##gff-version 3
Q60720	UniProtKB	Chain	1	250	.	.	.	ID=PRO_0000151028;Note=Transmembrane ascorbate-dependent reductase CYB561	
Q60720	UniProtKB	Topological domain	1	15	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q53TN4	
Q60720	UniProtKB	Transmembrane	16	36	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q60720	UniProtKB	Topological domain	37	50	.	.	.	Note=Vesicular;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q53TN4	
Q60720	UniProtKB	Transmembrane	51	71	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q60720	UniProtKB	Topological domain	72	83	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q53TN4	
Q60720	UniProtKB	Transmembrane	84	104	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q60720	UniProtKB	Topological domain	105	123	.	.	.	Note=Vesicular;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q53TN4	
Q60720	UniProtKB	Transmembrane	124	144	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q60720	UniProtKB	Topological domain	145	157	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q53TN4	
Q60720	UniProtKB	Transmembrane	158	178	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q60720	UniProtKB	Topological domain	179	197	.	.	.	Note=Vesicular;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q53TN4	
Q60720	UniProtKB	Transmembrane	198	218	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q60720	UniProtKB	Topological domain	219	250	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q53TN4	
Q60720	UniProtKB	Domain	18	219	.	.	.	Note=Cytochrome b561;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00242	
Q60720	UniProtKB	Binding site	52	52	.	.	.	Note=Axial binding residue;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q53TN4	
Q60720	UniProtKB	Binding site	72	72	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q53TN4	
Q60720	UniProtKB	Binding site	79	79	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q53TN4	
Q60720	UniProtKB	Binding site	79	79	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q53TN4	
Q60720	UniProtKB	Binding site	83	83	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q53TN4	
Q60720	UniProtKB	Binding site	86	86	.	.	.	Note=Axial binding residue;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q53TN4	
Q60720	UniProtKB	Binding site	115	118	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q53TN4	
Q60720	UniProtKB	Binding site	120	120	.	.	.	Note=Axial binding residue;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q53TN4	
Q60720	UniProtKB	Binding site	152	152	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q53TN4	
Q60720	UniProtKB	Binding site	159	159	.	.	.	Note=Axial binding residue;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q53TN4	
Q60720	UniProtKB	Binding site	180	180	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q53TN4	
Q60720	UniProtKB	Binding site	224	224	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q53TN4	
Q60720	UniProtKB	Modified residue	1	1	.	.	.	Note=N-acetylmethionine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P10897	
Q60720	UniProtKB	Modified residue	246	246	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:21183079;Dbxref=PMID:21183079	
Q60720	UniProtKB	Modified residue	248	248	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:21183079;Dbxref=PMID:21183079	
Q60720	UniProtKB	Mutagenesis	52	52	.	.	.	Note=Decreased protein abundance. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16256064;Dbxref=PMID:16256064	
Q60720	UniProtKB	Mutagenesis	72	72	.	.	.	Note=No effect on protein abundance. Decreased reduction by ascorbate. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16256064;Dbxref=PMID:16256064	
Q60720	UniProtKB	Mutagenesis	83	83	.	.	.	Note=No effect on protein abundance. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16256064;Dbxref=PMID:16256064	
Q60720	UniProtKB	Mutagenesis	86	86	.	.	.	Note=No effect on protein abundance. Decreased reduction by ascorbate%3B when associated with A-159. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16256064;Dbxref=PMID:16256064	
Q60720	UniProtKB	Mutagenesis	108	108	.	.	.	Note=No effect on protein abundance. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16256064;Dbxref=PMID:16256064	
Q60720	UniProtKB	Mutagenesis	120	120	.	.	.	Note=Decreased protein abundance. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16256064;Dbxref=PMID:16256064	
Q60720	UniProtKB	Mutagenesis	159	159	.	.	.	Note=No effect on protein abundance. Decreased reduction by ascorbate%3B when associated with A-86. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16256064;Dbxref=PMID:16256064	
Q60720	UniProtKB	Sequence conflict	9	21	.	.	.	Note=PAALPYYVAFSQL->LLHCRTMWPSPSC;Ontology_term=ECO:0000305;evidence=ECO:0000305	
Q60720	UniProtKB	Sequence conflict	171	174	.	.	.	Note=VGTA->AGHS;Ontology_term=ECO:0000305;evidence=ECO:0000305	
Q60720	UniProtKB	Sequence conflict	199	199	.	.	.	Note=L->V;Ontology_term=ECO:0000305;evidence=ECO:0000305	
Q60720	UniProtKB	Sequence conflict	222	226	.	.	.	Note=DWKRP->ALERG;Ontology_term=ECO:0000305;evidence=ECO:0000305	
Q60720	UniProtKB	Sequence conflict	248	249	.	.	.	Note=SP->TS;Ontology_term=ECO:0000305;evidence=ECO:0000305