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UniProtKB/Swiss-Prot entry P63044


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name VAMP2_MOUSE
Primary accession number P63044
Secondary accession number Q64357
Integrated into Swiss-Prot on August 31, 2004
Sequence was last modified on January 23, 2007 (Sequence version 2)
Annotations were last modified on    June 16, 2009 (Entry version 56)
Name and origin of the protein
Protein name Vesicle-associated membrane protein 2
Synonyms VAMP-2
Synaptobrevin-2
Gene name
Name: Vamp2
Synonyms: Syb2
From
Mus musculus (Mouse) [TaxID: 10090] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae; Murinae; Mus.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
DOI=10.1074/jbc.273.3.1444; PubMed=9430681 [NCBI, ExPASy, EBI, Israel, Japan]
Martin L.B., Shewan A., Millar C.A., Gould G.W., James D.E.;
"Vesicle-associated membrane protein 2 plays a specific role in the insulin-dependent trafficking of the facilitative glucose transporter GLUT4 in 3T3-L1 adipocytes.";
J. Biol. Chem. 273:1444-1452(1998).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J;
TISSUE=Brain;
DOI=10.1126/science.1112014; PubMed=16141072 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
PROTEIN SEQUENCE OF 31-47 AND 60-83, AND MASS SPECTROMETRY.
STRAIN=C57BL/6;
TISSUE=Brain;
Lubec G., Kang S.U.;
Submitted (APR-2007) to UniProtKB.
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-75, AND MASS SPECTROMETRY.
TISSUE=Brain cortex;
DOI=10.1074/mcp.M600046-MCP200; PubMed=17114649 [NCBI, ExPASy, EBI, Israel, Japan]
Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F., Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
"Qualitative and quantitative analyses of protein phosphorylation in naive and stimulated mouse synaptosomal preparations.";
Mol. Cell. Proteomics 6:283-293(2007).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
U60150; AAB03463.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK090178; BAC41125.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC055105; AAH55105.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00229703; -.
RefSeq NP_033523.1; -.
UniGene Mm.28643
3D structure databases
SMR P63044; 25-93.
ModBase P63044.
Protein-protein interaction databases
DIP DIP:29065N; -.
IntAct P63044; 3.
Organism-specific databases
MGI MGI:1313277; Vamp2.
Gene expression databases
ArrayExpress P63044; -.
Bgee P63044; -.
CleanEx MM_VAMP2; -.
GermOnline ENSMUSG00000020894; Mus musculus.
Ontologies
GO
GO:0030054; Cellular component: cell junction (inferred from electronic annotation from UniProtKB-SubCell).
GO:0016021; Cellular component: integral to membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0048471; Cellular component: perinuclear region of cytoplasm (inferred from direct assay from UniProtKB).
GO:0030672; Cellular component: synaptic vesicle membrane (inferred from direct assay from MGI).
GO:0019717; Cellular component: synaptosome (inferred from electronic annotation from UniProtKB-SubCell).
GO:0005802; Cellular component: trans-Golgi network (inferred from direct assay from UniProtKB).
GO:0042589; Cellular component: zymogen granule membrane (inferred from direct assay from MGI).
GO:0005516; Molecular function: calmodulin binding (inferred from direct assay from MGI).
GO:0005543; Molecular function: phospholipid binding (inferred from direct assay from MGI).
GO:0000149; Molecular function: SNARE binding (inferred from direct assay from MGI).
GO:0017156; Biological process: calcium ion-dependent exocytosis (inferred from direct assay from MGI).
GO:0006944; Biological process: membrane fusion (inferred from mutant phenotype from MGI).
GO:0017157; Biological process: regulation of exocytosis (inferred from direct assay from MGI).
GO:0016079; Biological process: synaptic vesicle exocytosis (inferred from mutant phenotype from MGI).
QuickGo view.
Family and domain databases
InterPro IPR001388; Synaptobrevin.
IPR016444; Synaptobrevin_met/fun.
Graphical view of domain structure.
Pfam PF00957; Synaptobrevin; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF005409; Synaptobrevin_euk; 1.
PRINTS PR00219; SYNAPTOBREVN.
ProDom PD001229; Synaptobrevin; 1.
[Domain structure / List of seq. sharing at least 1 domain]
PROSITE PS00417; SYNAPTOBREVIN; 1.
PS50892; V_SNARE; 1.
PROSITE graphical view of domain structure (profiles).
Genome annotation databases
Ensembl ENSMUSG00000020894; Mus musculus. [Contig view]
GeneID 22318; -.
KEGG mmu:22318; -.
Phylogenomic databases
HOGENOM P63044; -.
HOVERGEN P63044; -.
OMA P63044; ICVIILI.
Other
NextBio 302529; -.
SOURCE Vamp2; Mus musculus.
ProtoNet P63044.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Acetylation; Cell junction; Coiled coil; Cytoplasmic vesicle; Direct protein sequencing; Membrane; Phosphoprotein; Synapse; Synaptosome; Transmembrane.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed (By similarity). 
CHAIN   2   116  115     Vesicle-associated membrane protein 2. PRO_0000206725
TOPO_DOM   2    94  93     Cytoplasmic (Potential). 
TRANSMEM   95   114  20     Anchor for type IV membrane protein (Potential). 
TOPO_DOM   115   116  2     Vesicular (Potential). 
DOMAIN   31    91  61     v-SNARE coiled-coil homology. 
MOD_RES   2     2        N-acetylserine (By similarity). 
MOD_RES   75    75        Phosphoserine. 
Sequence information
Length: 116 AA [This is the length of the unprocessed precursor] Molecular weight: 12691 Da [This is the MW of the unprocessed precursor] CRC64: 4A0D0D56B5409D0A [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSATAATVPP AAPAGEGGPP APPPNLTSNR RLQQTQAQVD EVVDIMRVNV DKVLERDQKL 

        70         80         90        100        110 
SELDDRADAL QAGASQFETS AAKLKRKYWW KNLKMMIILG VICAIILIII IVYFST 

P63044 in FASTA format

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Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
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