The domain within your query sequence starts at position 349 and ends at position 422; the E-value for the DEP domain shown below is 3.06e-24.

LYAPVIKDRDYHLKTYKSVVPGSKLVDWLLAQGDCQTREEAVALGVGLCNNGFMHHVLEK
SEFKDESQYFRFHA

DEP

Domain found in Dishevelled, Egl-10, and Pleckstrin

• SMART accession number: SM00049
• Description: Domain of unknown function present in signalling proteins that contain PH, rasGEF, rhoGEF, rhoGAP, RGS, PDZ domains. DEP domain in Drosophila dishevelled is essential to rescue planar polarity defects and induce JNK signalling (Cell 94, 109-118).
• Interpro abstract (IPR000591):

  This entry represents the DEP (Dishevelled, Egl-10 and Pleckstrin) domain, a globular domain of about 80 residues that is found in over 50 proteins involved in G-protein signalling pathways. It was named after the three proteins it was initially found in:

  • Dishevelled (Dsh and Dvl), which play a key role in the transduction of the Wg/Wnt signal from the cell surface to the nucleus; it is a segment polarity protein required to establish coherent arrays of polarized cells and segments in embryos, and plays a role in wingless signalling.
  • Egl-10, which regulates G-protein signalling in the central nervous system.
  • Pleckstrin, the major substrate of protein kinase C in platelets; Pleckstrin contains two PH domains flanking the DEP domain.

  Mammalian regulators of G-protein signalling also contain these domains, and regulate signal transduction by increasing the GTPase activity of G-protein alpha subunits, thereby driving them into their inactive GDP-bound form. 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 [ (PUBMED:10987813) (PUBMED:11101902) ]. 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 [ (PUBMED:11101902) ].

• GO process: intracellular signal transduction (GO:0035556)

There are 13900 DEP domains in 12135 proteins in SMART's nrdb database.

Cellular role (predicted cellular role)

Binding / catalysis: unknown

Literature (relevant references for this domain)

Primary literature is listed below; Automatically-derived, secondary literature is also avaliable.

• Ponting CP, Bork P
• Pleckstrin's repeat performance: a novel domain in G-protein signaling?
• Trends Biochem Sci. 1996; 21: 245-6

• Mayer BJ, Ren R, Clark KL, Baltimore D
• A putative modular domain present in diverse signaling proteins.
• Cell. 1993; 73: 629-30

Metabolism (metabolic pathways involving proteins which contain this domain)

% proteins involved	KEGG pathway ID	Description
14.37	map04310	Wnt signaling pathway
14.37	map05210	Colorectal cancer
14.37	map05217	Basal cell carcinoma
14.37	map04916	Melanogenesis
14.37	map04330	Notch signaling pathway
8.98	map04670	Leukocyte transendothelial migration
4.79	map04810	Regulation of actin cytoskeleton
4.79	map00562	Inositol phosphate metabolism
4.79	map04720	Long-term potentiation
4.79	map04070	Phosphatidylinositol signaling system

This information is based on mapping of SMART genomic protein database to KEGG orthologous groups. Percentage points are related to the number of proteins with DEP domain which could be assigned to a KEGG orthologous group, and not all proteins containing DEP domain. Please note that proteins can be included in multiple pathways, ie. the numbers above will not always add up to 100%.

Structure (3D structures containing this domain)

3D Structures of DEP domains in PDB

PDB code	Title
1fsh	STRUCTURAL BASIS OF THE RECOGNITION OF THE DISHEVELLED DEP DOMAIN IN THE WNT SIGNALING PATHWAY
1o7f	CRYSTAL STRUCTURE OF THE REGULATORY DOMAIN OF EPAC2
1uhw	Solution structure of the DEP domain of mouse pleckstrin
1v3f	Solution structure of the DEP domain of mouse pleckstrin2
1w4m	Structure of the human pleckstrin DEP domain by multidimensional NMR
2byv	Structure of the cAMP responsive exchange factor Epac2 in its auto- inhibited state
2cso	Solution structure of the DEP domain of human pleckstrin
2pbi	The multifunctional nature of Gbeta5/RGS9 revealed from its crystal structure
2ysr	Solution structure of the DEP domain from human DEP domain-containing protein 1
3ml6	a complex between Dishevlled2 and clathrin adaptor AP-2
4f7z	Conformational dynamics of exchange protein directly activated by cAMP
5lnp	5LNP
5suy	5SUY
5suz	5SUZ

Links (links to other resources describing this domain)

• INTERPRO: IPR000591