Sec17, a yeast homolog of the human SNAP, patriciates in membrane fusion of vesicles complexes with SNARE and NSF to mediate assembly and disassembly.
Identifiers
Symbol
SNAP
Pfam
PF14938
PROSITE
PDOC50892 PDOC50192, PDOC50892
CDD
cd15832
Available protein structures:
Pfam
structures / ECOD
PDB
RCSB PDB; PDBe; PDBj
PDBsum
structure summary
Soluble N-ethylmaleimide-Sensitive Factor Attachment Proteins (SNAP, or Sec17p in yeast) are a family of cytosolic adaptor proteins involved in vesicular fusion at membranes during intracellular transport and exocytosis. SNAPs interact with proteins of the SNARE complex and NSF to play a key role in recycling the components of the fusion complex. SNAPs are involved in the priming of the vesicle fusion complex during assembly, as well as in the disassembly following a vesicle fusion event. Following membrane fusion, the tethering SNARE proteins complex disassembles in response to steric changes originating from the ATPase NSF. The energy provided by NSF is transferred throughout the SNARE complex and SNAP, allowing the proteins to untangle, and recycled for future fusion events. Mammals have three SNAP genes: α-SNAP, β-SNAP, and γ-SNAP. α- and γ-SNAP are expressed throughout the body, while β-SNAP is specific to the brain. The yeast homolog of the human SNAP is Sec17, the structural diagram of which is included on this page.
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