ATG16L1
entrez
55054
canonical
uniprot
Q676U5
canonical
ensembl
ENSG00000085978
resolver
ensembl
ENSG00000281089
resolver
ensp
ENSP00000318259
resolver
ensp
ENSP00000375872
resolver
ensp
ENSP00000375873
resolver
ensp
ENSP00000375875
resolver
ensp
ENSP00000486603
resolver
ensp
ENSP00000575998
resolver
ensp
ENSP00000576000
resolver
ensp
ENSP00000632417
resolver
ensp
ENSP00000680004
resolver
enst
ENST00000392018
resolver
enst
ENST00000626639
resolver
genesymbol
ATG16L1
resolver
genesymbol_syn
APG16L
resolver
hgnc
HGNC:21498
resolver
uniprot
A0A0G2JRB6
resolver
uniprot
A3EXK9
resolver
uniprot
A3EXL0
resolver
uniprot
B6ZDH0
resolver
uniprot
E7EVC7
resolver
uniprot
Q17RG0
resolver
uniprot
Q6IPN1
resolver
uniprot
Q6UXW4
resolver
uniprot
Q6ZVZ5
resolver
uniprot
Q8NCY2
resolver
uniprot
Q96JV5
resolver
uniprot
Q9H619
resolver
uniprot_entry
A0A0G2JRB6_HUMAN
resolver
uniprot_entry
A16L1_HUMAN
resolver
uniprot_entry
E7EVC7_HUMAN
resolver
uniprot_entry
Q17RG0_HUMAN
resolver
uniprot_sec
A3EXK9
resolver
uniprot_sec
A3EXL0
resolver
uniprot_sec
B6ZDH0
resolver
uniprot_sec
Q6IPN1
resolver
uniprot_sec
Q6UXW4
resolver
uniprot_sec
Q6ZVZ5
resolver
uniprot_sec
Q8NCY2
resolver
uniprot_sec
Q96JV5
resolver
uniprot_sec
Q9H619
resolver
amino_acid_sequence
MSSGLRAADFPRWKRHISEQLRRRDRLQRQAFEEIILQYNKLLEKSDLHSVLAQKLQAEKHDVPNRHEISPGHDGTWNDNQLQEMAQLRIKHQEELTELHKKRGELAQLVIDLNNQMQRKDREMQMNEAKIAECLQTISDLETECLDLRTKLCDLERANQTLKDEYDALQITFTALEGKLRKTTEENQELVTRWMAEKAQEANRLNAENEKDSRRRQARLQKELAEAAKEPLPVEQDDDIEVIVDETSDHTEETSPVRAISRAATKRLSQPAGGLLDSITNIFGRRSVSSFPVPQDNVDTHPGSGKEVRVPATALCVFDAHDGEVNAVQFSPGSRLLATGGMDRRVKLWEVFGEKCEFKGSLSGSNAGITSIEFDSAGSYLLAASNDFASRIWTVDDYRLRHTLTGHSGKVLSAKFLLDNARIVSGSHDRTLKLWDLRSKVCIKTVFAGSSCNDIVCTEQCVMSGHFDKKIRFWDIRSESIVREMELLGKITALDLNPERTELLSCSRDDLLKVIDLRTNAIKQTFSAPGFKCGSDWTRVVFSPDGSYVAAGSAEGSLYIWSVLTGKVEKVLSKQHSSSINAVAWSPSGSHVVSVDKGCKAVLWAQY
uniprot
proteins
disease_involvement
DISEASE: Inflammatory bowel disease 10 (IBD10) [MIM:611081]: A chronic, relapsing inflammation of the gastrointestinal tract with a complex etiology. It is subdivided into Crohn disease and ulcerative colitis phenotypes. Crohn disease may affect any part of the gastrointestinal tract from the mouth to the anus, but most frequently it involves the terminal ileum and colon. Bowel inflammation is transmural and discontinuous; it may contain granulomas or be associated with intestinal or perianal fistulas. In contrast, in ulcerative colitis, the inflammation is continuous and limited to rectal and colonic mucosal layers; fistulas and granulomas are not observed. Both diseases include extraintestinal inflammation of the skin, eyes, or joints. {ECO:0000269|PubMed:17200669, ECO:0000269|PubMed:17435756, ECO:0000269|PubMed:17484864, ECO:0000269|PubMed:18047540, ECO:0000269|PubMed:18499543, ECO:0000269|PubMed:18985712, ECO:0000269|PubMed:19659808, ECO:0000269|PubMed:24656308}. Note=Disease susceptibility is associated with variants affecting the gene represented in this entry.
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: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). {ECO:0000250|UniProtKB:Q8C0J2, ECO:0000269|PubMed:18849966, ECO:0000269|PubMed:20637199, ECO:0000269|PubMed:22749352, ECO:0000269|PubMed:23376921, ECO:0000269|PubMed:23392225, ECO:0000269|PubMed:24238340, ECO:0000269|PubMed:24553140, ECO:0000269|PubMed:24954904, ECO:0000269|PubMed:25645662, ECO:0000269|PubMed:27273576, ECO:0000269|PubMed:29317426, ECO:0000269|PubMed:30778222, ECO:0000269|PubMed:33909989}.
uniprot
proteins
mass_dalton
68265
uniprot
proteins
mutagenesis
MUTAGEN 17; /note="I->W: Abolishes interaction with ATG5."; /evidence="ECO:0000269|PubMed:25484072"; MUTAGEN 21; /note="L->W: Abolishes interaction with ATG5."; /evidence="ECO:0000269|PubMed:25484072"; MUTAGEN 24; /note="R->D: Abolishes interaction with ATG5."; /evidence="ECO:0000269|PubMed:25484072"; MUTAGEN 32..36; /note="FEEII->AEEAA: In FII mutant; abolished binding to membranes and lipidation to ATG8 family proteins."; /evidence="ECO:0000269|PubMed:30778222"; MUTAGEN 36; /note="I->W: Reduces interaction with ATG5."; /evidence="ECO:0000269|PubMed:25484072"; MUTAGEN 139; /note="S->A: Abolishes phosphorylation. Impairs interaction with ATG12-ATG5 complex."; /evidence="ECO:0000269|PubMed:26083323"; MUTAGEN 206; /note="N->A: Decreased binding affinity by 36-fold with RAB33B. Decreased binding affinity by 254-fold with RAB33B and colocalization to phagophore; when associated with A-209. No change in interaction with ATG5-ATG12 complex; when associated with A-209."; /evidence="ECO:0000269|PubMed:32960676"; MUTAGEN 209; /note="N->A: Decreased binding affinity by 9-fold with RAB33B. Decreased binding affinity by 254-fold with RAB33B and colocalization to phagophore; when associated with A-206. No change in interaction with ATG5-ATG12 complex; when associated with A-209."; /evidence="ECO:0000269|PubMed:32960676"; MUTAGEN 226; /note="E->R: Impairs interaction with WIPI2."; /evidence="ECO:0000269|PubMed:24954904"; MUTAGEN 230; /note="E->R: Impairs interaction with WIPI2."; /evidence="ECO:0000269|PubMed:24954904"; MUTAGEN 299; /note="D->E: Prevents cleavage by activated CASP3."; /evidence="ECO:0000269|PubMed:24553140"; MUTAGEN 308..310; /note="VRV->AAA: In VRV mutant; abolished binding to membranes and lipidation to ATG8 family proteins."; /evidence="ECO:0000269|PubMed:30778222"; MUTAGEN 467; /note="F->A: Abolished non-canonical autophagy without affecting canonical autophagy."; /evidence="ECO:0000269|PubMed:29317426, ECO:0000269|PubMed:30778222"; MUTAGEN 490; /note="K->A: Abolished non-canonical autophagy without affecting canonical autophagy. Impaired conjugation of phosphatidylserine (PS) to LC3 proteins."; /evidence="ECO:0000269|PubMed:29317426, ECO:0000269|PubMed:33909989"; MUTAGEN 540; /note="V->A: Impairs interaction with PPP1CA; when associated with A-542."; /evidence="ECO:0000269|PubMed:26083323"; MUTAGEN 542; /note="F->A: Impairs interaction with PPP1CA; when associated with A-540."; /evidence="ECO:0000269|PubMed:26083323
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:0000269|PubMed:26083323}.
uniprot
proteins
protein_family
WD repeat ATG16 family
uniprot
proteins
pubmed
12975309
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15620219
uniprot
proteins
pubmed
15815621
uniprot
proteins
pubmed
17200669
uniprot
proteins
pubmed
17435756
uniprot
proteins
pubmed
17484864
uniprot
proteins
pubmed
17974005
uniprot
proteins
pubmed
18047540
uniprot
proteins
pubmed
18499543
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
18849966
uniprot
proteins
pubmed
18985712
uniprot
proteins
pubmed
19659808
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
20637199
uniprot
proteins
pubmed
20639872
uniprot
proteins
pubmed
21808068
uniprot
proteins
pubmed
22749352
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
23202584
uniprot
proteins
pubmed
23262492
uniprot
proteins
pubmed
23376921
uniprot
proteins
pubmed
23392225
uniprot
proteins
pubmed
24191030
uniprot
proteins
pubmed
24238340
uniprot
proteins
pubmed
24553140
uniprot
proteins
pubmed
24656308
uniprot
proteins
pubmed
24954904
uniprot
proteins
pubmed
25484072
uniprot
proteins
pubmed
25645662
uniprot
proteins
pubmed
25891078
uniprot
proteins
pubmed
26083323
uniprot
proteins
pubmed
26347139
uniprot
proteins
pubmed
26812546
uniprot
proteins
pubmed
27273576
uniprot
proteins
pubmed
28561066
uniprot
proteins
pubmed
29317426
uniprot
proteins
pubmed
30143514
uniprot
proteins
pubmed
30778222
uniprot
proteins
pubmed
32960676
uniprot
proteins
pubmed
33087875
uniprot
proteins
pubmed
33909989
uniprot
proteins
pubmed
39284914
uniprot
proteins
sequence_length
607
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23392225}. Preautophagosomal structure membrane {ECO:0000269|PubMed:20639872, ECO:0000269|PubMed:23392225, ECO:0000269|PubMed:32960676}; Peripheral membrane protein {ECO:0000305}. Endosome membrane {ECO:0000269|PubMed:29317426}; Peripheral membrane protein {ECO:0000305}. Lysosome membrane {ECO:0000269|PubMed:29317426}; Peripheral membrane protein {ECO:0000305}. Note=Recruited to omegasomes membranes by WIPI2 (By similarity). Omegasomes are endoplasmic reticulum connected strutures at the origin of preautophagosomal structures (By similarity). Localized to preautophagosomal structure (PAS) where it is involved in the membrane targeting of ATG5 (By similarity). Also localizes to discrete punctae along the ciliary axoneme (By similarity). Upon activation of non-canonical autophagy, recruited to single-membrane endolysosomal compartments (PubMed:29317426). Under starved conditions, the ATG12-ATG5-ATG16L1 complex is translocated to phagophores driven by RAB33B (PubMed:32960676). {ECO:0000250|UniProtKB:Q8C0J2, ECO:0000269|PubMed:29317426, ECO:0000269|PubMed:32960676}.
uniprot
proteins