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Protein unc-13 homolog C (UNC13C), also known as Munc13-3, is a member of the Munc13 protein family that plays a critical role in the priming and regulation of synaptic vesicle exocytosis at presynaptic active zones in neurons[3][4][6]. UNC13C is essential for proper neurotransmitter release, particularly glutamate, and is highly expressed in the cerebellum where it is localized to the synaptic terminals of granule and Purkinje cells[3][4][6]. Its action is mediated through vesicle priming, facilitating SNARE complex assembly, and interacting with the diacylglycerol (DAG) pathway via its C1 and C2 domains, which are capable of calcium binding[3][5]. Loss of function in animal models results in reduced neurotransmitter release probability and impaired motor learning, but does not cause overt neurodevelopmental defects, likely due to redundancy among the Munc13 protein family members[4][6]. At present, UNC13C is not an established drug target or biomarker and has no known interacting therapeutics[3][4][6].
Not applicable. (No drugs reported to act on this protein.)
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