SNAP23 blocking peptide
SNAP23 Blocking Peptide
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NCBI and Uniprot Product Information
NCBI Description
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. The protein encoded by this gene 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. Two alternative transcript variants encoding different protein isoforms have been described for this gene. [provided by RefSeq, Jul 2008]
Uniprot Description
SNAP23: a member of the SNAP-25 family of SNARE proteins. 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. Two alternatively spliced isoforms have been described.
Protein type: Vesicle
Chromosomal Location of Human Ortholog: 15q14
Cellular Component: nucleoplasm; SNARE complex; azurophil granule; specific granule; neuron projection; focal adhesion; mast cell granule; cytoplasm; plasma membrane; synapse
Molecular Function: SNAP receptor activity; protein binding; syntaxin binding
Biological Process: synaptic vesicle fusion to presynaptic membrane; protein transport; histamine secretion by mast cell; vesicle targeting; post-Golgi vesicle-mediated transport; synaptic vesicle priming