##gff-version 3 Q08426 UniProtKB Chain 1 723 . . . ID=PRO_0000109247;Note=Peroxisomal bifunctional enzyme Q08426 UniProtKB Region 1 282 . . . Note=Enoyl-CoA hydratase / isomerase Q08426 UniProtKB Region 283 572 . . . Note=3-hydroxyacyl-CoA dehydrogenase Q08426 UniProtKB Motif 721 723 . . . Note=Microbody targeting signal Q08426 UniProtKB Binding site 101 101 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 Q08426 UniProtKB Site 104 104 . . . Note=Important for catalytic activity;Ontology_term=ECO:0000250;evidence=ECO:0000250 Q08426 UniProtKB Site 124 124 . . . Note=Important for catalytic activity;Ontology_term=ECO:0000250;evidence=ECO:0000250 Q08426 UniProtKB Modified residue 38 38 . . . Note=N6-succinyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9DBM2 Q08426 UniProtKB Modified residue 165 165 . . . Note=N6-acetyllysine%3B alternate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20167786;Dbxref=PMID:20167786 Q08426 UniProtKB Modified residue 165 165 . . . Note=N6-succinyllysine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9DBM2 Q08426 UniProtKB Modified residue 171 171 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20167786;Dbxref=PMID:20167786 Q08426 UniProtKB Modified residue 219 219 . . . Note=N6-acetyllysine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9DBM2 Q08426 UniProtKB Modified residue 219 219 . . . Note=N6-succinyllysine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9DBM2 Q08426 UniProtKB Modified residue 250 250 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9DBM2 Q08426 UniProtKB Modified residue 280 280 . . . Note=N6-succinyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9DBM2 Q08426 UniProtKB Modified residue 290 290 . . . Note=N6-succinyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9DBM2 Q08426 UniProtKB Modified residue 346 346 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20167786;Dbxref=PMID:20167786 Q08426 UniProtKB Modified residue 350 350 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9DBM2 Q08426 UniProtKB Modified residue 464 464 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9DBM2 Q08426 UniProtKB Modified residue 532 532 . . . Note=N6-succinyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9DBM2 Q08426 UniProtKB Modified residue 548 548 . . . Note=Phosphothreonine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:24275569;Dbxref=PMID:24275569 Q08426 UniProtKB Modified residue 577 577 . . . Note=N6-succinyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9DBM2 Q08426 UniProtKB Modified residue 584 584 . . . Note=N6-acetyllysine%3B alternate;Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:20167786,ECO:0007744|PubMed:19608861;Dbxref=PMID:19608861,PMID:20167786 Q08426 UniProtKB Modified residue 584 584 . . . Note=N6-succinyllysine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9DBM2 Q08426 UniProtKB Modified residue 591 591 . . . Note=N6-acetyllysine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9DBM2 Q08426 UniProtKB Modified residue 591 591 . . . Note=N6-succinyllysine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9DBM2 Q08426 UniProtKB Modified residue 710 710 . . . Note=N6-acetyllysine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9DBM2 Q08426 UniProtKB Modified residue 710 710 . . . Note=N6-succinyllysine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9DBM2 Q08426 UniProtKB Modified residue 718 718 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23186163;Dbxref=PMID:23186163 Q08426 UniProtKB Modified residue 722 722 . . . Note=N6-succinyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9DBM2 Q08426 UniProtKB Alternative sequence 1 96 . . . ID=VSP_042811;Note=In isoform 2. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:14702039;Dbxref=PMID:14702039 Q08426 UniProtKB Natural variant 3 3 . . . ID=VAR_070949;Note=In FRTS3%3B the mutant is mistargeted to mitochondria%3B results in impaired mitochondrial oxidative phosphorylation and defects in the transport of fluids across the epithelium of renal proximal tubular cells. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24401050;Dbxref=dbSNP:rs398124646,PMID:24401050 Q08426 UniProtKB Natural variant 40 40 . . . ID=VAR_054329;Note=V->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8188243;Dbxref=dbSNP:rs1062551,PMID:8188243 Q08426 UniProtKB Natural variant 41 41 . . . ID=VAR_054330;Note=I->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8188243;Dbxref=dbSNP:rs1062552,PMID:8188243 Q08426 UniProtKB Natural variant 75 75 . . . ID=VAR_047132;Note=T->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8188243;Dbxref=dbSNP:rs1062553,PMID:8188243 Q08426 UniProtKB Natural variant 274 274 . . . ID=VAR_047133;Note=A->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14702039;Dbxref=dbSNP:rs2302819,PMID:14702039 Q08426 UniProtKB Natural variant 325 325 . . . ID=VAR_054331;Note=A->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8188243;Dbxref=dbSNP:rs1062555,PMID:8188243 Q08426 UniProtKB Natural variant 598 598 . . . ID=VAR_054332;Note=K->T;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:1651711,ECO:0000269|PubMed:8188243;Dbxref=dbSNP:rs1042437,PMID:1651711,PMID:8188243 Q08426 UniProtKB Natural variant 606 606 . . . ID=VAR_047134;Note=T->P;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:1651711,ECO:0000269|PubMed:8188243;Dbxref=dbSNP:rs1042438,PMID:1651711,PMID:8188243 Q08426 UniProtKB Natural variant 685 685 . . . ID=VAR_047135;Note=Q->K;Dbxref=dbSNP:rs11919970 Q08426 UniProtKB Natural variant 715 715 . . . ID=VAR_047136;Note=L->S;Dbxref=dbSNP:rs11927618 Q08426 UniProtKB Mutagenesis 165 165 . . . Note=Greatly reduced acetylation and insensitive to treatment with TSA and NAM%3B when associated with Q-171%3B Q-346 and Q-584. K->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20167786;Dbxref=PMID:20167786 Q08426 UniProtKB Mutagenesis 171 171 . . . Note=Greatly reduced acetylation and insensitive to treatment with TSA and NAM%3B when associated with Q-165%3B Q-346 and Q-584. K->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20167786;Dbxref=PMID:20167786 Q08426 UniProtKB Mutagenesis 346 346 . . . Note=Greatly reduced acetylation and insensitive to treatment with TSA and NAM%3B when associated with Q-165%3B Q-171 and Q-584. K->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20167786;Dbxref=PMID:20167786 Q08426 UniProtKB Mutagenesis 584 584 . . . Note=Greatly reduced acetylation and insensitive to treatment with TSA and NAM%3B when associated with Q-165%3B Q-171 and Q-346. K->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20167786;Dbxref=PMID:20167786 Q08426 UniProtKB Sequence conflict 117 117 . . . Note=E->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q08426 UniProtKB Sequence conflict 656 657 . . . Note=WP->CA;Ontology_term=ECO:0000305;evidence=ECO:0000305