Search Results
Overview
| Uniprot ID | Q676U5 |
|---|---|
| Protein Name | Autophagy-related protein 16-1 |
| Gene Name | ATG16L1 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 222 | RRQARLQKELAEAAK |
Function
Plays an essential role in both canonical and non-canonical autophagy: interacts with ATG12-ATG5 to mediate the lipidation to ATG8 family proteins (MAP1LC3A, MAP1LC3B, MAP1LC3C, GABARAPL1, GABARAPL2 and GABARAP) (PubMed:23376921, PubMed:23392225, PubMed:24553140, PubMed:24954904, PubMed:27273576, PubMed:29317426, PubMed:30778222, PubMed:33909989). Acts as a molecular hub, coordinating autophagy pathways via distinct domains that support either canonical or non-canonical signaling (PubMed:29317426, PubMed:30778222). During canonical autophagy, interacts with ATG12-ATG5 to mediate the conjugation of phosphatidylethanolamine (PE) to ATG8 proteins, to produce a membrane-bound activated form of ATG8 (PubMed:23376921, PubMed:23392225, PubMed:24553140, PubMed:24954904, PubMed:27273576). Thereby, controls the elongation of the nascent autophagosomal membrane (PubMed:23376921, PubMed:23392225, PubMed:24553140, PubMed:24954904, PubMed:27273576). As part of the ATG8 conjugation system with ATG5 and ATG12, required for recruitment of LRRK2 to stressed lysosomes and induction of LRRK2 kinase activity in response to lysosomal stress (By similarity). Also involved in non-canonical autophagy, a parallel pathway involving conjugation of ATG8 proteins to single membranes at endolysosomal compartments, probably by catalyzing conjugation of phosphatidylserine (PS) to ATG8 (PubMed:33909989). Non-canonical autophagy plays a key role in epithelial cells to limit lethal infection by influenza A (IAV) virus (By similarity). Regulates mitochondrial antiviral signaling (MAVS)-dependent type I interferon (IFN-I) production (PubMed:22749352, PubMed:25645662). Negatively regulates NOD1- and NOD2-driven inflammatory cytokine response (PubMed:24238340). Instead, promotes an autophagy-dependent antibacterial pathway together with NOD1 or NOD2 (PubMed:20637199). Plays a role in regulating morphology and function of Paneth cell (PubMed:18849966)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0034274 | Atg12-Atg5-Atg16 complex |
| Cellular Component | GO:0005776 | autophagosome |
| Cellular Component | GO:0000421 | autophagosome membrane |
| Cellular Component | GO:0030424 | axon |
| Cellular Component | GO:0005930 | axoneme |
| Cellular Component | GO:0005829 | cytosol |
| Cellular Component | GO:0036020 | endolysosome membrane |
| Cellular Component | GO:0098978 | glutamatergic synapse |
| Cellular Component | GO:0034045 | phagophore assembly site membrane |
| Cellular Component | GO:0097225 | sperm midpiece |
| Cellular Component | GO:0120095 | vacuole-isolation membrane contact site |
| Molecular Function | GO:0051020 | GTPase binding |
| Molecular Function | GO:0042802 | identical protein binding |
| Molecular Function | GO:0043495 | protein-membrane adaptor activity |
| Molecular Function | GO:0019787 | ubiquitin-like protein transferase activity |
| Biological Process | GO:0000045 | autophagosome assembly |
| Biological Process | GO:0098930 | axonal transport |
| Biological Process | GO:0006501 | C-terminal protein lipidation |
| Biological Process | GO:0051607 | defense response to virus |
| Biological Process | GO:0016236 | macroautophagy |
| Biological Process | GO:0016237 | microautophagy |
| Biological Process | GO:0010508 | positive regulation of autophagy |
| Biological Process | GO:0034497 | protein localization to phagophore assembly site |
| Biological Process | GO:0015031 | protein transport |
Reference
[1] Yang Z, Yan C, Ma J, Peng P, Ren X et al.. Lactylome analysis suggests lactylation-dependent mechanisms of metabolic adaptation in hepatocellular carcinoma.. Nat Metab 5(1):61-79. 2023 Jan. PMID: 36593272.
[2] Wu Q, Li Z, Gong T, Zheng X, Zhou X et al.. Porphyromonas gingivalis infection induces lysine lactylation reprogramming in human umbilical vein endothelial cells.. Front Cell Infect Microbiol 16:1706727. 2026. PMID: 41696360.