SV2B

This gene encodes a member of the synaptic vesicle proteins 2 (SV2) family and major facilitator superfamily of proteins. This protein and other members of the family are localized to synaptic vesicles and may function in the regulation of vesicle trafficking and exocytosis. Studies in mice suggest that the encoded protein may act as a protein receptor for botulinum neurotoxin E in neurons, and that this protein may be important for the integrity of the glomerular filtration barrier. This gene shows reduced expression in areas of synaptic loss in the hippocampus of human temporal lobe epilepsy patients.

Full Name

SV2B

Function

Probably plays a role in the control of regulated secretion in neural and endocrine cells.
(Microbial infection) Receptor for the C.botulinum neurotoxin type A2 (BoNT/A, botA); glycosylation is not essential but enhances the interaction (PubMed:29649119).
Probably also serves as a receptor for the closely related C.botulinum neurotoxin type A1

Biological Process

Biological Process chemical synaptic transmissionIEA:InterPro
Biological Process neurotransmitter transportIEA:UniProtKB-KW

Cellular Location

Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane
Cytoplasmic vesicle, secretory vesicle, acrosome
Associated with synaptic-like microvesicles but not with insulin-containing vesicles in insulin-secreting cells of the pancreas (By similarity).
Localizes to microvesicles in the pinealocytes. Localizes to the acrosome in spermatids (By similarity).

Topology

Cytoplasmic: 1-108
Helical: 109-129
Extracellular: 130-148
Helical: 149-169
Cytoplasmic: 170-182
Helical: 183-203
Extracellular: 204-205
Helical: 206-226
Cytoplasmic: 227-237
Helical: 238-258
Extracellular: 259-277
Helical: 278-298
Cytoplasmic: 299-390
Helical: 391-411
Extracellular: 412-535
Helical: 536-556
Cytoplasmic: 557-565
Helical: 566-586
Extracellular: 587-592
Helical: 593-613
Cytoplasmic: 614-626
Helical: 627-649
Extracellular: 650-653
Helical: 654-672
Cytoplasmic: 673-683

PTM

N-glycosylated.
The N-terminal cytoplasmic domain is phosphorylated by CK1.