNOG	NOG74268.
GeneTree	ENSGT00390000014924.
HOGENOM	HOG000036550.
HOVERGEN	HBG003422.
InParanoid	Q9WVC3.
KO	K12958.
OMA	STHSFDK.
OrthoDB	EOG4PRSRW.
Gene expression databases
ArrayExpress	Q9WVC3.
Bgee	Q9WVC3.
CleanEx	MM_CAV2.
Genevestigator	Q9WVC3.
GermOnline	ENSMUSG00000000058. Mus musculus.
Family and domain databases
InterPro	IPR001612. Caveolin. IPR018361. Caveolin_CS. [Graphical view]
PANTHER	PTHR10844. PTHR10844. 1 hit.
Pfam	PF01146. Caveolin. 1 hit. [Graphical view]
PROSITE	PS01210. CAVEOLIN. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	281126.
SOURCE	Search...

Entry information

Entry name

CAV2_MOUSE

Accession

Primary (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:	May 1, 2013
This is version 94 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program