VAMP2_MOUSE
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 03-AUG-2022, entry version 165.
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; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC 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 GLUT4
RT 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., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., 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., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., 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 project:
RT 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) BY
RP C.BOTULINUM NEUROTOXIN TYPE B AND BY C.TETANI TETANUS TOXIN.
RX PubMed=10413679; DOI=10.1242/jcs.112.16.2715;
RA Lalli G., Herreros J., Osborne S.L., Montecucco C., Rossetto O.,
RA Schiavo G.;
RT "Functional characterisation of tetanus and botulinum neurotoxins binding
RT domains.";
RL J. Cell Sci. 112:2715-2724(1999).
RN [6]
RP FUNCTION.
RX PubMed=15475946; DOI=10.1038/ncb1185;
RA Deak F., Schoch S., Liu X., Suedhof T.C., Kavalali E.T.;
RT "Synaptobrevin is essential for fast synaptic-vesicle endocytosis.";
RL Nat. Cell Biol. 6:1102-1108(2004).
RN [7]
RP INTERACTION WITH WDFY2; PRKCZ AND PRKCI, AND COMPLEX FORMATION WITH WDFY2
RP 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 kinase
RT Czeta.";
RL FEBS J. 274:1552-1566(2007).
RN [8]
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 of
RT syntaxin 4-mediated exocytosis.";
RL J. Biol. Chem. 282:21786-21797(2007).
RN [9]
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 to
RT synaptophysin.";
RL J. Neurochem. 108:867-880(2009).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, and 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 expression.";
RL Cell 143:1174-1189(2010).
RN [11]
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., Bader D.M.;
RT "Identification of a novel Bves function: regulation of vesicular
RT transport.";
RL EMBO J. 29:532-545(2010).
RN [12]
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., Suedhof T.C.;
RT "Alpha-synuclein promotes SNARE-complex assembly in vivo and in vitro.";
RL Science 329:1663-1667(2010).
RN [13]
RP INTERACTION WITH STX3, AND TISSUE SPECIFICITY.
RX PubMed=26406599; DOI=10.1371/journal.pone.0138508;
RA Zulliger R., Conley S.M., Mwoyosvi M.L., Stuck M.W., Azadi S., Naash M.I.;
RT "SNAREs Interact with Retinal Degeneration Slow and Rod Outer Segment
RT Membrane Protein-1 during Conventional and Unconventional Outer Segment
RT Targeting.";
RL PLoS ONE 10:E0138508-E0138508(2015).
CC -!- FUNCTION: Involved in the targeting and/or fusion of transport vesicles
CC to their target membrane (PubMed:9430681). Major SNARE protein of
CC synaptic vesicles which mediates fusion of synaptic vesicles to release
CC neurotransmitters. Essential for fast vesicular exocytosis and
CC activity-dependent neurotransmitter release as well as fast endocytosis
CC that mediates rapid reuse of synaptic vesicles (PubMed:15475946).
CC Modulates the gating characteristics of the delayed rectifier voltage-
CC dependent potassium channel KCNB1 (By similarity).
CC {ECO:0000250|UniProtKB:P63045, ECO:0000269|PubMed:15475946,
CC ECO:0000269|PubMed:9430681}.
CC -!- SUBUNIT: Part of the SNARE core complex containing SNAP25, VAMP2 and
CC STX1A (PubMed:19196426). This complex binds to CPLX1. Interacts with
CC VAPA and VAPB (By similarity). Interacts (via N-terminus) with KCNB1
CC (via N-terminus and C-terminus); stimulates the channel inactivation
CC rate of KCNB1 (By similarity). Interacts with BVES and STX4. Interacts
CC with WDFY2, PRKCZ and PRKCI (PubMed:17313651). Forms a complex with
CC WDFY2 and PRKCZ (PubMed:17313651). Interacts with SEPT8; the
CC interaction inhibits interaction of VAMP2 with SYP (PubMed:19196426).
CC Interacts with SYP; the interaction is inhibited by interaction with
CC SEPT8 (PubMed:19196426). Interacts with PICALM (By similarity).
CC Interacts with alpha-synuclein/SNCA. Interacts with STX3 isoform 3B
CC (PubMed:26406599). {ECO:0000250|UniProtKB:P63045,
CC ECO:0000269|PubMed:17313651, ECO:0000269|PubMed:17548353,
CC ECO:0000269|PubMed:19196426, ECO:0000269|PubMed:20057356,
CC ECO:0000269|PubMed:20798282, ECO:0000269|PubMed:26406599}.
CC -!- INTERACTION:
CC P63044; P60766: Cdc42; NbExp=2; IntAct=EBI-521920, EBI-81763;
CC P63044; P60879: Snap25; NbExp=18; IntAct=EBI-521920, EBI-445270;
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic
CC vesicle membrane {ECO:0000250|UniProtKB:P63027}; Single-pass type IV
CC membrane protein {ECO:0000255}. Cell membrane
CC {ECO:0000250|UniProtKB:P63045}. Note=Colocalizes with PRKCZ and WDFY2
CC in intracellular vesicles. {ECO:0000250|UniProtKB:P63027}.
CC -!- TISSUE SPECIFICITY: Expressed in the outer plexiform layer of the
CC retina (at protein level). {ECO:0000269|PubMed:26406599}.
CC -!- PTM: Phosphorylated by PRKCZ in vitro and this phosphorylation is
CC increased in the presence of WDFY2. {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 spinal
CC cord cells almost all the protein has been digested (PubMed:10413679).
CC BoNT/B hydrolyzes the 76-Gln-|-Phe-77 bond and inhibits
CC neurotransmitter release (Probable). {ECO:0000269|PubMed:10413679,
CC ECO:0000305|PubMed:10413679}.
CC -!- PTM: (Microbial infection) Targeted and hydrolyzed by C.tetani toxin
CC (tetX); 20 hours after treatment of spinal cord cells almost all the
CC protein has been digested (PubMed:10413679). Tetanus toxin hydrolyzes
CC the 76-Gln-|-Phe-77 bond and inhibits neurotransmitter release
CC (Probable). {ECO:0000269|PubMed:10413679, 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 AlphaFoldDB; P63044; -.
DR BMRB; P63044; -.
DR SMR; P63044; -.
DR BioGRID; 204495; 55.
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 ProteomicsDB; 300211; -.
DR DNASU; 22318; -.
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 VEuPathDB; HostDB:ENSMUSG00000020894; -.
DR eggNOG; KOG0860; Eukaryota.
DR GeneTree; ENSGT00940000158370; -.
DR HOGENOM; CLU_064620_4_0_1; -.
DR InParanoid; P63044; -.
DR OMA; CQDTFAT; -.
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 BioGRID-ORCS; 22318; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Vamp2; mouse.
DR PRO; PR:P63044; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; P63044; protein.
DR Bgee; ENSMUSG00000020894; Expressed in perirhinal cortex and 255 other tissues.
DR ExpressionAtlas; P63044; baseline and differential.
DR Genevisible; P63044; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030136; C:clathrin-coated vesicle; ISS:ParkinsonsUK-UCL.
DR GO; GO:0060203; C:clathrin-sculpted glutamate transport vesicle membrane; TAS:Reactome.
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: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: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:0005484; F:SNAP receptor activity; IBA:GO_Central.
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:0044325; F:transmembrane transporter 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:0051649; P:establishment of localization in cell; IMP: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:0048488; P:synaptic vesicle endocytosis; IMP:UniProtKB.
DR GO; GO:0016079; P:synaptic vesicle exocytosis; IMP:UniProtKB.
DR GO; GO:0006906; P:vesicle fusion; ISS:UniProtKB.
DR GO; GO:0016192; P:vesicle-mediated transport; ISO:MGI.
DR InterPro; IPR001388; Synaptobrevin.
DR InterPro; IPR016444; Synaptobrevin/VAMP.
DR InterPro; IPR042855; V_SNARE_CC.
DR InterPro; IPR028717; VAMP2.
DR PANTHER; PTHR45701; PTHR45701; 1.
DR PANTHER; PTHR45701:SF5; PTHR45701:SF5; 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 membrane; Coiled coil; Cytoplasmic vesicle;
KW Direct protein sequencing; Membrane; Phosphoprotein; Reference proteome;
KW Synapse; Transmembrane; Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P63026"
FT CHAIN 2..116
FT /note="Vesicle-associated membrane protein 2"
FT /id="PRO_0000206725"
FT TOPO_DOM 2..94
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 95..114
FT /note="Helical; Anchor for type IV membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 115..116
FT /note="Vesicular"
FT /evidence="ECO:0000255"
FT DOMAIN 31..91
FT /note="v-SNARE coiled-coil homology"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00290"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 92..116
FT /note="Required for interaction with SEPT8"
FT /evidence="ECO:0000250|UniProtKB:P63045"
FT SITE 76..77
FT /note="(Microbial infection) Cleavage; by C.botulinum
FT neurotoxin type B (BoNT/B, botB)"
FT /evidence="ECO:0000305|PubMed:10413679"
FT SITE 76..77
FT /note="(Microbial infection) Cleavage; by C.tetani
FT neurotoxin (tetX)"
FT /evidence="ECO:0000305|PubMed:10413679"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:P63026"
SQ SEQUENCE 116 AA; 12691 MW; 4A0D0D56B5409D0A CRC64;
MSATAATVPP AAPAGEGGPP APPPNLTSNR RLQQTQAQVD EVVDIMRVNV DKVLERDQKL
SELDDRADAL QAGASQFETS AAKLKRKYWW KNLKMMIILG VICAIILIII IVYFST
