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Stromal membrane-associated protein 2 (SMAP2) is a cytoplasmic GTPase-activating protein (GAP) primarily targeting the small GTPase ARF1 and, in vitro, ARF6. It plays a significant role in clathrin-dependent retrograde transport, specifically in the movement of vesicles from early endosomes to the trans-Golgi network. SMAP2 contains a conserved zinc finger motif required for its GAP activity, interacts with clathrin and clathrin adaptor proteins such as AP-1 and CALM, and is involved in precise regulation of vesicle budding and trafficking. The protein is mainly located in the cytosol and nucleoplasm, with expression in several tissues. Currently, there is no direct therapeutic targeting of SMAP2, and it is not recognized as a conventional drug target. However, mutations in SMAP2 have been associated with specific developmental disorders such as Kniest dysplasia and vitreous syneresis.
Not applicable (no known drug interactions)
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