VAMP2_RAT
ID VAMP2_RAT Reviewed; 116 AA.
AC P63045; Q64357;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Vesicle-associated membrane protein 2;
DE Short=VAMP-2;
DE AltName: Full=Synaptobrevin-2;
GN Name=Vamp2; Synonyms=Syb2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=2472388; DOI=10.1016/s0021-9258(18)60426-0;
RA Elferink L.A., Trimble W.S., Scheller R.H.;
RT "Two vesicle-associated membrane protein genes are differentially expressed
RT in the rat central nervous system.";
RL J. Biol. Chem. 264:11061-11064(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
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 [3]
RP PROTEIN SEQUENCE OF 32-47 AND 60-83, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Hippocampus;
RA Lubec G., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [4]
RP PROTEIN SEQUENCE OF 33-86, AND PROTEOLYTIC CLEAVAGE (MICROBIAL INFECTION)
RP BY C.BOTULINUM NEUROTOXIN TYPE X.
RX PubMed=28770820; DOI=10.1038/ncomms14130;
RA Zhang S., Masuyer G., Zhang J., Shen Y., Lundin D., Henriksson L.,
RA Miyashita S.I., Martinez-Carranza M., Dong M., Stenmark P.;
RT "Identification and characterization of a novel botulinum neurotoxin.";
RL Nat. Commun. 8:14130-14130(2017).
RN [5]
RP PROTEIN SEQUENCE OF 77-101, POSSIBLE FUNCTION, AND PROTEOLYTIC CLEAVAGE
RP (MICROBIAL INFECTION) BY C.BOTULINUM NEUROTOXIN TYPE B AND BY C.TETANI
RP TETANUS TOXIN.
RX PubMed=1331807; DOI=10.1038/359832a0;
RA Schiavo G., Benfenati F., Poulain B., Rossetto O., de Laureto P.P.,
RA Dasgupta B.R., Montecucco C.;
RT "Tetanus and botulinum-B neurotoxins block neurotransmitter release by
RT proteolytic cleavage of synaptobrevin.";
RL Nature 359:832-835(1992).
RN [6]
RP PROTEIN SEQUENCE OF 59-82, AND PROTEOLYTIC CLEAVAGE (MICROBIAL INFECTION)
RP BY C.BOTULINUM NEUROTOXIN TYPE F.
RX PubMed=8505288; DOI=10.1016/s0021-9258(19)50230-7;
RA Schiavo G., Shone C.C., Rossetto O., Alexander F.C., Montecucco C.;
RT "Botulinum neurotoxin serotype F is a zinc endopeptidase specific for
RT VAMP/synaptobrevin.";
RL J. Biol. Chem. 268:11516-11519(1993).
RN [7]
RP PROTEOLYTIC CLEAVAGE (MICROBIAL INFECTION) BY C.BOTULINUM NEUROTOXIN TYPE
RP G.
RX PubMed=7910017; DOI=10.1006/bbrc.1994.1526;
RA Yamasaki S., Binz T., Hayashi T., Szabo E., Yamasaki N., Eklund M.,
RA Jahn R., Niemann H.;
RT "Botulinum neurotoxin type G proteolyses the Ala81-Ala82 bond of rat
RT synaptobrevin 2.";
RL Biochem. Biophys. Res. Commun. 200:829-835(1994).
RN [8]
RP PROTEOLYTIC CLEAVAGE (MICROBIAL INFECTION) BY C.BOTULINUM NEUROTOXIN TYPES
RP D AND F AND BY C.TETANI TETANUS TOXIN.
RX PubMed=8175689; DOI=10.1016/s0021-9258(18)99941-2;
RA Yamasaki S., Baumeister A., Binz T., Blasi J., Link E., Cornille F.,
RA Roques B., Fykse E.M., Suedhof T.C., Jahn R., Niemann H.;
RT "Cleavage of members of the synaptobrevin/VAMP family by types D and F
RT botulinal neurotoxins and tetanus toxin.";
RL J. Biol. Chem. 269:12764-12772(1994).
RN [9]
RP FUNCTION, INTERACTION WITH KCNB1, AND SUBCELLULAR LOCATION.
RX PubMed=19690160; DOI=10.1074/jbc.m109.028761;
RA Lvov A., Greitzer D., Berlin S., Chikvashvili D., Tsuk S., Lotan I.,
RA Michaelevski I.;
RT "Rearrangements in the relative orientation of cytoplasmic domains induced
RT by a membrane-anchored protein mediate modulations in Kv channel gating.";
RL J. Biol. Chem. 284:28276-28291(2009).
RN [10]
RP INTERACTION WITH SEPT8; SYP; SNAP25 AND STX1A, AND TISSUE SPECIFICITY.
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 [11]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 1-97 IN COMPLEX WITH STX1A AND
RP SNAP25.
RX PubMed=9759724; DOI=10.1038/26412;
RA Sutton R.B., Fasshauer D., Jahn R., Brunger A.T.;
RT "Crystal structure of a SNARE complex involved in synaptic exocytosis at
RT 2.4 A resolution.";
RL Nature 395:347-353(1998).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 30-94 IN COMPLEX WITH STX1A; CPLX1
RP AND SNAP25, AND STRUCTURE BY NMR.
RX PubMed=11832227; DOI=10.1016/s0896-6273(02)00583-4;
RA Chen X., Tomchick D.R., Kovrigin E., Arac D., Machius M., Suedhof T.C.,
RA Rizo J.;
RT "Three-dimensional structure of the complexin/SNARE complex.";
RL Neuron 33:397-409(2002).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF 29-90 IN COMPLEX WITH STX1A AND
RP SNAP25.
RX PubMed=12496247; DOI=10.1074/jbc.m211889200;
RA Ernst J.A., Brunger A.T.;
RT "High resolution structure, stability, and synaptotagmin binding of a
RT truncated neuronal SNARE complex.";
RL J. Biol. Chem. 278:8630-8636(2003).
CC -!- FUNCTION: Involved in the targeting and/or fusion of transport vesicles
CC to their target membrane (By similarity). 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 (Probable). Modulates
CC the gating characteristics of the delayed rectifier voltage-dependent
CC potassium channel KCNB1 (PubMed:19690160).
CC {ECO:0000250|UniProtKB:P63044, ECO:0000269|PubMed:19690160,
CC ECO:0000305|PubMed:1331807}.
CC -!- SUBUNIT: Part of the SNARE core complex containing SNAP25, VAMP2 and
CC STX1A (PubMed:19196426). This complex binds to CPLX1. Interacts with
CC BVES and STX4. Interacts with VAPA and VAPB. Interacts with WDFY2,
CC PRKCZ and PRKCI (By similarity). Interacts (via N-terminus) with KCNB1
CC (via N-terminus and C-terminus); stimulates the channel inactivation
CC rate of KCNB1 (PubMed:19690160). Forms a complex with WDFY2 and PRKCZ
CC (By similarity). Interacts with SEPT8; the interaction inhibits
CC interaction of VAMP2 with SYP (PubMed:19196426). Interacts with SYP;
CC the interaction is inhibited by interaction with SEPT8
CC (PubMed:19196426). Interacts with PICALM (By similarity). Interacts
CC with alpha-synuclein/SNCA (By similarity). Interacts with STX3 (By
CC similarity). {ECO:0000250|UniProtKB:P63027,
CC ECO:0000250|UniProtKB:P63044, ECO:0000269|PubMed:19196426,
CC ECO:0000269|PubMed:19690160}.
CC -!- INTERACTION:
CC P63045; D4A229: Prkd3; NbExp=2; IntAct=EBI-520880, EBI-1255458;
CC P63045; P60881-2: Snap25; NbExp=4; IntAct=EBI-520880, EBI-15685612;
CC P63045; P32851: Stx1a; NbExp=8; IntAct=EBI-520880, EBI-539720;
CC P63045; Q08850: Stx4; NbExp=8; IntAct=EBI-520880, EBI-918243;
CC P63045; P21707: Syt1; NbExp=7; IntAct=EBI-520880, EBI-458098;
CC P63045; P63045: Vamp2; NbExp=2; IntAct=EBI-520880, EBI-520880;
CC P63045; Q60770: Stxbp3; Xeno; NbExp=2; IntAct=EBI-520880, EBI-8430169;
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:0000269|PubMed:19690160}. Note=Colocalizes with PRKCZ and WDFY2 in
CC intracellular vesicles. {ECO:0000250|UniProtKB:P63027}.
CC -!- TISSUE SPECIFICITY: Nervous system specific. A higher level expression
CC is seen in the brain as compared to the spinal cord (PubMed:2472388).
CC Expressed in hippocampal neurons (PubMed:19196426).
CC {ECO:0000269|PubMed:19196426, ECO:0000269|PubMed:2472388}.
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) which hydrolyzes the 76-Gln-|-Phe-77
CC bond and inhibits neurotransmitter release (PubMed:1331807).
CC {ECO:0000269|PubMed:1331807}.
CC -!- PTM: (Microbial infection) Targeted and hydrolyzed by C.botulinum
CC neurotoxin type D (BoNT/D, botD) which hydrolyzes the 59-Lys-|-Leu-60
CC bond and inhibits neurotransmitter release (PubMed:8175689).
CC {ECO:0000269|PubMed:8175689}.
CC -!- PTM: (Microbial infection) Targeted and hydrolyzed by C.botulinum
CC neurotoxin type F (BoNT/F, botF) which hydrolyzes the 58-Gln-|-Lys-59
CC bond and probably inhibits neurotransmitter release (PubMed:8505288).
CC {ECO:0000269|PubMed:8505288, ECO:0000305|PubMed:8175689}.
CC -!- PTM: (Microbial infection) Targeted and hydrolyzed by C.botulinum
CC neurotoxin type G (BoNT/G, botG) which hydrolyzes the 81-Ala-|-Ala-82
CC bond and probably inhibits neurotransmitter release (PubMed:8505288).
CC {ECO:0000269|PubMed:7910017}.
CC -!- PTM: (Microbial infection) Targeted and hydrolyzed by C.botulinum
CC neurotoxin type X (BoNT/X) which hydrolyzes the 66-Arg-|-Ala-67 bond
CC and probably inhibits neurotransmitter release (PubMed:28770820). It
CC remains unknown whether BoNT/X is ever produced, or what organisms it
CC targets. {ECO:0000269|PubMed:28770820}.
CC -!- PTM: (Microbial infection) Targeted and hydrolyzed by C.tetani toxin
CC (tetX) which hydrolyzes the 76-Gln-|-Phe-77 bond and inhibits
CC neurotransmitter release (PubMed:1331807). {ECO:0000269|PubMed:1331807,
CC ECO:0000305|PubMed:8175689}.
CC -!- SIMILARITY: Belongs to the synaptobrevin family. {ECO:0000305}.
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DR EMBL; M24105; AAA42321.1; -; mRNA.
DR EMBL; BC074003; AAH74003.1; -; mRNA.
DR PIR; B34288; B34288.
DR RefSeq; NP_036795.1; NM_012663.2.
DR PDB; 1KIL; X-ray; 2.30 A; A=28-92.
DR PDB; 1N7S; X-ray; 1.45 A; A=28-88.
DR PDB; 1SFC; X-ray; 2.40 A; A/E/I=1-96.
DR PDB; 2KOG; NMR; -; A=1-116.
DR PDB; 2N1T; NMR; -; A=25-93.
DR PDB; 3HD7; X-ray; 3.40 A; A/E=30-116.
DR PDB; 3IPD; X-ray; 4.80 A; A/E=30-116.
DR PDB; 3J96; EM; 7.60 A; K=28-89.
DR PDB; 3J97; EM; 7.80 A; K=28-89.
DR PDB; 3J98; EM; 8.40 A; K=28-89.
DR PDB; 3J99; EM; 8.20 A; K=28-89.
DR PDB; 5CCG; X-ray; 3.50 A; A/G=28-89.
DR PDB; 5CCH; X-ray; 3.60 A; A=28-89.
DR PDB; 5CCI; X-ray; 4.10 A; A=28-89.
DR PDB; 5W5C; X-ray; 1.85 A; A=28-66.
DR PDB; 5W5D; X-ray; 2.50 A; A=28-66.
DR PDB; 6A30; X-ray; 2.79 A; P=87-92.
DR PDB; 6IP1; EM; 3.90 A; A=1-94.
DR PDB; 6MDM; EM; 4.40 A; J=1-89.
DR PDB; 6MDN; EM; 4.40 A; J=1-72.
DR PDB; 6MTI; EM; 10.40 A; A/E/I/M/Q/U=28-89.
DR PDB; 6WVW; X-ray; 2.11 A; A/E=28-89.
DR PDB; 7UDB; EM; 3.50 A; C=29-83.
DR PDBsum; 1KIL; -.
DR PDBsum; 1N7S; -.
DR PDBsum; 1SFC; -.
DR PDBsum; 2KOG; -.
DR PDBsum; 2N1T; -.
DR PDBsum; 3HD7; -.
DR PDBsum; 3IPD; -.
DR PDBsum; 3J96; -.
DR PDBsum; 3J97; -.
DR PDBsum; 3J98; -.
DR PDBsum; 3J99; -.
DR PDBsum; 5CCG; -.
DR PDBsum; 5CCH; -.
DR PDBsum; 5CCI; -.
DR PDBsum; 5W5C; -.
DR PDBsum; 5W5D; -.
DR PDBsum; 6A30; -.
DR PDBsum; 6IP1; -.
DR PDBsum; 6MDM; -.
DR PDBsum; 6MDN; -.
DR PDBsum; 6MTI; -.
DR PDBsum; 6WVW; -.
DR PDBsum; 7UDB; -.
DR AlphaFoldDB; P63045; -.
DR BMRB; P63045; -.
DR SMR; P63045; -.
DR BioGRID; 246926; 5.
DR CORUM; P63045; -.
DR DIP; DIP-35503N; -.
DR IntAct; P63045; 24.
DR MINT; P63045; -.
DR STRING; 10116.ENSRNOP00000054114; -.
DR iPTMnet; P63045; -.
DR PhosphoSitePlus; P63045; -.
DR SwissPalm; P63045; -.
DR jPOST; P63045; -.
DR PaxDb; P63045; -.
DR PRIDE; P63045; -.
DR Ensembl; ENSRNOT00000057295; ENSRNOP00000054114; ENSRNOG00000006989.
DR GeneID; 24803; -.
DR KEGG; rno:24803; -.
DR UCSC; RGD:3949; rat.
DR CTD; 6844; -.
DR RGD; 3949; Vamp2.
DR eggNOG; KOG0860; Eukaryota.
DR GeneTree; ENSGT00940000158370; -.
DR HOGENOM; CLU_064620_4_0_1; -.
DR InParanoid; P63045; -.
DR OMA; CQDTFAT; -.
DR OrthoDB; 1606985at2759; -.
DR PhylomeDB; P63045; -.
DR Reactome; R-RNO-181429; Serotonin Neurotransmitter Release Cycle.
DR Reactome; R-RNO-181430; Norepinephrine Neurotransmitter Release Cycle.
DR Reactome; R-RNO-199992; trans-Golgi Network Vesicle Budding.
DR Reactome; R-RNO-210500; Glutamate Neurotransmitter Release Cycle.
DR Reactome; R-RNO-212676; Dopamine Neurotransmitter Release Cycle.
DR Reactome; R-RNO-264642; Acetylcholine Neurotransmitter Release Cycle.
DR Reactome; R-RNO-432720; Lysosome Vesicle Biogenesis.
DR Reactome; R-RNO-432722; Golgi Associated Vesicle Biogenesis.
DR Reactome; R-RNO-449836; Other interleukin signaling.
DR Reactome; R-RNO-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-RNO-8856828; Clathrin-mediated endocytosis.
DR Reactome; R-RNO-888590; GABA synthesis, release, reuptake and degradation.
DR Reactome; R-RNO-9609523; Insertion of tail-anchored proteins into the endoplasmic reticulum membrane.
DR EvolutionaryTrace; P63045; -.
DR PRO; PR:P63045; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000006989; Expressed in frontal cortex and 20 other tissues.
DR Genevisible; P63045; RN.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030136; C:clathrin-coated vesicle; ISS:ParkinsonsUK-UCL.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0031410; C:cytoplasmic vesicle; ISO:RGD.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; ISO:RGD.
DR GO; GO:0030285; C:integral component of synaptic vesicle membrane; IDA:SynGO.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:RGD.
DR GO; GO:0043229; C:intracellular organelle; IDA:RGD.
DR GO; GO:0016020; C:membrane; ISS:ParkinsonsUK-UCL.
DR GO; GO:0043005; C:neuron projection; IDA:RGD.
DR GO; GO:0044306; C:neuron projection terminus; IDA:ParkinsonsUK-UCL.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0030141; C:secretory granule; IDA:UniProtKB.
DR GO; GO:0031201; C:SNARE complex; IDA:ParkinsonsUK-UCL.
DR GO; GO:0000322; C:storage vacuole; ISO:RGD.
DR GO; GO:0045202; C:synapse; ISO:RGD.
DR GO; GO:0008021; C:synaptic vesicle; IDA:ParkinsonsUK-UCL.
DR GO; GO:0030672; C:synaptic vesicle membrane; IDA:CAFA.
DR GO; GO:0070044; C:synaptobrevin 2-SNAP-25-syntaxin-1a complex; IDA:RGD.
DR GO; GO:0070032; C:synaptobrevin 2-SNAP-25-syntaxin-1a-complexin I complex; IDA:MGI.
DR GO; GO:0070033; C:synaptobrevin 2-SNAP-25-syntaxin-1a-complexin II complex; IDA:RGD.
DR GO; GO:0043195; C:terminal bouton; HDA:ParkinsonsUK-UCL.
DR GO; GO:0005802; C:trans-Golgi network; ISO:RGD.
DR GO; GO:0031982; C:vesicle; ISO:RGD.
DR GO; GO:0042589; C:zymogen granule membrane; ISO:RGD.
DR GO; GO:0048306; F:calcium-dependent protein binding; IPI:ParkinsonsUK-UCL.
DR GO; GO:0005516; F:calmodulin binding; ISO:RGD.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0017022; F:myosin binding; IPI:RGD.
DR GO; GO:0005543; F:phospholipid binding; ISO:RGD.
DR GO; GO:0008022; F:protein C-terminus binding; IPI:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; IPI:RGD.
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; ISO:RGD.
DR GO; GO:0017075; F:syntaxin-1 binding; IDA:MGI.
DR GO; GO:0044325; F:transmembrane transporter binding; IPI:UniProtKB.
DR GO; GO:0017156; P:calcium-ion regulated exocytosis; ISO:RGD.
DR GO; GO:0032869; P:cellular response to insulin stimulus; ISO:RGD.
DR GO; GO:0043308; P:eosinophil degranulation; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0046879; P:hormone secretion; ISO:RGD.
DR GO; GO:0060291; P:long-term synaptic potentiation; ISO:RGD.
DR GO; GO:0061025; P:membrane fusion; ISO:RGD.
DR GO; GO:0090316; P:positive regulation of intracellular protein transport; ISO:RGD.
DR GO; GO:0015031; P:protein transport; IMP:RGD.
DR GO; GO:0065003; P:protein-containing complex assembly; IDA:RGD.
DR GO; GO:0045055; P:regulated exocytosis; ISO:RGD.
DR GO; GO:1902259; P:regulation of delayed rectifier potassium channel activity; IDA:UniProtKB.
DR GO; GO:0017157; P:regulation of exocytosis; IMP:RGD.
DR GO; GO:1903421; P:regulation of synaptic vesicle recycling; IMP:RGD.
DR GO; GO:0060627; P:regulation of vesicle-mediated transport; ISO:RGD.
DR GO; GO:0009749; P:response to glucose; IDA:UniProtKB.
DR GO; GO:0035493; P:SNARE complex assembly; IMP:CAFA.
DR GO; GO:0016081; P:synaptic vesicle docking; ISO:RGD.
DR GO; GO:0048488; P:synaptic vesicle endocytosis; ISS:UniProtKB.
DR GO; GO:0016079; P:synaptic vesicle exocytosis; IDA:SynGO.
DR GO; GO:0006906; P:vesicle fusion; ISS:UniProtKB.
DR GO; GO:0016192; P:vesicle-mediated transport; IMP:RGD.
DR DisProt; DP00622; -.
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 3D-structure; 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_0000206726"
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:0000269|PubMed:19196426"
FT SITE 58..59
FT /note="(Microbial infection) Cleavage; by C.botulinum
FT neurotoxin type F (BoNT/F, botF)"
FT /evidence="ECO:0000269|PubMed:8505288"
FT SITE 59..60
FT /note="(Microbial infection) Cleavage; by C.botulinum
FT neurotoxin type D (BoNT/D, botD)"
FT /evidence="ECO:0000269|PubMed:8175689"
FT SITE 66..67
FT /note="(Microbial infection) Cleavage; by C.botulinum
FT neurotoxin type X (BoNT/X)"
FT /evidence="ECO:0000269|PubMed:28770820"
FT SITE 76..77
FT /note="(Microbial infection) Cleavage; by C.botulinum
FT neurotoxin type B (BoNT/B, botB)"
FT /evidence="ECO:0000269|PubMed:1331807"
FT SITE 76..77
FT /note="(Microbial infection) Cleavage; by C.tetani tetanus
FT toxin (tetX)"
FT /evidence="ECO:0000269|PubMed:1331807"
FT SITE 81..82
FT /note="(Microbial infection) Cleavage; by C.botulinum
FT neurotoxin type G (BoNT/G, botG)"
FT /evidence="ECO:0000269|PubMed:7910017"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:P63026"
FT STRAND 25..28
FT /evidence="ECO:0007829|PDB:2KOG"
FT HELIX 29..88
FT /evidence="ECO:0007829|PDB:1N7S"
FT HELIX 91..115
FT /evidence="ECO:0007829|PDB:2KOG"
SQ SEQUENCE 116 AA; 12691 MW; 4A0D0D56B5409D0A CRC64;
MSATAATVPP AAPAGEGGPP APPPNLTSNR RLQQTQAQVD EVVDIMRVNV DKVLERDQKL
SELDDRADAL QAGASQFETS AAKLKRKYWW KNLKMMIILG VICAIILIII IVYFST
