ARD1 was first described in 1993 as the deduced protein product of clones isolated from human and rat genomic cDNA libraries that encoded an about 18-kDa ADP-ribosylation factor (Arf) sequence at the C-terminus of a 64-kDa molecule (Mishima et al. 1993). Human ARD1 coding region cDNA hybridized with 3.7- and 4.1-kb mRNAs from all rat tissues examined. Both recombinant, full-length ARD1 and its Arf domain (M403-A574), activated cholera toxin ADP-ribosyltransferase activity, at that time a defining characteristic of Arf function, whereas the non-Arf (M1-K402) fragment of ARD1 did not. Using recombinant proteins on nitrocellulose membranes, only the Arf domain (and a recombinant ARF3), not the full-length ARD1, bound radio-labeled GTP (Mishima et al. 1993).
Further investigation of GTPase activity of the same recombinant proteins in solution provided evidence that...
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