Protein-coding gene in the species Homo sapiens

SNAP23

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Aliases: SNAP23, HsT17016, SNAP-23, SNAP23A, SNAP23B, synaptosome associated protein 23kDa, synaptosome associated protein 23
External IDs: OMIM: 602534; MGI: 109356; GeneCards: SNAP23
PDB: Ortholog search: PDBe RCSB
Chr.: Chromosome 15 (human)
Band: 15q15.1-q15.2
End: 42,545,356 bp
Chr.: Chromosome 2 (mouse)
Band: 2 60.37 cM|2 E5
End: 120,431,736 bp
BioGPS: More reference expression data
Databases: NCBI: entry; OMA: entry
Species: Human
Entrez: 8773
Ensembl: ENSG00000092531
UniProt: O00161
RefSeq (mRNA): NM_003825NM_130798
RefSeq (protein): NP_003816NP_570710
Location (UCSC): Chr 15: 42.49 – 42.55 Mb

Synaptosomal-associated protein 23 is a protein that in humans is encoded by the SNAP23 gene. Two alternative transcript variants encoding different protein isoforms have been described for this gene.

Function

Specificity of vesicular transport is regulated, in part, by the interaction of a vesicle-associated membrane protein termed synaptobrevin/VAMP with a target compartment membrane protein termed syntaxin. These proteins, together with SNAP25 (synaptosome-associated protein of 25 kDa), form a complex which serves as a binding site for the general membrane fusion machinery. Synaptobrevin/VAMP and syntaxin are believed to be involved in vesicular transport in most, if not all cells, while SNAP25 is present almost exclusively in the brain, suggesting that a ubiquitously expressed homolog of SNAP25 exists to facilitate transport vesicle/target membrane fusion in other tissues.

SNAP23 is structurally and functionally similar to SNAP25 and binds tightly to multiple syntaxins and synaptobrevins/VAMPs. It is an essential component of the high affinity receptor for the general membrane fusion machinery and is an important regulator of transport vesicle docking and fusion.

Clinical significance

In individuals with insulin resistance, SNAP23 is found to be translocated from the plasma membrane to the cytosol where it becomes associated with lipid droplets and is therefore unable to translocate GLUT-4 to the membrane, hindering glucose transport.