VAMP2

The protein encoded by this gene is a member of the vesicle-associated membrane protein (VAMP)/synaptobrevin family. Synaptobrevins/VAMPs, syntaxins, and the 25-kD synaptosomal-associated protein SNAP25 are the main components of a protein complex involved in the docking and/or fusion of synaptic vesicles with the presynaptic membrane. This gene is thought to participate in neurotransmitter release at a step between docking and fusion. The protein forms a stable complex with syntaxin, synaptosomal-associated protein, 25 kD, and synaptotagmin. It also forms a distinct complex with synaptophysin. It is a likely candidate gene for familial infantile myasthenia (FIMG) because of its map location and because it encodes a synaptic vesicle protein of the type that has been implicated in the pathogenesis of FIMG. [provided by RefSeq, Jul 2008]

Full Name

Vesicle Associated Membrane Protein 2

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.

Biological Process

Biological Process calcium-ion regulated exocytosis Source:ParkinsonsUK-UCL
Biological Process cellular response to insulin stimulus Source:ParkinsonsUK-UCL
Biological Process eosinophil degranulation Source:UniProtKB1 Publication
Biological Process exocytosis Source:ParkinsonsUK-UCL1 Publication
Biological Process Golgi to plasma membrane protein transport Source:ParkinsonsUK-UCL
Biological Process long-term synaptic potentiation Source:ParkinsonsUK-UCL
Biological Process membrane fusion Source:ParkinsonsUK-UCL
Biological Process positive regulation of intracellular protein transport Source:ParkinsonsUK-UCL
Biological Process protein transport Source:ParkinsonsUK-UCL
Biological Process protein-containing complex assembly Source:ParkinsonsUK-UCL
Biological Process regulation of delayed rectifier potassium channel activity Source:UniProtKB
Biological Process regulation of exocytosis Source:ParkinsonsUK-UCL
Biological Process regulation of vesicle-mediated transport Source:ParkinsonsUK-UCL
Biological Process response to glucose Source:ParkinsonsUK-UCL
Biological Process SNARE complex assembly Source:GO_Central1 Publication
Biological Process synaptic vesicle endocytosis Source:UniProtKB
Biological Process synaptic vesicle exocytosis Source:ParkinsonsUK-UCL
Biological Process vesicle fusion Source:UniProtKB1 Publication
Biological Process vesicle-mediated transport Source:ParkinsonsUK-UCL

Cellular Location

Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane
Cell membrane
Colocalizes with PRKCZ and WDFY2 in intracellular vesicles (PubMed:17313651).

Involvement in disease

Neurodevelopmental disorder with hypotonia and autistic features with or without hyperkinetic movements (NEDHAHM):
An autosomal dominant disorder characterized by axial hypotonia apparent at birth, global developmental delay, intellectual disability, seizures, and autistic features. Involuntary hyperkinetic movements are present in some patients.

Topology

Cytoplasmic: 2-94
Helical: 95-114
Vesicular: 115-116

PTM

Phosphorylated by PRKCZ in vitro and this phosphorylation is increased in the presence of WDFY2.
(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).
(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.
(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).
(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).