ID VAMP2_MOUSE Reviewed; 116 AA. AC P63044; Q64357; DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 24-JUL-2013, entry version 94. DE RecName: Full=Vesicle-associated membrane protein 2; DE Short=VAMP-2; DE AltName: Full=Synaptobrevin-2; GN Name=Vamp2; Synonyms=Syb2; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION. RX PubMed=9430681; DOI=10.1074/jbc.273.3.1444; RA Martin L.B., Shewan A., Millar C.A., Gould G.W., James D.E.; RT "Vesicle-associated membrane protein 2 plays a specific role in the RT insulin-dependent trafficking of the facilitative glucose transporter RT GLUT4 in 3T3-L1 adipocytes."; RL J. Biol. Chem. 273:1444-1452(1998). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Brain; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP INTERACTION WITH STX4. RX PubMed=17548353; DOI=10.1074/jbc.M701661200; RA Ke B., Oh E., Thurmond D.C.; RT "Doc2beta is a novel Munc18c-interacting partner and positive effector RT of syntaxin 4-mediated exocytosis."; RL J. Biol. Chem. 282:21786-21797(2007). RN [5] RP PROTEIN SEQUENCE OF 31-47 AND 60-83, AND MASS SPECTROMETRY. RC STRAIN=C57BL/6; TISSUE=Brain; RA Lubec G., Kang S.U.; RL Submitted (APR-2007) to UniProtKB. RN [6] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-75, AND MASS RP SPECTROMETRY. RC TISSUE=Brain cortex; RX PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200; RA Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F., RA Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., RA Gerrits B., Panse C., Schlapbach R., Mansuy I.M.; RT "Qualitative and quantitative analyses of protein phosphorylation in RT naive and stimulated mouse synaptosomal preparations."; RL Mol. Cell. Proteomics 6:283-293(2007). RN [7] RP INTERACTION WITH BVES. RX PubMed=20057356; DOI=10.1038/emboj.2009.379; RA Hager H.A., Roberts R.J., Cross E.E., Proux-Gillardeaux V., RA Bader D.M.; RT "Identification of a novel Bves function: regulation of vesicular RT transport."; RL EMBO J. 29:532-545(2010). CC -!- FUNCTION: Involved in the targeting and/or fusion of transport CC vesicles to their target membrane. CC -!- SUBUNIT: Part of the SNARE core complex containing SNAP25, VAMP2 CC and STX1A. This complex binds to CPLX1. Interacts with VAPA and CC VAPB (By similarity). Interacts with BVES and STX4. CC -!- INTERACTION: CC P60766:Cdc42; NbExp=2; IntAct=EBI-521920, EBI-81763; CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, CC synaptic vesicle membrane; Single-pass type IV membrane protein. CC Cell junction, synapse, synaptosome. Note=Neuronal synaptic CC vesicles. CC -!- SIMILARITY: Belongs to the synaptobrevin family. CC -!- SIMILARITY: Contains 1 v-SNARE coiled-coil homology domain. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U60150; AAB03463.1; -; mRNA. DR EMBL; AK090178; BAC41125.1; -; mRNA. DR EMBL; BC055105; AAH55105.1; -; mRNA. DR IPI; IPI00229703; -. DR RefSeq; NP_033523.1; NM_009497.3. DR UniGene; Mm.28643; -. DR ProteinModelPortal; P63044; -. DR SMR; P63044; 30-116. DR DIP; DIP-29065N; -. DR IntAct; P63044; 6. DR MINT; MINT-2411573; -. DR PhosphoSite; P63044; -. DR PaxDb; P63044; -. DR PRIDE; P63044; -. DR Ensembl; ENSMUST00000021273; ENSMUSP00000021273; ENSMUSG00000020894. DR GeneID; 22318; -. DR KEGG; mmu:22318; -. DR UCSC; uc007jpe.1; mouse. DR CTD; 6844; -. DR MGI; MGI:1313277; Vamp2. DR eggNOG; NOG266115; -. DR HOGENOM; HOG000042711; -. DR HOVERGEN; HBG006675; -. DR KO; K13504; -. DR OrthoDB; EOG43JC6B; -. DR Reactome; REACT_112621; Metabolism. DR Reactome; REACT_147847; Translocation of Glut4 to the Plasma Membrane. DR Reactome; REACT_88307; Membrane Trafficking. DR ChiTaRS; VAMP2; mouse. DR NextBio; 302529; -. DR ArrayExpress; P63044; -. DR Bgee; P63044; -. DR CleanEx; MM_VAMP2; -. DR Genevestigator; P63044; -. DR GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW. DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW. DR GO; GO:0043005; C:neuron projection; IEA:UniProtKB-SubCell. DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB. DR GO; GO:0005886; C:plasma membrane; IDA:MGI. DR GO; GO:0030672; C:synaptic vesicle membrane; IDA:MGI. DR GO; GO:0070044; C:synaptobrevin 2-SNAP-25-syntaxin-1a complex; IDA:MGI. DR GO; GO:0070032; C:synaptobrevin 2-SNAP-25-syntaxin-1a-complexin I complex; ISO:MGI. DR GO; GO:0005802; C:trans-Golgi network; IDA:UniProtKB. DR GO; GO:0042589; C:zymogen granule membrane; IDA:MGI. DR GO; GO:0005516; F:calmodulin binding; IDA:MGI. DR GO; GO:0005543; F:phospholipid binding; IDA:MGI. DR GO; GO:0017075; F:syntaxin-1 binding; ISO:MGI. DR GO; GO:0017156; P:calcium ion-dependent exocytosis; IDA:MGI. DR GO; GO:0006944; P:cellular membrane fusion; IMP:MGI. DR GO; GO:0032869; P:cellular response to insulin stimulus; IDA:MGI. DR GO; GO:0043001; P:Golgi to plasma membrane protein transport; IMP:MGI. DR GO; GO:0090316; P:positive regulation of intracellular protein transport; IMP:MGI. DR GO; GO:0006461; P:protein complex assembly; IEA:Compara. DR GO; GO:0017157; P:regulation of exocytosis; IDA:MGI. DR GO; GO:0009749; P:response to glucose stimulus; IEA:Compara. DR GO; GO:0016079; P:synaptic vesicle exocytosis; IMP:MGI. DR InterPro; IPR001388; Synaptobrevin. DR InterPro; IPR016444; Synaptobrevin_met/fun. DR Pfam; PF00957; Synaptobrevin; 1. DR PIRSF; PIRSF005409; Synaptobrevin_euk; 1. DR PRINTS; PR00219; SYNAPTOBREVN. DR PROSITE; PS00417; SYNAPTOBREVIN; 1. DR PROSITE; PS50892; V_SNARE; 1. PE 1: Evidence at protein level; KW Acetylation; Cell junction; Coiled coil; Complete proteome; KW Cytoplasmic vesicle; Direct protein sequencing; Membrane; KW Phosphoprotein; Reference proteome; Synapse; Synaptosome; KW Transmembrane; Transmembrane helix. FT INIT_MET 1 1 Removed (By similarity). FT CHAIN 2 116 Vesicle-associated membrane protein 2. FT /FTId=PRO_0000206725. FT TOPO_DOM 2 94 Cytoplasmic (Potential). FT TRANSMEM 95 114 Helical; Anchor for type IV membrane FT protein; (Potential). FT TOPO_DOM 115 116 Vesicular (Potential). FT DOMAIN 31 91 v-SNARE coiled-coil homology. FT MOD_RES 2 2 N-acetylserine (By similarity). FT MOD_RES 75 75 Phosphoserine. SQ SEQUENCE 116 AA; 12691 MW; 4A0D0D56B5409D0A CRC64; MSATAATVPP AAPAGEGGPP APPPNLTSNR RLQQTQAQVD EVVDIMRVNV DKVLERDQKL SELDDRADAL QAGASQFETS AAKLKRKYWW KNLKMMIILG VICAIILIII IVYFST //