##gff-version 3
Q8BGW1	UniProtKB	Chain	1	502	.	.	.	ID=PRO_0000286164;Note=Alpha-ketoglutarate-dependent dioxygenase FTO	
Q8BGW1	UniProtKB	Region	32	324	.	.	.	Note=Fe2OG dioxygenase domain;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9C0B1	
Q8BGW1	UniProtKB	Region	210	221	.	.	.	Note=Loop L1%3B predicted to block binding of double-stranded DNA or RNA;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9C0B1	
Q8BGW1	UniProtKB	Binding site	96	96	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9C0B1	
Q8BGW1	UniProtKB	Binding site	108	108	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9C0B1	
Q8BGW1	UniProtKB	Binding site	202	202	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9C0B1	
Q8BGW1	UniProtKB	Binding site	228	231	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9C0B1	
Q8BGW1	UniProtKB	Binding site	228	228	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9C0B1	
Q8BGW1	UniProtKB	Binding site	230	230	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9C0B1	
Q8BGW1	UniProtKB	Binding site	292	292	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9C0B1	
Q8BGW1	UniProtKB	Binding site	304	304	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9C0B1	
Q8BGW1	UniProtKB	Binding site	313	315	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9C0B1	
Q8BGW1	UniProtKB	Binding site	317	317	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9C0B1	
Q8BGW1	UniProtKB	Binding site	319	319	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9C0B1	
Q8BGW1	UniProtKB	Modified residue	213	213	.	.	.	Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9C0B1	
Q8BGW1	UniProtKB	Alternative sequence	296	316	.	.	.	ID=VSP_025007;Note=In isoform 4. DDLNATHQHCVLAGSQPRFSS->GNVGSLRVGHLWGFEIHFWIL;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:16141072;Dbxref=PMID:16141072	
Q8BGW1	UniProtKB	Alternative sequence	317	502	.	.	.	ID=VSP_025008;Note=In isoform 4. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:16141072;Dbxref=PMID:16141072	
Q8BGW1	UniProtKB	Alternative sequence	411	413	.	.	.	ID=VSP_025009;Note=In isoform 3. TNA->VSA;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:16141072;Dbxref=PMID:16141072	
Q8BGW1	UniProtKB	Alternative sequence	414	502	.	.	.	ID=VSP_025010;Note=In isoform 3. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:16141072;Dbxref=PMID:16141072	
Q8BGW1	UniProtKB	Alternative sequence	453	502	.	.	.	ID=VSP_025011;Note=In isoform 2. CQSRVVRTLPVQQKPDCRPYWEKDDPSMPLPFDLTDVVSELRGQLLEARS->FVLLRGGVWCPCPSSARPAQRTKVEDILS;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:14621295;Dbxref=PMID:14621295	
Q8BGW1	UniProtKB	Mutagenesis	304	304	.	.	.	Note=Reduced enzyme activity. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17991826;Dbxref=PMID:17991826	
Q8BGW1	UniProtKB	Mutagenesis	313	313	.	.	.	Note=Loss of enzyme activity. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17991826;Dbxref=PMID:17991826	
Q8BGW1	UniProtKB	Mutagenesis	367	367	.	.	.	Note=Reduces enzyme activity by about 60%25. I->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19680540;Dbxref=PMID:19680540	
Q8BGW1	UniProtKB	Mutagenesis	367	367	.	.	.	Note=Alters protein structure and causes an increase in whole body metabolism%2C leading to a lean phenotype in adult males%2C but not in females. I->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19680540;Dbxref=PMID:19680540	
Q8BGW1	UniProtKB	Sequence conflict	181	181	.	.	.	Note=G->R;Ontology_term=ECO:0000305;evidence=ECO:0000305	
Q8BGW1	UniProtKB	Sequence conflict	384	384	.	.	.	Note=N->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
Q8BGW1	UniProtKB	Sequence conflict	410	410	.	.	.	Note=M->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
Q8BGW1	UniProtKB	Sequence conflict	463	463	.	.	.	Note=V->A;Ontology_term=ECO:0000305;evidence=ECO:0000305