v5.1.0.3
Cicer data from the Legume Information System
| Type | Domain |
| Description | DOCK family members are evolutionarily conserved guanine nucleotide exchange factors (GEFs) for Rho-family GTPases [ ]. DOCK proteins are required during several cellular processes, such as cell motility and phagocytosis. The N-terminal SH3 domain of the DOCK proteins functions as an inhibitor of GEF, which can be relieved upon its binding to the ELMO1-3 adaptor proteins, after their binding to active RhoG at the plasma membrane [, ]. DOCK family proteins are categorised into four subfamilies based on their sequence homology: DOCK-A subfamily (DOCK1/180, 2, 5), DOCK-B subfamily (DOCK3, 4), DOCK-C subfamily (DOCK6, 7, 8), DOCK-D subfamily (DOCK9, 10, 11) []. All DOCKs contain two homology domains: the DHR-1 (Dock homology region-1), also called CZH1 (CED-5, Dock180, and MBC-zizimin homology 1), and DHR-2 (also called CZH2 or Docker). DOCK5 is an atypical guanine nucleotide exchange factor (GEF) that lacks the conventional Dbl homology (DH) domain. It functions upstream of Rac1 to regulate osteoclast function [ ]. Along with DOCK1, DOCK5 mediates CRK/CRKL regulation of epithelial and endothelial cell spreading and migration on collagen IV [].This entry represents the DHR-2 domain of DOCK5, which contains the catalytic GEF activity for Rac and/or Cdc42. Class A DOCKs, like DOCK5, are specific GEFs for Rac. |
| Short Name | DHR2_DOCK5 |