Atg16l1
entrez
77040
canonical
uniprot
Q8C0J2
canonical
ensembl
ENSMUSG00000026289
resolver
ensp
ENSMUSP00000027512
resolver
ensp
ENSMUSP00000108811
resolver
ensp
ENSMUSP00000108815
resolver
ensp
ENSMUSP00000234894
resolver
genesymbol
Atg16l1
resolver
genesymbol_syn
Apg16l
resolver
genesymbol_syn
Atg16L1 gamma
resolver
uniprot
G9M4M6
resolver
uniprot
Q3TDQ5
resolver
uniprot
Q6KAT7
resolver
uniprot
Q80U97
resolver
uniprot
Q80U98
resolver
uniprot
Q80U99
resolver
uniprot
Q80Y53
resolver
uniprot
Q9DB63
resolver
uniprot_entry
A16L1_MOUSE
resolver
uniprot_entry
G9M4M6_MOUSE
resolver
uniprot_entry
Q3TDQ5_MOUSE
resolver
uniprot_sec
Q6KAT7
resolver
uniprot_sec
Q80U97
resolver
uniprot_sec
Q80U98
resolver
uniprot_sec
Q80U99
resolver
uniprot_sec
Q80Y53
resolver
uniprot_sec
Q9DB63
resolver
amino_acid_sequence
MSSGLRAADFPRWKRHIAEELRRRDRLQRQAFEEIILQYTKLLEKSDLHSVLTQKLQAEKHDMPNRHEISPGHDGAWNDSQLQEMAQLRIKHQEELTELHKKRGELAQLVIDLNNQMQQKDKEIQMNEAKISEYLQTISDLETNCLDLRTKLQDLEVANQTLKDEYDALQITFTALEEKLRKTTEENQELVTRWMAEKAQEANRLNAENEKDSRRRQARLQKELAEAAKEPLPVEQDDDIEVIVDETSDHTEETSPVRAVSRAATKRLSQPAGGLLDSITNIFGRRSVSSIPVPQDIMDTHPASGKDVRVPTTASYVFDAHDGEVNAVQFSPGSRLLATGGMDRRVKLWEAFGDKCEFKGSLSGSNAGITSIEFDSAGAYLLAASNDFASRIWTVDDYRLRHTLTGHSGKVLSAKFLLDNARIVSGSHDRTLKLWDLRSKVCIKTVFAGSSCNDIVCTEQCVMSGHFDKKIRFWDIRSESVVREMELLGKITALDLNPERTELLSCSRDDLLKVIDLRTNAVKQTFSAPGFKCGSDWTRVVFSPDGSYVAAGSAEGSLYVWSVLTGKVEKVLSKQHSSSINAVAWAPSGLHVVSVDKGSRAVLWAQP
uniprot
proteins
function
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:12665549, PubMed:18849966, PubMed:19898471, PubMed:23392225, PubMed:24553140, PubMed:24954904, PubMed:33586810). Acts as a molecular hub, coordinating autophagy pathways via distinct domains that support either canonical or non-canonical signaling (PubMed:33586810). 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 (By similarity). Thereby, controls the elongation of the nascent autophagosomal membrane (By similarity). 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 (PubMed:38227290). 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 (By similarity). Non-canonical autophagy plays a key role in epithelial cells to limit lethal infection by influenza A (IAV) virus (PubMed:33586810). Regulates mitochondrial antiviral signaling (MAVS)-dependent type I interferon (IFN-I) production (By similarity). Negatively regulates NOD1- and NOD2-driven inflammatory cytokine response (PubMed:24238340). Instead, promotes an autophagy-dependent antibacterial pathway together with NOD1 or NOD2 (PubMed:19898471, PubMed:19966812, PubMed:24238340). Plays a role in regulating morphology and function of Paneth cell (By similarity). {ECO:0000250|UniProtKB:Q676U5, ECO:0000269|PubMed:12665549, ECO:0000269|PubMed:18849966, ECO:0000269|PubMed:19898471, ECO:0000269|PubMed:19966812, ECO:0000269|PubMed:23392225, ECO:0000269|PubMed:24238340, ECO:0000269|PubMed:24553140, ECO:0000269|PubMed:24954904, ECO:0000269|PubMed:33586810, ECO:0000269|PubMed:38227290}.
uniprot
proteins
mass_dalton
68172
uniprot
proteins
mutagenesis
MUTAGEN 231..607; /note="Missing: Impaired non-canonical autophagy, leading to susceptibility to influenza A virus (IAV) infection in mice."; /evidence="ECO:0000269|PubMed:33586810"; MUTAGEN 299; /note="D->E: Prevents cleavage by activated CASP3."; /evidence="ECO:0000269|PubMed:24553140"; MUTAGEN 300; /note="T->A: No effect on the stability of the protein under normal conditions. Enhances cleavage and degradation mediated by activated CASP3 and CASP7. Results in reduced autophagy and defective clearance of intestinal pathogens. Increases secretion of pro-inflammatory cytokine IL1B and type IIFN."; /evidence="ECO:0000269|PubMed:24553140, ECO:0000269|PubMed:24821797
uniprot
proteins
post_translational_modification
PTM: Proteolytic cleavage by activated CASP3 leads to degradation and may regulate autophagy upon cellular stress and apoptotic stimuli. {ECO:0000269|PubMed:24553140}.; PTM: Phosphorylation at Ser-139 promotes association with the ATG12-ATG5 conjugate to form the ATG12-ATG5-ATG16L1 complex. {ECO:0000250|UniProtKB:Q676U5}.
uniprot
proteins
protein_family
WD repeat ATG16 family
uniprot
proteins
pubmed
12665549
uniprot
proteins
pubmed
15449545
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
18448665
uniprot
proteins
pubmed
18849966
uniprot
proteins
pubmed
19898471
uniprot
proteins
pubmed
19966812
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
22082872
uniprot
proteins
pubmed
23262492
uniprot
proteins
pubmed
23392225
uniprot
proteins
pubmed
24089209
uniprot
proteins
pubmed
24238340
uniprot
proteins
pubmed
24553140
uniprot
proteins
pubmed
24821797
uniprot
proteins
pubmed
24954904
uniprot
proteins
pubmed
32960676
uniprot
proteins
pubmed
33087875
uniprot
proteins
pubmed
33586810
uniprot
proteins
pubmed
38227290
uniprot
proteins
sequence_length
607
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:33087875}. Preautophagosomal structure membrane {ECO:0000269|PubMed:24954904}; Peripheral membrane protein {ECO:0000305}. Endosome membrane {ECO:0000250|UniProtKB:Q676U5}; Peripheral membrane protein {ECO:0000305}. Lysosome membrane {ECO:0000250|UniProtKB:Q676U5}; Peripheral membrane protein {ECO:0000305}. Note=Recruited to omegasomes membranes by WIPI2 (PubMed:24954904). Omegasomes are endoplasmic reticulum connected strutures at the origin of preautophagosomal structures. Localized to preautophagosomal structure (PAS) where it is involved in the membrane targeting of ATG5 (PubMed:24954904). Localizes also to discrete punctae along the ciliary axoneme (PubMed:24954904). Upon activation of non-canonical autophagy, recruited to single-membrane endolysosomal compartments (By similarity). Under starved conditions, the ATG12-ATG5-ATG16L1 complex is translocated to phagophores driven by RAB33B (By similarity). {ECO:0000250|UniProtKB:Q676U5, ECO:0000269|PubMed:24954904}.
uniprot
proteins