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 28-JUL-2009, entry version 57. 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. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION. RX MEDLINE=98104125; 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 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 [5] 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). CC -!- FUNCTION: Involved in the targeting and/or fusion of transport CC vesicles to their target membrane. CC -!- SUBUNIT: Interacts with VAPA and VAPB. Part of the SNARE core CC complex containing SNAP25, VAMP2 and STX1A. This complex binds to CC CPLX1 (By similarity). 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; -. DR UniGene; Mm.28643; -. DR SMR; P63044; 25-93. DR DIP; DIP:29065N; -. DR IntAct; P63044; 3. DR Ensembl; ENSMUST00000021273; ENSMUSP00000021273; ENSMUSG00000020894; Mus musculus. DR Ensembl; ENSMUST00000117780; ENSMUSP00000112611; ENSMUSG00000020894; Mus musculus. DR GeneID; 22318; -. DR KEGG; mmu:22318; -. DR UCSC; uc007jpe.1; mouse. DR MGI; MGI:1313277; Vamp2. DR HOGENOM; P63044; -. DR HOVERGEN; P63044; -. DR OMA; P63044; ICVIILI. DR NextBio; 302529; -. DR ArrayExpress; P63044; -. DR Bgee; P63044; -. DR CleanEx; MM_VAMP2; -. DR GermOnline; ENSMUSG00000020894; Mus musculus. DR GO; GO:0030054; C:cell junction; IEA:UniProtKB-SubCell. DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW. DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB. DR GO; GO:0030672; C:synaptic vesicle membrane; IDA:MGI. DR GO; GO:0019717; C:synaptosome; IEA:UniProtKB-SubCell. 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:0000149; F:SNARE binding; IDA:MGI. DR GO; GO:0017156; P:calcium ion-dependent exocytosis; IDA:MGI. DR GO; GO:0006944; P:membrane fusion; IMP:MGI. DR GO; GO:0017157; P:regulation of exocytosis; IDA:MGI. 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 ProDom; PD001229; Synaptobrevin; 1. DR PROSITE; PS00417; SYNAPTOBREVIN; 1. DR PROSITE; PS50892; V_SNARE; 1. PE 1: Evidence at protein level; KW Acetylation; Cell junction; Coiled coil; Cytoplasmic vesicle; KW Direct protein sequencing; Membrane; Phosphoprotein; Synapse; KW Synaptosome; Transmembrane. 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 Anchor for type IV membrane protein FT (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 //