vesicle-associated membrane protein 5 (myobrevin) | |||||||
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Identifiers | |||||||
Symbol | VAMP5 | ||||||
NCBI gene | 10791 | ||||||
HGNC | 12646 | ||||||
OMIM | 607029 | ||||||
RefSeq | NM_006634 | ||||||
UniProt | O95183 | ||||||
Other data | |||||||
Locus | Chr. 2 p11.2 | ||||||
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Vesicle-associated membrane protein 5 also known as VAMP5 is a human gene which encodes a member of the synaptobrevin protein family. [1] [2]
VAMPs (synaptobrevins) along with syntaxins and the 25-kD synaptosomal-associated protein are the main components of a protein complex involved in the docking and/or fusion of vesicles and cell membranes. The VAMP5 gene is a member of the vesicle-associated membrane protein (VAMP)/synaptobrevin family and the SNARE superfamily. This VAMP family member may participate in vesicle trafficking events that are associated with myogenesis. [2]
SNARE proteins – "SNAPREceptor" – are a large protein family consisting of at least 24 members in yeasts, more than 60 members in mammalian cells, and some numbers in plants. The primary role of SNARE proteins is to mediate vesicle fusion – the fusion of vesicles with the target membrane; this notably mediates exocytosis, but can also mediate the fusion of vesicles with membrane-bound compartments. The best studied SNAREs are those that mediate the neurotransmitter release of synaptic vesicles in neurons. These neuronal SNAREs are the targets of the neurotoxins responsible for botulism and tetanus produced by certain bacteria.
Vesicle associated membrane proteins (VAMP) are a family of SNARE proteins with similar structure, and are mostly involved in vesicle fusion.
Synaptobrevins are small integral membrane proteins of secretory vesicles with molecular weight of 18 kilodalton (kDa) that are part of the vesicle-associated membrane protein (VAMP) family.
Synaptosomal-Associated Protein, 25kDa (SNAP-25) is a Target Soluble NSF (N-ethylmaleimide-sensitive factor) Attachment Protein Receptor (t-SNARE) protein encoded by the SNAP25 gene found on chromosome 20p12.2 in humans. SNAP-25 is a component of the trans-SNARE complex, which accounts for membrane fusion specificity and directly executes fusion by forming a tight complex that brings the synaptic vesicle and plasma membranes together.
Syntaxin-1A is a protein that in humans is encoded by the STX1A gene.
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.
Syntaxin-4 is a protein that in humans is encoded by the STX4 gene.
Vesicle-associated membrane protein 2 (VAMP2) is a protein that in humans is encoded by the VAMP2 gene.
Synaptobrevin-like protein 1 (SYBL1), also known as vesicle-associated membrane protein 7 (VAMP7), is a protein that in humans is encoded by the VAMP7, or SYBL1, gene.
Syntaxin-7 is a protein that in humans is encoded by the STX7 gene.
Syntaxin-6 is a protein that in humans is encoded by the STX6 gene.
N-ethylmaleimide-sensitive factor Attachment Protein Alpha, also known as SNAP-α, is a SNAP protein that is involved in the intra-cellular trafficking and fusing of vesicles to target membranes in cells.
Vesicle-associated membrane protein 3 is a protein that in humans is encoded by the VAMP3 gene.
Syntaxin-2, also known as epimorphin, is a protein that in humans is encoded by the STX2 gene.
Vesicle-associated membrane protein 8 is a protein that in humans is encoded by the VAMP8 gene.
Vesicle-associated membrane protein 4 is a protein that in humans is encoded by the VAMP4 gene.
Vesicle-associated membrane protein 1 (VAMP1) is a protein that in humans is encoded by the VAMP1 gene.
Syntaxin 3, also known as STX3, is a protein which in humans is encoded by the STX3 gene.
Syntaxins are a family of membrane integrated Q-SNARE proteins participating in exocytosis.
Munc-18 proteins are the mammalian homologue of UNC-18 and are a member of the Sec1/Munc18-like (SM) protein family. Munc-18 proteins have been identified as essential components of the synaptic vesicle fusion protein complex and are crucial for the regulated exocytosis of neurons and neuroendocrine cells.
This article incorporates text from the United States National Library of Medicine, which is in the public domain.