{PDOC50186}
{PS50186; DEP}
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* DEP domain profile *
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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 beta-hairpin 'arm' composed of two beta-
strands and two short beta-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.

-Sequences known to belong to this class detected by the profile: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.
-Last update: December 2001 / First entry.

[ 1] Ponting C.P., Bork P.
     "Pleckstrin's repeat performance: a novel domain in G-protein
     signaling?"
     Trends Biochem. Sci. 21:245-246(1996).
     PubMed=8755244
[ 2] Burchett S.A.
     "Regulators of G protein signaling: a bestiary of modular protein
     binding domains."
     J. Neurochem. 75:1335-1351(2000).
     PubMed=10987813
[ 3] Wong H.C., Mao J., Nguyen J.T., Srinivas S., Zhang W., Liu B., Li L.,
     Wu D., Zheng J.
     "Structural basis of the recognition of the dishevelled DEP domain in
     the Wnt signaling pathway."
     Nat. Struct. Biol. 7:1178-1184(2000).
     PubMed=11101902; DOI=10.1038/82047

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