Anti-APG16L

ATG16L1/APG16L is part of a large protein complex that functions as a molecular scaffold mediating protein-protein interactions necessary for formation of the autophagosome in response to both classical and pathogen-related autophagy stimuli. APG16L protein contains an N-terminal Atg5-binding domain, a coiled-coil domain and a C-terminal WD (tryptophan-aspartic acid)-repeat domain. APG16L forms a complex with the Atg12 Atg5 conjugate and together they are actively translocated to the phagophore and are further elongated during autophagosome formation. Genetic variation in the APG16L gene has been recently implicated in Crohn's disease pathogenesis. Polymorphism within APG16L gene results in excessive production of IL-1beta and IL-6 culmunating in the inflammatory process in Crohn's disease. Protein function: Plays an essential role in autophagy: interacts with ATG12-ATG5 to mediate the conjugation of phosphatidylethanolamine (PE) to LC3 (MAP1LC3A, MAP1LC3B or MAP1LC3C), to produce a membrane-bound activated form of LC3 named LC3-II. Thereby, controls the elongation of the nascent autophagosomal membrane (PubMed:24553140, PubMed:23376921, PubMed:24954904, PubMed:27273576, PubMed:23392225). Regulates mitochondrial antiviral signaling (MAVS)-dependent type I interferon (IFN-I) production (PubMed:25645662). Negatively regulates NOD1- and NOD2- driven inflammatory cytokine response (PubMed:24238340). Instead, promotes with NOD2 an autophagy-dependent antibacterial pathway (PubMed:20637199). Plays a role in regulating morphology and function of Paneth cell (PubMed:18849966). [The UniProt Consortium]