ID VAMP2_MOUSE STANDARD; PRT; 115 AA. AC P63044; Q64357; DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot. DT 31-AUG-2004, sequence version 1. DT 04-APR-2006, entry version 19. DE Vesicle-associated membrane protein 2 (VAMP-2) (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 Schonbach 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 MEDLINE=22388257; PubMed=12477932; DOI=10.1073/pnas.242603899; RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G., RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D., RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K., RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F., RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L., RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E., RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C., RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J., RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H., RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W., RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A., RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A., RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G., RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C., RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M., RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E., RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.; RT "Generation and initial analysis of more than 15,000 full-length human RT and mouse cDNA sequences."; RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002). 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: Type IV membrane protein. 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 UniGene; Mm.28643; -. DR SMR; P63044; 24-92. DR IntAct; P63044; -. DR MGI; MGI:1313277; Vamp2. DR GO; GO:0016021; C:integral to membrane; RCA. DR GO; GO:0030141; C:secretory granule; IDA. DR GO; GO:0030672; C:synaptic vesicle membrane; IDA. DR GO; GO:0042589; C:zymogen granule membrane; IDA. DR GO; GO:0005516; F:calmodulin binding; IDA. DR GO; GO:0005543; F:phospholipid binding; IDA. DR GO; GO:0000149; F:SNARE binding; IDA. DR GO; GO:0017156; P:calcium ion-dependent exocytosis; IDA. DR GO; GO:0017157; P:regulation of exocytosis; IDA. DR GO; GO:0016079; P:synaptic vesicle exocytosis; IMP. DR InterPro; IPR001388; Synaptobrevin. DR Pfam; PF00957; Synaptobrevin; 1. DR PRINTS; PR00219; SYNAPTOBREVN. DR PROSITE; PS00417; SYNAPTOBREVIN; 1. DR PROSITE; PS50892; V_SNARE; 1. KW Acetylation; Coiled coil; Membrane; Synapse; Synaptosome; KW Transmembrane. FT INIT_MET 0 0 By similarity. FT CHAIN 1 115 Vesicle-associated membrane protein 2. FT /FTId=PRO_0000206725. FT TOPO_DOM 1 93 Cytoplasmic (Potential). FT TRANSMEM 94 113 Anchor for type IV membrane protein FT (Potential). FT TOPO_DOM 114 115 Vesicular (Potential). FT DOMAIN 30 90 v-SNARE coiled-coil homology. FT MOD_RES 1 1 N-acetylserine (By similarity). SQ SEQUENCE 115 AA; 12560 MW; EA400D6291ABF0BC CRC64; SATAATVPPA APAGEGGPPA PPPNLTSNRR LQQTQAQVDE VVDIMRVNVD KVLERDQKLS ELDDRADALQ AGASQFETSA AKLKRKYWWK NLKMMIILGV ICAIILIIII VYFST //