##gff-version 3 Q2TAZ0 UniProtKB Chain 1 1938 . . . ID=PRO_0000315234;Note=Autophagy-related protein 2 homolog A Q2TAZ0 UniProtKB Domain 14 111 . . . Note=Chorein N-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q2TAZ0 UniProtKB Region 1242 1272 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q2TAZ0 UniProtKB Region 1315 1359 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q2TAZ0 UniProtKB Region 1358 1404 . . . Note=WIPI-interacting;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:32483132;Dbxref=PMID:32483132 Q2TAZ0 UniProtKB Region 1438 1476 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q2TAZ0 UniProtKB Region 1614 1657 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q2TAZ0 UniProtKB Compositional bias 1344 1359 . . . Note=Acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q2TAZ0 UniProtKB Compositional bias 1449 1474 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q2TAZ0 UniProtKB Compositional bias 1622 1649 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q2TAZ0 UniProtKB Modified residue 765 765 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:24275569;Dbxref=PMID:24275569 Q2TAZ0 UniProtKB Modified residue 878 878 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q6P4T0 Q2TAZ0 UniProtKB Modified residue 892 892 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q6P4T0 Q2TAZ0 UniProtKB Modified residue 894 894 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q6P4T0 Q2TAZ0 UniProtKB Modified residue 1266 1266 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q6P4T0 Q2TAZ0 UniProtKB Modified residue 1301 1301 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23186163;Dbxref=PMID:23186163 Q2TAZ0 UniProtKB Modified residue 1309 1309 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23186163;Dbxref=PMID:23186163 Q2TAZ0 UniProtKB Modified residue 1402 1402 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23186163;Dbxref=PMID:23186163 Q2TAZ0 UniProtKB Alternative sequence 1 1607 . . . ID=VSP_030510;Note=In isoform 3. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:15489334;Dbxref=PMID:15489334 Q2TAZ0 UniProtKB Alternative sequence 58 121 . . . ID=VSP_030511;Note=In isoform 4. SVNEVLESMESPLELVEGFVGSIEVAVPWAALLTDHCTVRVSGLQLTLQPRRGPAPGAADSQSW->VRSQARVQEVCERGAGVNGVTAGAGGRLRGLHRGGRALGCSAHRPLHSARVRPPAHLAAPPGSR;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:14702039;Dbxref=PMID:14702039 Q2TAZ0 UniProtKB Alternative sequence 122 1938 . . . ID=VSP_030512;Note=In isoform 4. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:14702039;Dbxref=PMID:14702039 Q2TAZ0 UniProtKB Alternative sequence 1259 1259 . . . ID=VSP_030515;Note=In isoform 2. K->KVQ;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:15489334;Dbxref=PMID:15489334 Q2TAZ0 UniProtKB Alternative sequence 1608 1724 . . . ID=VSP_030516;Note=In isoform 3. INPVVPGETSAEARPETRAQPSSPLEGQAEGVETTGSQEAPGGGHSPSPPDQQPIYFREFRFTSEVPIWLDYHGKHVTMDQVGTFAGLLIGLAQLNCSELKLKRLCCRHGLLGVDKV->MAVAMVKLCERAGLPLLAAPLLRSLLPRAPQPGPAQPRSVQGQRCPARHPPGNLVCERGAGVNGVTAGAGGRLRGLHRGGRALGCSAHRPLHSARVRPPAHLAAPPGSSARGCRLTE;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:15489334;Dbxref=PMID:15489334 Q2TAZ0 UniProtKB Natural variant 175 175 . . . ID=VAR_038158;Note=V->I;Dbxref=dbSNP:rs12293826 Q2TAZ0 UniProtKB Natural variant 394 394 . . . ID=VAR_061027;Note=R->C;Dbxref=dbSNP:rs35115827 Q2TAZ0 UniProtKB Natural variant 404 404 . . . ID=VAR_061028;Note=A->V;Dbxref=dbSNP:rs60711419 Q2TAZ0 UniProtKB Natural variant 627 627 . . . ID=VAR_038159;Note=A->V;Dbxref=dbSNP:rs2285347 Q2TAZ0 UniProtKB Natural variant 656 656 . . . ID=VAR_061029;Note=P->R;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15489334,ECO:0000269|PubMed:9455477;Dbxref=dbSNP:rs656195,PMID:15489334,PMID:9455477 Q2TAZ0 UniProtKB Natural variant 948 948 . . . ID=VAR_038160;Note=G->R;Dbxref=dbSNP:rs11827140 Q2TAZ0 UniProtKB Mutagenesis 54 54 . . . Note=In Mutant 1%3B abolished lipid transfer activity%3B when associated with R-82%2C E-101%2C R-167%2C E-171%2C R-193%2C R-200%2C E-223%2C R-285%2C R-304 and R-328. L->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:30952800;Dbxref=PMID:30952800 Q2TAZ0 UniProtKB Mutagenesis 80 80 . . . Note=In Mutant 2%3B abolished lipid transfer activity%3B when associated with D-103%2C K-167%2C R-171%2C E-193%2C K-259%2C E-285 and R-304. I->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:30952800;Dbxref=PMID:30952800 Q2TAZ0 UniProtKB Mutagenesis 82 82 . . . Note=In Mutant 1%3B abolished lipid transfer activity%3B when associated with R-54%2C E-101%2C R-167%2C E-171%2C R-193%2C R-200%2C E-223%2C R-285%2C R-304 and R-328. V->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:30952800;Dbxref=PMID:30952800 Q2TAZ0 UniProtKB Mutagenesis 101 101 . . . Note=In Mutant 1%3B abolished lipid transfer activity%3B when associated with R-54%2C R-82%2C R-167%2C E-171%2C R-193%2C R-200%2C E-223%2C R-285%2C R-304 and R-328. L->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:30952800;Dbxref=PMID:30952800 Q2TAZ0 UniProtKB Mutagenesis 103 103 . . . Note=In Mutant 2%3B abolished lipid transfer activity%3B when associated with E-80%2CK-167%2C R-171%2C E-193%2C K-259%2C E-285 and R-304. L->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:30952800;Dbxref=PMID:30952800 Q2TAZ0 UniProtKB Mutagenesis 167 167 . . . Note=In Mutant 2%3B abolished lipid transfer activity%3B when associated with E-80%2C D-103%2C R-171%2C E-193%2C K-259%2C E-285 and R-304. I->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:30952800;Dbxref=PMID:30952800 Q2TAZ0 UniProtKB Mutagenesis 167 167 . . . Note=In Mutant 1%3B abolished lipid transfer activity%3B when associated with R-54%2C R-82%2C E-101%2C E-171%2C R-193%2C R-200%2C E-223%2C R-285%2C R-304 and R-328. I->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:30952800;Dbxref=PMID:30952800 Q2TAZ0 UniProtKB Mutagenesis 171 171 . . . Note=In Mutant 1%3B abolished lipid transfer activity%3B when associated with R-54%2C R-82%2C E-101%2C R-167%2C R-193%2C R-200%2C E-223%2C R-285%2C R-304 and R-328. F->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:30952800;Dbxref=PMID:30952800 Q2TAZ0 UniProtKB Mutagenesis 171 171 . . . Note=In Mutant 2%3B abolished lipid transfer activity%3B when associated with E-80%2C D-103%2C K-167%2C E-193%2C K-259%2C E-285 and R-304. F->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:30952800;Dbxref=PMID:30952800 Q2TAZ0 UniProtKB Mutagenesis 193 193 . . . Note=In Mutant 2%3B abolished lipid transfer activity%3B when associated with E-80%2C D-103%2C K-167%2C R-171%2C K-259%2C E-285 and R-304. V->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:30952800;Dbxref=PMID:30952800 Q2TAZ0 UniProtKB Mutagenesis 193 193 . . . Note=In Mutant 1%3B abolished lipid transfer activity%3B when associated with R-54%2C R-82%2C E-101%2C R-167%2C E-171%2C R-200%2C E-223%2C R-285%2C R-304 and R-328. V->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:30952800;Dbxref=PMID:30952800 Q2TAZ0 UniProtKB Mutagenesis 200 200 . . . Note=In Mutant 1%3B abolished lipid transfer activity%3B when associated with R-54%2C R-82%2C E-101%2C R-167%2C E-171%2C R-193%2C E-223%2C R-285%2C R-304 and R-328. Y->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:30952800;Dbxref=PMID:30952800 Q2TAZ0 UniProtKB Mutagenesis 223 223 . . . Note=In Mutant 1%3B abolished lipid transfer activity%3B when associated with R-54%2C R-82%2C E-101%2C R-167%2C E-171%2C R-193%2C R-200%2C R-285%2C R-304 and R-328. L->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:30952800;Dbxref=PMID:30952800 Q2TAZ0 UniProtKB Mutagenesis 259 259 . . . Note=In Mutant 2%3B abolished lipid transfer activity%3B when associated with E-80%2C D-103%2C K-167%2C R-171%2C E-193%2C E-285 and R-304. M->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:30952800;Dbxref=PMID:30952800 Q2TAZ0 UniProtKB Mutagenesis 285 285 . . . Note=In Mutant 2%3B abolished lipid transfer activity%3B when associated with E-80%2C D-103%2C K-167%2C R-171%2C E-193%2C K-259 and R-304. L->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:30952800;Dbxref=PMID:30952800 Q2TAZ0 UniProtKB Mutagenesis 285 285 . . . Note=In Mutant 1%3B abolished lipid transfer activity%3B when associated with R-54%2C R-82%2C E-101%2C R-167%2C E-171%2C R-193%2C R-200%2C E-223%2C R-304 and R-328. L->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:30952800;Dbxref=PMID:30952800 Q2TAZ0 UniProtKB Mutagenesis 304 304 . . . Note=In Mutant 1%3B abolished lipid transfer activity%3B when associated with R-54%2C R-82%2C E-101%2C R-167%2C E-171%2C R-193%2C R-200%2C E-223%2C R-285 and R-328. In Mutant 2%3B abolished lipid transfer activity%3B when associated with E-80%2C D-103%2C K-167%2C R-171%2C E-193%2C K-259 and E-285. V->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:30952800;Dbxref=PMID:30952800 Q2TAZ0 UniProtKB Mutagenesis 328 328 . . . Note=In Mutant 1%3B abolished lipid transfer activity%3B when associated with R-54%2C R-82%2C E-101%2C R-167%2C E-171%2C R-193%2C R-200%2C E-223%2C R-285 and R-304. W->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:30952800;Dbxref=PMID:30952800 Q2TAZ0 UniProtKB Mutagenesis 1381 1381 . . . Note=Decreased interaction with WDR45/WIPI4 and ability to promote autophagy. V->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:32483132;Dbxref=PMID:32483132 Q2TAZ0 UniProtKB Mutagenesis 1382 1382 . . . Note=Decreased interaction with WDR45/WIPI4 and ability to promote autophagy. T->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:32483132;Dbxref=PMID:32483132 Q2TAZ0 UniProtKB Mutagenesis 1389 1389 . . . Note=Decreased interaction with WDR45/WIPI4 and ability to promote autophagy. I->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:32483132;Dbxref=PMID:32483132 Q2TAZ0 UniProtKB Mutagenesis 1395 1395 . . . Note=Decreased interaction with WDR45/WIPI4 and ability to promote autophagy. Y->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:32483132;Dbxref=PMID:32483132 Q2TAZ0 UniProtKB Mutagenesis 1396 1396 . . . Note=Decreased interaction with WDR45/WIPI4 and ability to promote autophagy. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:32483132;Dbxref=PMID:32483132 Q2TAZ0 UniProtKB Sequence conflict 1286 1286 . . . Note=A->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q2TAZ0 UniProtKB Beta strand 1380 1383 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6KLR