GTP-binding protein ARD-1 is a protein that in humans is encoded by the TRIM23gene.
The protein encoded by this gene is a member of the tripartite motif (TRIM) family. The TRIM motif includes three zinc-binding domains, a RING, a B-box type 1 and a B-box type 2, and a coiled-coil region. This protein is also a member of the ADP ribosylation factor family of guanine nucleotide-binding family of proteins. Its carboxy terminus contains an ADP-ribosylation factor domain and a guanine nucleotide binding site, while the amino terminus contains a GTPase activating protein domain which acts on the guanine nucleotide binding site. The protein localizes to lysosomes and the Golgi apparatus. It plays a role in the formation of intracellular transport vesicles, their movement from one compartment to another, and phospholipase D activation. Three alternatively spliced transcript variants for this gene have been described.
Vitale N, Moss J, Vaughan M (1997). "Characterization of a GDP dissociation inhibitory region of ADP-ribosylation factor domain protein ARD1". J. Biol. Chem.272 (40): 25077–82. doi:10.1074/jbc.272.40.25077. PMID9312116.
Vitale N, Moss J, Vaughan M (1998). "Molecular characterization of the GTPase-activating domain of ADP-ribosylation factor domain protein 1 (ARD1)". J. Biol. Chem.273 (5): 2553–60. doi:10.1074/jbc.273.5.2553. PMID9446556.
Vitale N, Pacheco-Rodriguez G, Ferrans VJ, et al. (2000). "Specific functional interaction of human cytohesin-1 and ADP-ribosylation factor domain protein (ARD1)". J. Biol. Chem.275 (28): 21331–9. doi:10.1074/jbc.M909642199. PMID10748148.