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RhoGEF domain

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Protein domain
Protein domain
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 1foe E:1044-1233 1f5x A:198-372 1ki1 D:1241-1422

1nty A:1237-1407 1kzg C:636-811 1lb1 C:636-811 1kz7 C:636-811 1rj2 D:511-686 1xcg E:738-922 1txd A:791-976 1x86 E:791-976 1by1 A:275-450

1dbh A:204-389 1xdv B:204-389 1xd4 A:204-389
Protein domain
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

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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

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

See also

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References

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  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

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