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 08-JUN-2016, entry version 125. 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 PROTEIN SEQUENCE OF 31-47 AND 60-83, AND IDENTIFICATION BY MASS RP SPECTROMETRY. RC STRAIN=C57BL/6J; TISSUE=Brain; RA Lubec G., Kang S.U.; RL Submitted (APR-2007) to UniProtKB. RN [5] RP INTERACTION WITH WDFY2; PRKCZ AND PRKCI, AND COMPLEX FORMATION WITH RP WDFY2 AND PRKCZ. RX PubMed=17313651; DOI=10.1111/j.1742-4658.2007.05702.x; RA Fritzius T., Frey A.D., Schweneker M., Mayer D., Moelling K.; RT "WD-repeat-propeller-FYVE protein, ProF, binds VAMP2 and protein RT kinase Czeta."; RL FEBS J. 274:1552-1566(2007). RN [6] 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 [7] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, and RC Testis; RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and RT expression."; RL Cell 143:1174-1189(2010). RN [8] 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 (PubMed:9430681). Modulates the CC gating characteristics of the delayed rectifier voltage-dependent CC potassium channel KCNB1 (By similarity). CC {ECO:0000250|UniProtKB:P63045, ECO:0000269|PubMed:9430681}. CC -!- SUBUNIT: Interacts (via N-terminus) with KCNB1 (via N-terminus and CC C-terminus); stimulates the channel inactivation rate of KCNB1 (By CC similarity). Part of the SNARE core complex containing SNAP25, CC VAMP2 and STX1A. This complex binds to CPLX1. Interacts with VAPA CC and VAPB (By similarity). Interacts with BVES and STX4. Interacts CC with WDFY2, PRKCZ and PRKCI (PubMed:17313651). Forms a complex CC with WDFY2 and PRKCZ (PubMed:17313651). CC {ECO:0000250|UniProtKB:P63045, ECO:0000269|PubMed:17313651, CC ECO:0000269|PubMed:17548353, ECO:0000269|PubMed:20057356}. CC -!- INTERACTION: CC P60766:Cdc42; NbExp=2; IntAct=EBI-521920, EBI-81763; CC O09044:Snap23; NbExp=2; IntAct=EBI-521920, EBI-1812522; CC P60879:Snap25; NbExp=5; IntAct=EBI-521920, EBI-445270; CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, CC synaptic vesicle membrane; Single-pass type IV membrane protein. CC Cell junction, synapse, synaptosome. Cell membrane CC {ECO:0000250|UniProtKB:P63045}. Note=Neuronal synaptic vesicles. CC Colocalizes with PRKCZ and WDFY2 in intracellular vesicles. CC {ECO:0000250|UniProtKB:P63027}. CC -!- PTM: Phosphorylated by PRKCZ in vitro and this phosphorylation is CC increased in the presence of WDFY2. CC {ECO:0000250|UniProtKB:P63027}. CC -!- SIMILARITY: Belongs to the synaptobrevin family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 v-SNARE coiled-coil homology domain. CC {ECO:0000255|PROSITE-ProRule:PRU00290}. 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 CCDS; CCDS24881.1; -. DR RefSeq; NP_033523.1; NM_009497.3. DR UniGene; Mm.28643; -. DR ProteinModelPortal; P63044; -. DR SMR; P63044; 30-116. DR BioGrid; 204495; 31. DR DIP; DIP-29065N; -. DR IntAct; P63044; 33. DR MINT; MINT-2411573; -. DR STRING; 10090.ENSMUSP00000021273; -. DR TCDB; 1.F.1.1.4; the synaptosomal vesicle fusion pore (svf-pore) family. DR iPTMnet; P63044; -. DR PhosphoSite; P63044; -. DR SwissPalm; P63044; -. DR EPD; 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; KOG0860; Eukaryota. DR eggNOG; COG5143; LUCA. DR HOGENOM; HOG000042711; -. DR HOVERGEN; HBG006675; -. DR InParanoid; P63044; -. DR KO; K13504; -. DR OrthoDB; EOG7MSMRJ; -. DR PhylomeDB; P63044; -. DR TreeFam; TF313666; -. DR Reactome; R-MMU-1445148; Translocation of GLUT4 to the plasma membrane. DR Reactome; R-MMU-181430; Norepinephrine Neurotransmitter Release Cycle. DR Reactome; R-MMU-210500; Glutamate Neurotransmitter Release Cycle. DR Reactome; R-MMU-264642; Acetylcholine Neurotransmitter Release Cycle. DR Reactome; R-MMU-421837; Clathrin derived vesicle budding. DR Reactome; R-MMU-422356; Regulation of insulin secretion. DR Reactome; R-MMU-432720; Lysosome Vesicle Biogenesis. DR Reactome; R-MMU-432722; Golgi Associated Vesicle Biogenesis. DR Reactome; R-MMU-888590; GABA synthesis, release, reuptake and degradation. DR ChiTaRS; Vamp2; mouse. DR PRO; PR:P63044; -. DR Proteomes; UP000000589; Chromosome 11. DR Bgee; P63044; -. DR CleanEx; MM_VAMP2; -. DR ExpressionAtlas; P63044; baseline and differential. DR Genevisible; P63044; MM. DR GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW. DR GO; GO:0030136; C:clathrin-coated vesicle; ISS:ParkinsonsUK-UCL. DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:MGI. DR GO; GO:0030659; C:cytoplasmic vesicle membrane; TAS:Reactome. DR GO; GO:0005829; C:cytosol; IMP:GOC. DR GO; GO:0070062; C:extracellular exosome; ISO:MGI. DR GO; GO:0016020; C:membrane; ISS:ParkinsonsUK-UCL. DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB. DR GO; GO:0005886; C:plasma membrane; IDA:MGI. DR GO; GO:0030141; C:secretory granule; IDA:MGI. DR GO; GO:0030667; C:secretory granule membrane; TAS:Reactome. DR GO; GO:0031201; C:SNARE complex; ISS:UniProtKB. DR GO; GO:0000322; C:storage vacuole; IDA:MGI. DR GO; GO:0045202; C:synapse; IDA:MGI. DR GO; GO:0008021; C:synaptic vesicle; 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:0070033; C:synaptobrevin 2-SNAP-25-syntaxin-1a-complexin II complex; IEA:Ensembl. DR GO; GO:0043195; C:terminal bouton; IEA:Ensembl. DR GO; GO:0005802; C:trans-Golgi network; IDA:UniProtKB. DR GO; GO:0031982; C:vesicle; IDA:UniProtKB. DR GO; GO:0008076; C:voltage-gated potassium channel complex; IEA:Ensembl. DR GO; GO:0042589; C:zymogen granule membrane; IDA:MGI. DR GO; GO:0048306; F:calcium-dependent protein binding; ISS:ParkinsonsUK-UCL. 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:0019905; F:syntaxin binding; IPI:UniProtKB. DR GO; GO:0017075; F:syntaxin-1 binding; ISO:MGI. DR GO; GO:0017156; P:calcium ion regulated exocytosis; IDA:MGI. DR GO; GO:0032869; P:cellular response to insulin stimulus; IDA:MGI. DR GO; GO:0043308; P:eosinophil degranulation; ISO:MGI. DR GO; GO:0043001; P:Golgi to plasma membrane protein transport; IMP:MGI. DR GO; GO:0060291; P:long-term synaptic potentiation; IMP:MGI. DR GO; GO:0061025; P:membrane fusion; IMP:MGI. DR GO; GO:0061024; P:membrane organization; TAS:Reactome. DR GO; GO:0090316; P:positive regulation of intracellular protein transport; IMP:MGI. DR GO; GO:0006461; P:protein complex assembly; IEA:Ensembl. DR GO; GO:0017158; P:regulation of calcium ion-dependent exocytosis; TAS:ParkinsonsUK-UCL. DR GO; GO:1902259; P:regulation of delayed rectifier potassium channel activity; ISS:UniProtKB. DR GO; GO:0017157; P:regulation of exocytosis; IDA:MGI. DR GO; GO:0050796; P:regulation of insulin secretion; TAS:Reactome. DR GO; GO:0060627; P:regulation of vesicle-mediated transport; IMP:MGI. DR GO; GO:0009749; P:response to glucose; IEA:Ensembl. DR GO; GO:0016079; P:synaptic vesicle exocytosis; IMP:MGI. DR Gene3D; 1.10.3840.10; -; 1. DR InterPro; IPR001388; Synaptobrevin. DR InterPro; IPR016444; Synaptobrevin/VAMP. 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; Cell membrane; Coiled coil; KW Complete proteome; Cytoplasmic vesicle; Direct protein sequencing; KW Membrane; Phosphoprotein; Reference proteome; Synapse; Synaptosome; KW Transmembrane; Transmembrane helix. FT INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:P63026}. FT CHAIN 2 116 Vesicle-associated membrane protein 2. FT /FTId=PRO_0000206725. FT TOPO_DOM 2 94 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 95 114 Helical; Anchor for type IV membrane FT protein. {ECO:0000255}. FT TOPO_DOM 115 116 Vesicular. {ECO:0000255}. FT DOMAIN 31 91 v-SNARE coiled-coil homology. FT {ECO:0000255|PROSITE-ProRule:PRU00290}. FT MOD_RES 2 2 N-acetylserine. FT {ECO:0000250|UniProtKB:P63026}. SQ SEQUENCE 116 AA; 12691 MW; 4A0D0D56B5409D0A CRC64; MSATAATVPP AAPAGEGGPP APPPNLTSNR RLQQTQAQVD EVVDIMRVNV DKVLERDQKL SELDDRADAL QAGASQFETS AAKLKRKYWW KNLKMMIILG VICAIILIII IVYFST //