##gff-version 3 Q8NBI2 UniProtKB Chain 1 242 . . . ID=PRO_0000314838;Note=Lysosomal membrane ascorbate-dependent ferrireductase CYB561A3 Q8NBI2 UniProtKB Topological domain 1 7 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q53TN4 Q8NBI2 UniProtKB Transmembrane 8 28 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q8NBI2 UniProtKB Topological domain 29 45 . . . Note=Lumenal;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q53TN4 Q8NBI2 UniProtKB Transmembrane 46 66 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q8NBI2 UniProtKB Topological domain 67 83 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q53TN4 Q8NBI2 UniProtKB Transmembrane 84 104 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q8NBI2 UniProtKB Topological domain 105 119 . . . Note=Lumenal;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q53TN4 Q8NBI2 UniProtKB Transmembrane 120 140 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q8NBI2 UniProtKB Topological domain 141 154 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q53TN4 Q8NBI2 UniProtKB Transmembrane 155 175 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q8NBI2 UniProtKB Topological domain 176 202 . . . Note=Lumenal;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q53TN4 Q8NBI2 UniProtKB Transmembrane 203 223 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q8NBI2 UniProtKB Topological domain 224 242 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q53TN4 Q8NBI2 UniProtKB Domain 12 219 . . . Note=Cytochrome b561;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00242 Q8NBI2 UniProtKB Binding site 47 47 . . . Note=Axial binding residue;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q53TN4 Q8NBI2 UniProtKB Binding site 67 67 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q53TN4 Q8NBI2 UniProtKB Binding site 76 76 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q53TN4 Q8NBI2 UniProtKB Binding site 80 80 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q53TN4 Q8NBI2 UniProtKB Binding site 83 83 . . . Note=Axial binding residue;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q53TN4 Q8NBI2 UniProtKB Binding site 112 115 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q53TN4 Q8NBI2 UniProtKB Binding site 117 117 . . . Note=Axial binding residue;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q53TN4 Q8NBI2 UniProtKB Binding site 149 149 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q53TN4 Q8NBI2 UniProtKB Binding site 156 156 . . . Note=Axial binding residue;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q53TN4 Q8NBI2 UniProtKB Binding site 177 177 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q53TN4 Q8NBI2 UniProtKB Binding site 224 224 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q53TN4 Q8NBI2 UniProtKB Glycosylation 38 38 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q8NBI2 UniProtKB Alternative sequence 1 1 . . . ID=VSP_047358;Note=In isoform 2. M->MGKNFSDSFLSRECVIRM;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:14702039;Dbxref=PMID:14702039 Q8NBI2 UniProtKB Sequence conflict 122 122 . . . Note=I->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q8NBI2 UniProtKB Sequence conflict 168 168 . . . Note=I->N;Ontology_term=ECO:0000305;evidence=ECO:0000305