|
General Comment |
ADP-ribosylation factors (ARFs), small guanine nucleotide-binding proteins that enhance the enzymatic activities of cholera toxin, constitute 1 family of the RAS superfamily. Monomeric guanine nucleotide-binding proteins of the RAS superfamily function in a variety of cellular processes including signaling, growth, immunity, and protein transport. ARFs are essential and ubiquitous in eukaryotes, being involved in vesicular transport and functioning as activators of phospholipase D. The functions of ARF proteins in membrane traffic and organelle integrity are intimately tied to their reversible association with membranes and specific interactions with membrane phospholipids. A common feature of these functions is their regulation by the binding and hydrolysis of GTP. Monaco et al. (1990) used degenerate PCR with genomic DNA to identify a member of the human ADP-ribosylation factor (ARF) gene family. The gene, designated ARF4, encodes a predicted 180-amino acid protein that is approximately 80% identical to the other human ARFs
NCBI Summary:
ADP-ribosylation factor 4 (ARF4) is a member of the human ARF gene family. These genes encode small guanine nucleotide-binding proteins that stimulate the ADP-ribosyltransferase activity of cholera toxin and play a role in vesicular trafficking and as activators of phospholipase D. The gene products include 6 ARF proteins and 11 ARF-like proteins and constitute 1 family of the RAS superfamily. The ARF proteins are categorized as class I (ARF1, ARF2,and ARF3), class II (ARF4 and ARF5) and class III (ARF6). The members of each class share a common gene organization. The ARF4 gene spans approximately 12kb and contains six exons and five introns. The ARF4 is the most divergent member of the human ARFs. Conflicting Map positions at 3p14 or 3p21 have been reported for this gene.
|