InterPro domain: IPR027714

This entry includes the yeast Fyv10 protein and the animal E3 ubiquitin-protein transferase MAEA.

Rmd5 and Fyv10 form the heterodimeric E3 ligase unit of the Gid (glucose induced degradation deficient) complex, which is is involved in the proteasome-dependent degradation of fructose-1,6-bisphosphatase [ 1 , 2 ]. In Saccharomyces cerevisiae, it is required for survival upon exposure to K1 killer toxin [ 3 ].

MAEA is a core component of the CTLH E3 ubiquitin-protein ligase complex that selectively accepts ubiquitin from UBE2H and mediates ubiquitination and subsequent proteasomal degradation of the transcription factor HBP1. MAEA and RMND5A are both required for catalytic activity of the CTLH E3 ubiquitin-protein ligase complex [ 4 ].

1. The yeast GID complex, a novel ubiquitin ligase (E3) involved in the regulation of carbohydrate metabolism. Mol. Biol. Cell 19, 3323-33
2. Gid9, a second RING finger protein contributes to the ubiquitin ligase activity of the Gid complex required for catabolite degradation. FEBS Lett. 585
3. A Saccharomyces cerevisiae genome-wide mutant screen for altered sensitivity to K1 killer toxin. Genetics 163, 875-94
4. The multi-subunit GID/CTLH E3 ubiquitin ligase promotes cell proliferation and targets the transcription factor Hbp1 for degradation. Elife 7, 3856-61