| IED ID | IndEnz0002010097 |
| Enzyme Type ID | protease010097 |
| Protein Name |
Vesicle-associated membrane protein 2 VAMP-2 Synaptobrevin-2 |
| Gene Name | VAMP2 SYB2 |
| Organism | Homo sapiens (Human) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human) |
| Enzyme Sequence | MSATAATAPPAAPAGEGGPPAPPPNLTSNRRLQQTQAQVDEVVDIMRVNVDKVLERDQKLSELDDRADALQAGASQFETSAAKLKRKYWWKNLKMMIILGVICAIILIIIIVYFST |
| Enzyme Length | 116 |
| Uniprot Accession Number | P63027 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: Involved in the targeting and/or fusion of transport vesicles to their target membrane (By similarity). Major SNARE protein of synaptic vesicles which mediates fusion of synaptic vesicles to release neurotransmitters. Essential for fast vesicular exocytosis and activity-dependent neurotransmitter release as well as fast endocytosis that mediates rapid reuse of synaptic vesicles (By similarity) (PubMed:30929742). Modulates the gating characteristics of the delayed rectifier voltage-dependent potassium channel KCNB1. {ECO:0000250|UniProtKB:P63044, ECO:0000250|UniProtKB:P63045, ECO:0000269|PubMed:30929742}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Beta strand (1); Chain (1); Domain (1); Helix (1); Initiator methionine (1); Modified residue (1); Mutagenesis (9); Natural variant (5); Region (2); Sequence conflict (3); Site (3); Topological domain (2); Transmembrane (1); Turn (1) |
| Keywords | 3D-structure;Acetylation;Cell junction;Cell membrane;Coiled coil;Cytoplasmic vesicle;Disease variant;Membrane;Mental retardation;Phosphoprotein;Reference proteome;Synapse;Transmembrane;Transmembrane helix |
| Interact With | Q13520; Q3SXY8; Q9HA82; Q96BA8; Q15125; Q9Y282; P31937; Q7Z5P4; Q8N5M9; Q8N6L0; Q5T0T0; O94806; Q9NY72; Q8IWU4; Q8TBB6; O95721; P37840; Q16623; P61266; P32856-2; Q12846; Q96IK0; Q8N661; P55072; Q3ZAQ7; D2KHQ9; A7GBG3; Q57236; O55012 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000269|PubMed:17313651}; Single-pass type IV membrane protein {ECO:0000255}. Cell membrane {ECO:0000250|UniProtKB:P63045}. Note=Colocalizes with PRKCZ and WDFY2 in intracellular vesicles (PubMed:17313651). {ECO:0000269|PubMed:17313651}. |
| Modified Residue | MOD_RES 2; /note=N-acetylserine; /evidence=ECO:0000250|UniProtKB:P63026 |
| Post Translational Modification | PTM: Phosphorylated by PRKCZ in vitro and this phosphorylation is increased in the presence of WDFY2. {ECO:0000269|PubMed:17313651}.; PTM: (Microbial infection) Targeted and hydrolyzed by C.botulinum neurotoxin type B (BoNT/B, botB) which hydrolyzes the 76-Gln-|-Phe-77 bond and probably inhibits neurotransmitter release (PubMed:7803399). {ECO:0000269|PubMed:7803399, ECO:0000305|PubMed:22289120}.; PTM: (Microbial infection) Targeted and hydrolyzed by C.botulinum neurotoxin type D (BoNT/D, botD) which probably hydrolyzes the 59-Lys-|-Leu-60 bond and inhibits neurotransmitter release (PubMed:22289120). Note that humans are not known to be infected by C.botulinum type D. {ECO:0000269|PubMed:22289120, ECO:0000305, ECO:0000305|PubMed:22289120}.; PTM: (Microbial infection) Targeted and hydrolyzed by C.botulinum neurotoxin type F (BoNT/F, botF) which hydrolyzes the 58-Gln-|-Lys-59 bond and probably inhibits neurotransmitter release (PubMed:19543288). {ECO:0000305|PubMed:19543288, ECO:0000305|PubMed:22289120}.; PTM: (Microbial infection) Targeted and hydrolyzed by C.tetani tetanus toxin (tetX) which hydrolyzes the 76-Gln-|-Phe-77 bond and probably inhibits neurotransmitter release (PubMed:7803399). {ECO:0000269|PubMed:7803399}. |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (5) |
| Cross Reference PDB | 3FIE; 3FII; 3RK2; 3RK3; 3RL0; |
| Mapped Pubmed ID | 10394364; 10436022; 10440375; 10480595; 10535736; 10542231; 10559861; 10559924; 10625686; 10713150; 10766823; 11001057; 11017172; 11082044; 11163272; 11231140; 11239472; 11309201; 11470803; 11517213; 11532990; 11577110; 11604418; 11694590; 11815450; 11815463; 11842301; 11865063; 11873862; 11889126; 11994746; 12057195; 12130530; 12403834; 12517971; 12519779; 12558796; 12684222; 12750892; 12887316; 12952949; 1331807; 1361727; 1396558; 14514350; 14562105; 14622578; 14622579; 14676208; 15169906; 15217342; 15252009; 15260957; 15318165; 15502812; 15502813; 15537656; 15572341; 15649145; 15690086; 15703209; 15708368; 15728193; 15829963; 15895077; 15935055; 16099818; 16103228; 16155256; 16195891; 16215232; 16326391; 16410077; 16443778; 16516836; 16519520; 16714477; 16720719; 16722236; 16777091; 16798879; 16903783; 17001002; 17018281; 17055430; 17116749; 17158794; 17196367; 17202135; 17301226; 17331077; 17356306; 17382883; 17478680; 17502420; 17512409; 17515613; 17540576; 17609109; 17681954; 17765681; 17827149; 17891149; 17900700; 17978091; 17989281; 18093523; 18162464; 18182011; 18215623; 18388313; 18477612; 18511417; 18511418; 18512733; 18617632; 18628682; 18724936; 18790740; 18801842; 18981233; 19004828; 19046570; 19074577; 19092055; 19188424; 19296720; 19375301; 19458185; 19536138; 19557857; 19575674; 19603039; 19696796; 19822142; 20015340; 20033059; 20059951; 20231386; 20375064; 20416077; 20428113; 20448150; 20471030; 20554915; 20676083; 20826345; 20921140; 20946875; 21092861; 21127070; 2115402; 21187331; 21278753; 21316588; 21444687; 21444755; 21445324; 21466504; 21482805; 21565611; 21613550; 21636303; 21719644; 21743475; 21779028; 21785414; 21835666; 21841790; 21927000; 21927001; 21962517; 22099461; 22172278; 22233676; 22505844; 22645275; 22684149; 22993210; 23041287; 23129660; 23142665; 23246001; 23297414; 23533635; 23536704; 23610396; 23823722; 23861397; 23891661; 23936420; 24164654; 24186068; 24392163; 24478316; 24581490; 24727835; 24789820; 24966051; 25043001; 25107275; 25122888; 25179605; 25341920; 25368153; 25415308; 25416956; 25445064; 25481410; 25535373; 25713138; 25745174; 26042225; 26134228; 26412491; 26451041; 26638075; 26639969; 26675233; 26794648; 26929012; 27193484; 27226539; 27247366; 27458190; 27458546; 27616736; 28104892; 28495859; 28696301; 28877464; 28973888; 29111973; 29242231; 29328362; 29358308; 30582321; 30721745; 31110017; 31638250; 32194132; 32580088; 32675412; 33217562; 34183050; 34190041; 6146630; 7556990; 7641683; 7877694; 7910017; 8051110; 8071310; 8175689; 8226912; 8374173; 8402889; 8524399; 8552632; 8670264; 8997178; 9092476; 9100026; 9427626; 9428629; 9635431; 9701566; 9736607; 9914469; |
| Motif | |
| Gene Encoded By | |
| Mass | 12,663 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |