Member database | Pfam |
Pfam type | domain |
Short name | ATG5_UblB |
Clan | Ubiquitin |
Author | Wood V;0000-0001-6330-7526 Finn RD;0000-0001-8626-2148 |
Sequence Ontology | 0000417 |
Description
ATG5 is directly required for the import of aminopeptidase I via the cytoplasm-to-vacuole targeting pathway
[2]. ATG5 is conjugated to ATG12; this conjugate exhibits E3 ligase-like activity which facilitates the lipidation of members of the LC3 family, and therefore autophagosome formation
[3]. ATG5 comprises N- and C-terminal ubiquitin-like domains (UblA and UblB) that flank the helical-rich region (HBR). This is the UblB domain, found at the C-terminal
[3, 1].
References
1.Structure of Atg5.Atg16, a complex essential for autophagy. Matsushita M, Suzuki NN, Obara K, Fujioka Y, Ohsumi Y, Inagaki F. J. Biol. Chem. 282, 6763-72, (2007). View articlePMID: 17192262
2.Apg5p functions in the sequestration step in the cytoplasm-to-vacuole targeting and macroautophagy pathways. George MD, Baba M, Scott SV, Mizushima N, Garrison BS, Ohsumi Y, Klionsky DJ. Mol. Biol. Cell 11, 969-82, (2000). View articlePMID: 10712513
3.Structure of the human ATG12~ATG5 conjugate required for LC3 lipidation in autophagy. Otomo C, Metlagel Z, Takaesu G, Otomo T. Nat. Struct. Mol. Biol. 20, 59-66, (2013). View articlePMID: 23202584