The DEP domain is a globular domain of about 80 residues that is found in more than 50 proteins involved in G protein signaling pathways. It has been named after the three proteins (Dishevelled, Egl-10, and Pleckstrin) in which it was initially identified [1]. It has been proposed that the DEP domain could play a selective role in targeting DEP domain-containing proteins to specific subcellular membranous sites, perhaps even to specific G protein-coupled signaling pathways [2,3].

Nuclear magnetic resonance spectroscopy has revealed that the DEP domain comprises a three-helix bundle, a β-hairpin 'arm' composed of two β-strands and two short β-strands in the C-terminal region [3].

Representative example of proteins containing DEP domains are listed below:

• Drosophila and vertebrate dishevelled (Dsh and Dvl), proteins that play a key role in the transduction of the Wg/Wnt signal from the cell surface to the nucleus.
• Vertebrate Pleckstrin, the major substrate of protein kinase C in platelets. Pleckstrin contains two PH domains (see <PDOC50003>) flanking the DEP domain.
• Mammalian regulator of G-protein signaling (RGS) proteins 6, 7, 9 and 11 (see <PDOC50132>).
• Caenorhabditis elegans egl-10, which regulates G protein signaling in nervous system.

The profile we developed covers the entire DEP domain.