SNAP25
Synaptic vesicle membrane docking and fusion is mediated by SNAREs (soluble N-ethylmaleimide-sensitive factor attachment protein receptors) located on the vesicle membrane (v-SNAREs) and the target membrane (t-SNAREs). The assembled v-SNARE/t-SNARE complex consists of a bundle of four helices, one of which is supplied by v-SNARE and the other three by t-SNARE. For t-SNAREs on the plasma membrane, the protein syntaxin supplies one helix and the protein encoded by this gene contributes the other two. Therefore, this gene product is a presynaptic plasma membrane protein involved in the regulation of neurotransmitter release. Two alternative transcript variants encoding different protein isoforms have been described for this gene. [provided by RefSeq, Jul 2008]
Full Name
Synaptosome Associated Protein 25
Function
t-SNARE involved in the molecular regulation of neurotransmitter release. May play an important role in the synaptic function of specific neuronal systems. Associates with proteins involved in vesicle docking and membrane fusion. Regulates plasma membrane recycling through its interaction with CENPF. Modulates the gating characteristics of the delayed rectifier voltage-dependent potassium channel KCNB1 in pancreatic beta cells.
Biological Process
Biological Process associative learningIEA:Ensembl
Biological Process chemical synaptic transmission1 PublicationNAS:UniProtKB
Biological Process exocytic insertion of neurotransmitter receptor to postsynaptic membraneIEA:Ensembl
Biological Process exocytosisManual Assertion Based On ExperimentIBA:GO_Central
Biological Process localization1 PublicationEXP:DisProt
Biological Process locomotory behaviorIEA:Ensembl
Biological Process long-term synaptic potentiationIEA:Ensembl
Biological Process neurotransmitter receptor internalizationIEA:Ensembl
Biological Process neurotransmitter uptake1 PublicationNAS:UniProtKB
Biological Process regulation of insulin secretionManual Assertion Based On ExperimentTAS:UniProtKB
Biological Process regulation of neuron projection developmentIEA:Ensembl
Biological Process synaptic vesicle docking1 PublicationNAS:UniProtKB
Biological Process synaptic vesicle exocytosisManual Assertion Based On ExperimentTAS:ParkinsonsUK-UCL
Biological Process synaptic vesicle fusion to presynaptic active zone membraneManual Assertion Based On ExperimentIBA:GO_Central
Biological Process synaptic vesicle primingManual Assertion Based On ExperimentIBA:GO_Central
Biological Process vesicle fusionManual Assertion Based On ExperimentIBA:GO_Central
Cellular Location
Cytoplasm, perinuclear region
Cell membrane
Synapse, synaptosome
Photoreceptor inner segment
Membrane association requires palmitoylation. Expressed throughout cytoplasm, concentrating at the perinuclear region. Colocalizes with KCNB1 at the cell membrane (By similarity).
Colocalizes with PLCL1 at the cell membrane (By similarity).
Involvement in disease
Myasthenic syndrome, congenital, 18 (CMS18):
A form of congenital myasthenic syndrome, a group of disorders characterized by failure of neuromuscular transmission, including pre-synaptic, synaptic, and post-synaptic disorders that are not of autoimmune origin. Clinical features are easy fatigability and muscle weakness affecting the axial and limb muscles (with hypotonia in early-onset forms), the ocular muscles (leading to ptosis and ophthalmoplegia), and the facial and bulbar musculature (affecting sucking and swallowing, and leading to dysphonia). The symptoms fluctuate and worsen with physical effort. CMS18 is an autosomal dominant presynaptic disorder clinically characterized by early-onset muscle weakness and easy fatigability associated with delayed psychomotor development and ataxia.
PTM
Palmitoylated (PubMed:28757145).
Cys-85 appears to be the main site, and palmitoylation is required for membrane association (By similarity).
(Microbial infection) Targeted and hydrolyzed by C.botulinum neurotoxin type A (BoNT/A, botA) which hydrolyzes the 197-Gln-|-Arg-198 bond and inhibits neurotransmitter release (PubMed:15592454, PubMed:9886085).
(Microbial infection) Targeted and hydrolyzed by C.botulinum neurotoxin type C (BoNT/C) which hydrolyzes the 198-Arg-|-Ala-199 bond and inhibits neurotransmitter release (PubMed:9886085, PubMed:17718519).
C.botulinum type C only rarely infects humans.
(Microbial infection) Targeted and hydrolyzed by C.botulinum neurotoxin type E (BoNT/E) which hydrolyzes the 180-Arg-|-Ile-181 bond and inhibits neurotransmitter release (PubMed:9886085).
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