InterPro domain: IPR006285
General Information
- Identifier IPR006285
- Description Ubiquitin-like modifier-activating enzyme Atg7
- Number of genes 103
- Gene duplication stats Loading...
- Associated GO terms GO:0005737
Abstract
This is a family of eukaryotic proteins found in animals, plants, and yeasts that includes Atg7p (YHR171W) from Saccharomyces cerevisiae (Baker's yeast) and ATG7 from Pichia angusta. Members are about 650 to 700 residues in length and include a central domain of about 150 residues shared with the ThiF/MoeB/HesA family of proteins. A low level of similarity to ubiquitin-activating enzyme E1 is described in a paper on peroxisome autophagy mediated by ATG7 [ 1 ], and is the basis of the name ubiquitin activating enzyme E1-like protein. Members of the family are involved in protein lipidation events analogous to ubiquitination and required for membrane fusion events during autophagy.
This protein is important for several processes. It plays a key role in the maintenance of axonal homeostasis, the prevention of axonal degeneration [ 2 ], the maintenance of hematopoietic stem cells [ 3 ], the formation of Paneth cell granules [[cite22291845]], as well as in adipose differentiation [ 4 ]. It is involved in circadian clock regulation in the liver and glucose metabolism through the autophagic degradation of CRY1 (clock repressor) in a time-dependent manner [ 5 ].
1. ATG genes involved in non-selective autophagy are conserved from yeast to man, but the selective Cvt and pexophagy pathways also require organism-specific genes. Autophagy 3, 106-16
2. Essential role for autophagy protein Atg7 in the maintenance of axonal homeostasis and the prevention of axonal degeneration. Proc. Natl. Acad. Sci. U.S.A. 104, 14489-94
3. The autophagy protein Atg7 is essential for hematopoietic stem cell maintenance. J. Exp. Med. 208, 455-67
4. Adipose-specific deletion of autophagy-related gene 7 (atg7) in mice reveals a role in adipogenesis. Proc. Natl. Acad. Sci. U.S.A. 106, 19860-5
5. Autophagy Regulates the Liver Clock and Glucose Metabolism by Degrading CRY1. Cell Metab. 28, 268-281.e4