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DH/PH RhoGEF domain
Structure of the RhoGEF domain from the human Son of sevenless protein, an example of a DH/PH domain RhoGEF. [1]
Identifiers
SymbolRhoGEF
Pfam PF00621
InterPro IPR035899 IPR000219, IPR035899
SMART RhoGEF
SCOP2 1dbh / SCOPe / SUPFAM
OPM protein 1xd4
CDD cd00160
Available protein structures:
Pfam   structures / ECOD  
PDB RCSB PDB; PDBe; PDBj
PDBsum structure summary
PDB 1foeE:1044-1233 1f5xA:198-372 1ki1D:1241-1422

1ntyA:1237-1407 1kzgC:636-811 1lb1C:636-811 1kz7C:636-811 1rj2D:511-686 1xcgE:738-922 1txdA:791-976 1x86E:791-976 1by1A:275-450

1dbhA:204-389 1xdvB:204-389 1xd4A:204-389
Dedicator of cytokinesis (DOCK) RhoGEF domain
Identifiers
SymbolRhoGEF
Pfam PF06920
InterPro IPR010703 IPR026791, IPR010703
SCOP2 1wg7 / SCOPe / SUPFAM
CDD cd11684
Available protein structures:
Pfam   structures / ECOD  
PDB RCSB PDB; PDBe; PDBj
PDBsum structure summary
PDB 1wg7

RhoGEF domain describes two distinct structural domains with guanine nucleotide exchange factor (GEF) activity to regulate small GTPases in the Rho family. Rho small GTPases are inactive when bound to GDP but active when bound to GTP; RhoGEF domains in proteins are able to promote GDP release and GTP binding to activate specific Rho family members, including RhoA, Rac1 and Cdc42.

The largest class of RhoGEFs is composed of proteins containing the " Dbl-homology" (DH) domain, which almost always is found together with a pleckstrin-homology (PH) domain to form a combined DH/PH domain structure. [2] [3]

A distinct class of RhoGEFs is those proteins containing the DOCK/CZH/DHR-2 domain. This structure has no sequence similarity with DBL-homology domains. [4]

Human proteins containing DH/PH RhoGEF domain

ABR; AKAP13/ARHGEF13/Lbc; ALS2; ALS2CL; ARHGEF1/p115-RhoGEF; ARHGEF10; ARHGEF10L; ARHGEF11/PDZ-RhoGEF.; ARHGEF12/LARG; ARHGEF15; ARHGEF16; ARHGEF17; ARHGEF18; ARHGEF19; ARHGEF2; ARHGEF25; ARHGEF26; ARHGEF28; ARHGEF3; ARHGEF33; ARHGEF35; ARHGEF37; ARHGEF38; ARHGEF39; ARHGEF4; ARHGEF40; ARHGEF5; ARHGEF6/alpha-PIX; ARHGEF7/beta-PIX; ARHGEF9; BCR; DNMBP; ECT2; ECT2L; FARP1; FARP2; FGD1; FGD2; FGD3; FGD4; FGD5; FGD6; ITSN1/Intersectin 1; ITSN2/Intersectin 2; KALRN/Kalirin; MCF2; MCF2L; MCF2L2; NET1; NGEF; OBSCN; PLEKHG1; PLEKHG2; PLEKHG3; PLEKHG4; PLEKHG4B; PLEKHG5; PLEKHG6; PREX1; PREX2; RASGRF1; RASGRF2; SPATA13; TIAM1; TIAM2; TRIO; VAV1; VAV2; VAV3.

Human proteins containing DOCK/CZH RhoGEF domain

DOCK1/DOCK180; DOCK2; DOCK3/MOCA; DOCK4; DOCK5; DOCK6/ZIR1; DOCK7/ZIR2; DOCK8/ZIR3; DOCK9/Zizimin1; DOCK10/Zizimin2; DOCK11/Zizimin3

See also

References

  1. ^ Soisson SM, Nimnual AS, Uy M, Bar-Sagi D, Kuriyan J (October 1998). "Crystal structure of the Dbl and pleckstrin homology domains from the human Son of sevenless protein". Cell. 95 (2): 259–68. doi: 10.1016/S0092-8674(00)81756-0. PMID  9790532. S2CID  11868669.
  2. ^ Fort P, Blangy A (June 2017). "The Evolutionary Landscape of Dbl-Like RhoGEF Families: Adapting Eukaryotic Cells to Environmental Signals". Genome Biology and Evolution. 9 (6): 1471–1486. doi: 10.1093/gbe/evx100. PMC  5499878. PMID  28541439.
  3. ^ Cerione RA, Zheng Y (April 1996). "The Dbl family of oncogenes". Current Opinion in Cell Biology. 8 (2): 216–22. doi: 10.1016/s0955-0674(96)80068-8. PMID  8791419.
  4. ^ Côté JF, Vuori K (December 2002). "Identification of an evolutionarily conserved superfamily of DOCK180-related proteins with guanine nucleotide exchange activity". Journal of Cell Science. 115 (Pt 24): 4901–13. doi: 10.1242/jcs.00219. PMID  12432077.

Further reading