Description
Product Characteristics:
E2 conjugating enzyme required for the cytoplasm to vacuole transport (Cvt), autophagy, and mitochondrial homeostasis. Responsible for the E2-like covalent binding of phosphatidylethanolamine to the C-terminal Gly of ATG8-like proteins (GABARAP, GABARAPL1, GABARAPL2 or MAP1LC3A). The ATG12-ATG5 conjugate plays a role of an E3 and promotes the transfer of ATG8-like proteins from ATG3 to phosphatidylethanolamine (PE). This step is required for the membrane association of ATG8-like proteins. The formation of the ATG8-phosphatidylethanolamine conjugates is essential for autophagy and for the cytoplasm to vacuole transport (Cvt). Preferred substrate is MAP1LC3A. Also acts as an autocatalytic E2-like enzyme, catalyzing the conjugation of ATG12 to itself, ATG12 conjugation to ATG3 playing a role in mitochondrial homeostasis but not in autophagy. ATG7 (E1-like enzyme) facilitates this reaction by forming an E1-E2 complex with ATG3. Promotes primary ciliogenesis by removing OFD1 from centriolar satellites via the autophagic pathway.
Subcellular location: Cytoplasm
Synonyms: APG3, APG3L, PC3-96, APG3-LIKE, Ubiquitin-like-conjugating enzyme ATG3, Autophagy-related protein 3, hApg3, Protein PC3-96, ATG3
Target Information: Autophagy is a process of bulk degradation of cytoplasmic components by the lysosome or vacuole. Human ATG3 displays the same enzymatic characteristics in vitro as yeast Apg3, a protein-conjugating enzyme essential for autophagy (Tanida et al., 2002 [PubMed 11825910]).[supplied by OMIM, Mar 2008]