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 18-SEP-2019, entry version 150. 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; Myomorpha; 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 SUBCELLULAR LOCATION, AND PROTEOLYTIC CLEAVAGE (MICROBIAL INFECTION) RP BY C.BOTULINUM NEUROTOXIN TYPE B AND BY C.TETANI TETANUS TOXIN. RX PubMed=10413679; RA Lalli G., Herreros J., Osborne S.L., Montecucco C., Rossetto O., RA Schiavo G.; RT "Functional characterisation of tetanus and botulinum neurotoxins RT binding domains."; RL J. Cell Sci. 112:2715-2724(1999). RN [6] 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 [7] 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 [8] RP INTERACTION WITH SEPT8; SYP; SNAP25 AND STX1A. RX PubMed=19196426; DOI=10.1111/j.1471-4159.2008.05849.x; RA Ito H., Atsuzawa K., Morishita R., Usuda N., Sudo K., Iwamoto I., RA Mizutani K., Katoh-Semba R., Nozawa Y., Asano T., Nagata K.; RT "Sept8 controls the binding of vesicle-associated membrane protein 2 RT to synaptophysin."; RL J. Neurochem. 108:867-880(2009). RN [9] 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 [10] 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). RN [11] RP INTERACTION WITH ALPHA-SYNUCLEIN/SNCA. RX PubMed=20798282; DOI=10.1126/science.1195227; RA Burre J., Sharma M., Tsetsenis T., Buchman V., Etherton M.R., RA Suedhof T.C.; RT "Alpha-synuclein promotes SNARE-complex assembly in vivo and in RT vitro."; RL Science 329:1663-1667(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 (PubMed:19196426). This complex binds to CPLX1. CC Interacts with VAPA and VAPB (By similarity). Interacts with BVES CC and STX4. Interacts with WDFY2, PRKCZ and PRKCI (PubMed:17313651). CC Forms a complex with WDFY2 and PRKCZ (PubMed:17313651). Interacts CC with SEPT8; the interaction inhibits interaction of VAMP2 with SYP CC (PubMed:19196426). Interacts with SYP; the interaction is inhibit CC by interaction with SEPT8 (PubMed:19196426). Interacts with PICALM CC (By similarity). Interacts with alpha-synuclein/SNCA. CC {ECO:0000250|UniProtKB:P63045, ECO:0000269|PubMed:17313651, CC ECO:0000269|PubMed:17548353, ECO:0000269|PubMed:19196426, CC ECO:0000269|PubMed:20057356, ECO:0000269|PubMed:20798282}. CC -!- INTERACTION: CC P60766:Cdc42; NbExp=2; IntAct=EBI-521920, EBI-81763; CC O09044:Snap23; NbExp=3; IntAct=EBI-521920, EBI-1812522; CC P60879:Snap25; NbExp=18; 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 -!- PTM: (Microbial infection) Targeted and hydrolyzed by C.botulinum CC neurotoxin type B (BoNT/B, botB); 20 hours after treatment of CC spinal cord cells almost all the protein has been digested CC (PubMed:10413679). BoNT/B hydrolyzes the 76-Gln-|-Phe-77 bond and CC inhibits neurotransmitter release (Probable). CC {ECO:0000269|PubMed:10413679, ECO:0000305|PubMed:10413679}. CC -!- PTM: (Microbial infection) Targeted and hydrolyzed by C.tetani CC toxin (tetX); 20 hours after treatment of spinal cord cells almost CC all the protein has been digested (PubMed:10413679). Tetanus toxin CC hydrolyzes the 76-Gln-|-Phe-77 bond and inhibits neurotransmitter CC release (Probable). {ECO:0000269|PubMed:10413679, CC ECO:0000305|PubMed:10413679}. CC -!- SIMILARITY: Belongs to the synaptobrevin family. {ECO:0000305}. 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 SMR; P63044; -. DR BioGrid; 204495; 31. DR CORUM; P63044; -. DR DIP; DIP-29065N; -. DR IntAct; P63044; 40. DR MINT; P63044; -. DR STRING; 10090.ENSMUSP00000021273; -. DR TCDB; 1.F.1.1.4; the synaptosomal vesicle fusion pore (svf-pore) family. DR iPTMnet; P63044; -. DR PhosphoSitePlus; P63044; -. DR SwissPalm; P63044; -. DR EPD; P63044; -. DR jPOST; 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 GeneTree; ENSGT00940000158370; -. DR HOGENOM; HOG000042711; -. DR InParanoid; P63044; -. DR KO; K13504; -. DR OMA; ILLVYIW; -. DR OrthoDB; 1606985at2759; -. DR PhylomeDB; P63044; -. DR TreeFam; TF313666; -. DR Reactome; R-MMU-181429; Serotonin Neurotransmitter Release Cycle. DR Reactome; R-MMU-181430; Norepinephrine Neurotransmitter Release Cycle. DR Reactome; R-MMU-199992; trans-Golgi Network Vesicle Budding. DR Reactome; R-MMU-210500; Glutamate Neurotransmitter Release Cycle. DR Reactome; R-MMU-212676; Dopamine Neurotransmitter Release Cycle. DR Reactome; R-MMU-264642; Acetylcholine Neurotransmitter Release Cycle. DR Reactome; R-MMU-432720; Lysosome Vesicle Biogenesis. DR Reactome; R-MMU-432722; Golgi Associated Vesicle Biogenesis. DR Reactome; R-MMU-449836; Other interleukin signaling. DR Reactome; R-MMU-8856825; Cargo recognition for clathrin-mediated endocytosis. DR Reactome; R-MMU-8856828; Clathrin-mediated endocytosis. DR Reactome; R-MMU-888590; GABA synthesis, release, reuptake and degradation. DR Reactome; R-MMU-9609523; Insertion of tail-anchored proteins into the endoplasmic reticulum membrane. DR ChiTaRS; Vamp2; mouse. DR PRO; PR:P63044; -. DR Proteomes; UP000000589; Chromosome 11. DR Bgee; ENSMUSG00000020894; Expressed in 295 organ(s), highest expression level in primary motor cortex. 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:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:MGI. DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IDA:MGI. DR GO; GO:0030285; C:integral component of synaptic vesicle membrane; ISO:MGI. DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI. DR GO; GO:0043229; C:intracellular organelle; ISO:MGI. DR GO; GO:0016020; C:membrane; ISS:ParkinsonsUK-UCL. DR GO; GO:0043005; C:neuron projection; ISO:MGI. DR GO; GO:0044306; C:neuron projection terminus; ISO:MGI. 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:UniProtKB. DR GO; GO:0030667; C:secretory granule membrane; TAS:Reactome. DR GO; GO:0031201; C:SNARE complex; IDA:MGI. 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; ISO:MGI. 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:0042802; F:identical protein binding; ISO:MGI. DR GO; GO:0044325; F:ion channel binding; ISO:MGI. DR GO; GO:0017022; F:myosin binding; ISO:MGI. DR GO; GO:0005543; F:phospholipid binding; IDA:MGI. DR GO; GO:0008022; F:protein C-terminus binding; ISO:MGI. DR GO; GO:0044877; F:protein-containing complex binding; ISO: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; IDA:ParkinsonsUK-UCL. 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:0098967; P:exocytic insertion of neurotransmitter receptor to postsynaptic membrane; IMP:SynGO. DR GO; GO:0043001; P:Golgi to plasma membrane protein transport; IMP:MGI. DR GO; GO:0046879; P:hormone secretion; IDA:UniProtKB. DR GO; GO:0060291; P:long-term synaptic potentiation; IMP:MGI. DR GO; GO:0061025; P:membrane fusion; IMP:MGI. DR GO; GO:0090316; P:positive regulation of intracellular protein transport; IMP:MGI. DR GO; GO:0015031; P:protein transport; ISO:MGI. DR GO; GO:0065003; P:protein-containing complex assembly; ISO:MGI. DR GO; GO:0045055; P:regulated exocytosis; IDA:UniProtKB. 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:1903421; P:regulation of synaptic vesicle recycling; ISO:MGI. DR GO; GO:0060627; P:regulation of vesicle-mediated transport; IMP:MGI. DR GO; GO:0009749; P:response to glucose; ISO:MGI. DR GO; GO:0035493; P:SNARE complex assembly; ISO:MGI. DR GO; GO:0016081; P:synaptic vesicle docking; IDA:SynGO. DR GO; GO:0016079; P:synaptic vesicle exocytosis; IMP:MGI. DR GO; GO:0016192; P:vesicle-mediated transport; ISO:MGI. DR InterPro; IPR001388; Synaptobrevin. DR InterPro; IPR016444; Synaptobrevin/VAMP. DR InterPro; IPR028717; VAMP2. DR PANTHER; PTHR45701:SF15; PTHR45701:SF15; 1. 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 REGION 92 116 Required for interaction with SEPT8. FT {ECO:0000250|UniProtKB:P63045}. FT SITE 76 77 (Microbial infection) Cleavage; by FT C.botulinum neurotoxin type B (BoNT/B, FT botB). {ECO:0000305|PubMed:10413679}. FT SITE 76 77 (Microbial infection) Cleavage; by FT C.tetani neurotoxin (tetX). FT {ECO:0000305|PubMed:10413679}. 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 //