SNAREs (soluble N-ethylmaleimide-sensitive factor-attachment protein receptors) are essential proteins for intracellular membrane fusion. SNAREs localized on opposing membranes assemble to form a trans-SNARE complex, an extended, parallel four-helix bundle whose assembly releases energy that drives membrane fusion. The core SNARE complex typically consists of four alpha-helical domains, three from target membrane SNAREs (t-SNAREs) and one from a vesicle SNARE (v- SNARE) (PubMed:10036234, PubMed:30929742). VAMP2 is a v-SNARE assembling into a SNARE complex with the t-SNAREs SNAP25 and STX1A to mediate the fusion of synaptic vesicles with the presynaptic plasma membrane in neurotransmitter release (PubMed:30929742). Also functions in compensatory endocytosis for synaptic vesicle recycling (By similarity). In adipocytes, it is involved in the insulin-dependent exocytosis of GLUT4 storage vesicles (By similarity). Independently of its SNARE activity, it could modulate the gating characteristics of the delayed rectifier voltage-dependent potassium channel KCNB1 (By similarity). {ECO:0000250|UniProtKB:P63044, ECO:0000250|UniProtKB:P63045, ECO:0000269|PubMed:10036234, ECO:0000269|PubMed:30929742}. This is the function of VAMP2 (vesicle associated membrane protein 2, ENSG00000220205).