##gff-version 3 Q9NT62 UniProtKB Chain 1 314 . . . ID=PRO_0000213569;Note=Ubiquitin-like-conjugating enzyme ATG3 Q9NT62 UniProtKB Region 140 170 . . . Note=Interaction with ATG12;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24191030;Dbxref=PMID:24191030 Q9NT62 UniProtKB Region 143 163 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q9NT62 UniProtKB Motif 4 19 . . . Note=Membrane-curvature-sensing motif;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9CPX6 Q9NT62 UniProtKB Motif 101 103 . . . Note=Increases ATG3 translation efficiency by the ribomome assisted of EIF5A;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9CPX6 Q9NT62 UniProtKB Motif 104 110 . . . Note=LIR motif;Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:37252361,ECO:0007744|PDB:8AFI;Dbxref=PMID:37252361 Q9NT62 UniProtKB Motif 166 169 . . . Note=Caspase cleavage motif LETD;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22644571;Dbxref=PMID:22644571 Q9NT62 UniProtKB Active site 264 264 . . . Note=Glycyl thioester intermediate;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:11825910;Dbxref=PMID:11825910 Q9NT62 UniProtKB Site 169 170 . . . Note=Cleavage%3B by CASP8;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22644571;Dbxref=PMID:22644571 Q9NT62 UniProtKB Modified residue 1 1 . . . Note=N-acetylmethionine;Ontology_term=ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:19413330,ECO:0007744|PubMed:22223895;Dbxref=PMID:19413330,PMID:22223895 Q9NT62 UniProtKB Cross-link 243 243 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ATG12);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9CPX6 Q9NT62 UniProtKB Alternative sequence 290 314 . . . ID=VSP_013037;Note=In isoform 2. LLIFLKFVQAVIPTIEYDYTRHFTM->PSLYVRLVAKWLLTIFFLRNLV;Ontology_term=ECO:0000303,ECO:0000303;evidence=ECO:0000303|PubMed:14702039,ECO:0000303|PubMed:15489334;Dbxref=PMID:14702039,PMID:15489334 Q9NT62 UniProtKB Mutagenesis 8 8 . . . Note=Significantly reduces ATG8-family conjugating enzyme activity%3B when associated with K-15. Decreases protein membrane interactions%3B when associated with K-15. Does not affect formation of the covalent thioester intermediate with MAP1LC3B%3B when associated with K-15. V->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:33446636;Dbxref=PMID:33446636 Q9NT62 UniProtKB Mutagenesis 9 9 . . . Note=Slightly decreases interaction with lipid monolayers%3B when associated with D-11. Slightly decreases insertion into lipid monolayers%3B when associated with D-11. Decreases affinity for monolayers containing cardiolipin (CL)%3B when associated with D-11. Cancels selectivity for anionic phospholipids%3B when associated with D-11. Impairs binding to lipid bilayers%3B when associated with D-11. Impairs insertion into lipid bilayers%3B when associated with D-11. Does not induce vesicle tethering%3B when associated with D-11. K->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:29142222;Dbxref=PMID:29142222 Q9NT62 UniProtKB Mutagenesis 11 11 . . . Note=Slightly decreases interaction with lipid monolayers%3B when associated with D-9. Slightly decreases insertion into lipid monolayers%3B when associated with D-9. Decreases affinity for monolayers containing cardiolipin (CL)%3B when associated with D-9. Cancels selectivity for anionic phospholipids%3B when associated with D-11. Impairs binding to lipid bilayers%3B when associated with D-11. Impairs insertion into lipid bilayers%3B when associated with D-11. Does not induce vesicle tethering%3B when associated with D-11. K->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:29142222;Dbxref=PMID:29142222 Q9NT62 UniProtKB Mutagenesis 15 15 . . . Note=Significantly reduces ATG8-family conjugating enzyme activity%3B when associated with D-8. Decreases protein membrane interactions%3B when associated with D-8. Does not affect formation of the covalent thioester intermediate with MAP1LC3B%3B when associated with D-8. V->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:33446636;Dbxref=PMID:33446636 Q9NT62 UniProtKB Mutagenesis 21 21 . . . Note=Impairs ATG8-family conjugating enzyme activity. Does not affect protein membrane interactions. Does not affect formation of the covalent thioester intermediate with MAP1LC3B. Partially rescues MAP1LC3B lipidation in cell lacking ATG3. P->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:33446636;Dbxref=PMID:33446636 Q9NT62 UniProtKB Mutagenesis 23 23 . . . Note=Severely reduces ATG8-family conjugating enzyme activity. Reduces of about 40%25 protein membrane interactions. Does not affect formation of the covalent thioester intermediate with MAP1LC3B. Completely fails to induce membrane-bound MAP1LC3B (MAP1LC3B-II) and autophagic flux when expressed in cell lacking ATG3. L->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:33446636;Dbxref=PMID:33446636 Q9NT62 UniProtKB Mutagenesis 25 25 . . . Note=Increases of about 30%25 more ATG8-family conjugating enzyme activity. Does not affect protein membrane interactions. Does not affect formation of the covalent thioester intermediate with MAP1LC3B. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:33446636;Dbxref=PMID:33446636 Q9NT62 UniProtKB Mutagenesis 95 95 . . . Note=Severely diminish GABARAP:ATG3 conjugation. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:37252361;Dbxref=PMID:37252361 Q9NT62 UniProtKB Mutagenesis 97 97 . . . Note=Severely diminish GABARAP:ATG3 conjugation. I->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:37252361;Dbxref=PMID:37252361 Q9NT62 UniProtKB Mutagenesis 107 107 . . . Note=Almost completely abrogates GABARAP:ATG3 conjugation. W->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:37252361;Dbxref=PMID:37252361 Q9NT62 UniProtKB Mutagenesis 108 108 . . . Note=Significantly reduces GABARAP:ATG3 conjugation. V->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:37252361;Dbxref=PMID:37252361 Q9NT62 UniProtKB Mutagenesis 144 151 . . . Note=Strongly decreases affinity for the complex ATG12:ATG5:ATG16L1. Severely decreases phosphatidylethanolamine (PE)-conjugated ATG8-like proteins formation. EEEEDEDE->AAAAAAAA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24191030;Dbxref=PMID:24191030 Q9NT62 UniProtKB Mutagenesis 156 156 . . . Note=Strongly decreases affinity for the complex ATG12:ATG5:ATG16L1. Impairs interaction with the complex ATG12:ATG5:ATG16L1%3B when associated with A-157. Impairs phosphatidylethanolamine (PE)-conjugated ATG8-like protein formation. Loss of phosphatidylethanolamine (PE)-conjugated ATG8-like proteins formation%3B when associated with A-157. Impairs interaction with ATG12:ATG5%3B when associated with A-157. Does not affect interaction with ATG7%3B when associated with A-157. Does not affect the formation of the ATG8-like protein:ATG3 intermediate complex%3B when associated with A-157. Affects modestly the ATG3-ATG7 interaction%3B when associated with A-157. Reduces the thioester-linkage formation with GABARAP%3B when associated with A-157. D->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:24191030,ECO:0000269|PubMed:26043688;Dbxref=PMID:24191030,PMID:26043688 Q9NT62 UniProtKB Mutagenesis 157 157 . . . Note=Strongly decreases affinity for the complex ATG12:ATG5:ATG16L1. Impairs interaction with the complex ATG12:ATG5:ATG16L1%3B when associated with A-156. Impairs phosphatidylethanolamine (PE)-conjugated ATG8-like proteins formation. Loss of phosphatidylethanolamine (PE)-conjugated ATG8-like proteins formation%3B when associated with A-156. Impairs interaction with ATG12:ATG5%3B when associated with A-156. Does not affect interaction with ATG7%3B when associated with A-156. Does not affect the formation of the ATG8-like protein:ATG3 intermediate complex%3B when associated with A-156. Affects modestly the ATG3-ATG7 interaction%3B when associated with A-156. Reduces the thioester-linkage formation with GABARAP%3B when associated with A-156. M->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:24191030,ECO:0000269|PubMed:26043688;Dbxref=PMID:24191030,PMID:26043688 Q9NT62 UniProtKB Mutagenesis 160 160 . . . Note=Strongly decreases affinity for the complex ATG12:ATG5:ATG16L1. Affects modestly the ATG3-ATG7 interaction. Reduces the thioester-linkage formation with GABARAP. Y->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:24191030,ECO:0000269|PubMed:26043688;Dbxref=PMID:24191030,PMID:26043688 Q9NT62 UniProtKB Mutagenesis 161 161 . . . Note=Strongly decreases affinity for the complex ATG12:ATG5:ATG16L1. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24191030;Dbxref=PMID:24191030 Q9NT62 UniProtKB Mutagenesis 167 167 . . . Note=Weakens the ATG3-ATG7 interaction. Reduces the thioester-linkage formation with GABARAP. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26043688;Dbxref=PMID:26043688 Q9NT62 UniProtKB Mutagenesis 169 169 . . . Note=Weakens the ATG3-ATG7 interaction. Severly reduces the thioester-linkage formation with GABARAP. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26043688;Dbxref=PMID:26043688 Q9NT62 UniProtKB Mutagenesis 171 171 . . . Note=Weakens the ATG3-ATG7 interaction. Reduces the thioester-linkage formation with GABARAP. A->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26043688;Dbxref=PMID:26043688 Q9NT62 UniProtKB Mutagenesis 172 172 . . . Note=Weakens the ATG3-ATG7 interaction. Significantly reduces the thioester-linkage formation with GABARAP. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26043688;Dbxref=PMID:26043688 Q9NT62 UniProtKB Mutagenesis 173 173 . . . Note=Weakens the ATG3-ATG7 interaction. Significantly reduces the thioester-linkage formation with GABARAP. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26043688;Dbxref=PMID:26043688 Q9NT62 UniProtKB Mutagenesis 264 264 . . . Note=Does not affect interaction with ATG12:ATG5. Impairs MAP1LC3A lipidation. Impairs MAP1LC3B lipidation. Impairs ATG3:ATG8-like proteins thioester complex formation. C->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:24191030,ECO:0000269|PubMed:37252361;Dbxref=PMID:24191030,PMID:37252361 Q9NT62 UniProtKB Mutagenesis 264 264 . . . Note=Instead of the formation of an intermediate complex with a thiol ester bond between ATG3 (E2-like enzyme) and GABARAPL1/APG8L (substrate)%2C a stable complex with an O-ester bond is formed. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11825910;Dbxref=PMID:11825910 Q9NT62 UniProtKB Helix 157 163 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4NAW