A novel member of the vesicle-associated membrane protein (VAMP):synaptobrevin family, VAMP-3 is a v-SNARE protein that resides in recycling endosomes and endosome-derived transport vesicles. It colocalizes with endocytosed transferrin receptors and the glucose transporter GLUT4 in adipocytes, and is also present in alpha-granules in platelets. The protein has been implicated in recycling of transferrin receptors to the plasma membrane, secretion of alpha-granules in platelets, recycling of T-cell receptors to the immunological synapses, and membrane trafficking during cell migration. It is a homologue of VAMP-2 and has a broad tissue distribution in humans. Like VAMP-2, it can be cleaved by tetanus toxin, a metallo-endoprotease which blocks synaptic exocytosis. In humans, the VAMP-3 gene is mapped to chromosome 1p36.23.
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