ATG7: Lysates

Autophagy Related 7 (ATG7), also known as APG7-like Gene (APG7L), is a 703 amino acid (aa) noncanonical member of the Ubiquitin-activating (E1) enzyme family with a predicted molecular weight of 78 kDa. The mouse and rat ATG7 orthologs share 93% aa sequence identity with the human protein. While ATG7 lacks a Ubiquitin fold domain, it contains a conserved metal binding domain, an active site cysteine residue, Cys572 in humans, and an ATP-binding domain common to E1 enzyme family members. ATG7 is highly conserved in eukaryotes and is widely expressed in cells and tissues including the kidney, liver, bone marrow, and lymph nodes. It functions as a homodimer to activate two Ubiquitin-like modifiers, ATG8 and ATG12, through the creation of similar ATG7-ATG8 or ATG7-ATG12 conjugates via a thioester bond. Two human isoforms of ATG7 have been identified, the full length protein and a truncated protein that lacks the C-terminal portion, aa 626-652, required for ATG8 lipidation, which is involved in autophagosomal membrane formation. ATG7 is a critical mediator of macroautophagy and has been shown to mediate lysosomal photodamage, p53-mediated regulation of the cell cycle and survival during metabolic stress, mitochondrial removal during erythropoiesis, and maintenance of hematopoietic stem cell and axonal homeostasis.