This entry represents the C-terminal domain (CTD) (residues 1,291-1,603) of the DEPDC5 protein []. It contains two structurally similar lobes and has a pseudo-2-fold rotational symmetry. Each half consists of a five-stranded β-sheet, with an α-helix covering one side. The CTD is located in the core of DEPDC5 and contacts all the other domains of DEPDC5 except the NTD, making it the central organizer of this multi-domain protein [].
Proteins in this family contain a DEP domain, which is a globular domain of about 80 residues. This entry includes GTPase-activating proteins (GAPs), such as Iml1 from fungi and GATOR complex protein DEPDC5 from mammals. In Saccharomyces cerevisiae, Iml1 is a GAP subunit of both the SEA (Seh1-associated) and Iml1 complexes (Iml1-Npr2-Npr3). SEA complex is associates dynamically with the vacuole and is involved in autophagy [, , ]. Iml1 complex is required for non-nitrogen-starvation (NNS)-induced autophagy []. In mammals, DEPDC5 is a component of the GATOR1 complex functions as an inhibitor of the amino acid-sensing branch of the TORC1 pathway [, ].
