##gff-version 3
Q9BQS7	UniProtKB	Signal peptide	1	23	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q9BQS7	UniProtKB	Chain	24	1158	.	.	.	ID=PRO_0000002915;Note=Hephaestin	
Q9BQS7	UniProtKB	Topological domain	24	1110	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q9BQS7	UniProtKB	Transmembrane	1111	1131	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q9BQS7	UniProtKB	Topological domain	1132	1158	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q9BQS7	UniProtKB	Domain	24	206	.	.	.	Note=Plastocyanin-like 1	
Q9BQS7	UniProtKB	Domain	218	366	.	.	.	Note=Plastocyanin-like 2	
Q9BQS7	UniProtKB	Domain	379	560	.	.	.	Note=Plastocyanin-like 3	
Q9BQS7	UniProtKB	Domain	570	718	.	.	.	Note=Plastocyanin-like 4	
Q9BQS7	UniProtKB	Domain	731	903	.	.	.	Note=Plastocyanin-like 5	
Q9BQS7	UniProtKB	Domain	911	1087	.	.	.	Note=Plastocyanin-like 6	
Q9BQS7	UniProtKB	Binding site	126	126	.	.	.	Note=Type 2 copper site;Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q9BQS7	UniProtKB	Binding site	128	128	.	.	.	Note=Type 3 copper site;Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q9BQS7	UniProtKB	Binding site	186	186	.	.	.	Note=Type 3 copper site;Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q9BQS7	UniProtKB	Binding site	188	188	.	.	.	Note=Type 3 copper site;Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q9BQS7	UniProtKB	Binding site	304	304	.	.	.	Note=Type 1 copper site;Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q9BQS7	UniProtKB	Binding site	347	347	.	.	.	Note=Type 1 copper site;Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q9BQS7	UniProtKB	Binding site	352	352	.	.	.	Note=Type 1 copper site;Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q9BQS7	UniProtKB	Binding site	656	656	.	.	.	Note=Type 1 copper site;Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q9BQS7	UniProtKB	Binding site	699	699	.	.	.	Note=Type 1 copper site;Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q9BQS7	UniProtKB	Binding site	704	704	.	.	.	Note=Type 1 copper site;Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q9BQS7	UniProtKB	Binding site	709	709	.	.	.	Note=Type 1 copper site;Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q9BQS7	UniProtKB	Binding site	1000	1000	.	.	.	Note=Type 1 copper site;Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q9BQS7	UniProtKB	Binding site	1003	1003	.	.	.	Note=Type 2 copper site;Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q9BQS7	UniProtKB	Binding site	1005	1005	.	.	.	Note=Type 3 copper site;Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q9BQS7	UniProtKB	Binding site	1045	1045	.	.	.	Note=Type 3 copper site;Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q9BQS7	UniProtKB	Binding site	1046	1046	.	.	.	Note=Type 1 copper site;Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q9BQS7	UniProtKB	Binding site	1047	1047	.	.	.	Note=Type 3 copper site;Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q9BQS7	UniProtKB	Binding site	1051	1051	.	.	.	Note=Type 1 copper site;Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q9BQS7	UniProtKB	Binding site	1056	1056	.	.	.	Note=Type 1 copper site;Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q9BQS7	UniProtKB	Modified residue	1145	1145	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23186163;Dbxref=PMID:23186163	
Q9BQS7	UniProtKB	Modified residue	1150	1150	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23186163;Dbxref=PMID:23186163	
Q9BQS7	UniProtKB	Modified residue	1155	1155	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9Z0Z4	
Q9BQS7	UniProtKB	Glycosylation	164	164	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q9BQS7	UniProtKB	Glycosylation	236	236	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q9BQS7	UniProtKB	Glycosylation	588	588	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q9BQS7	UniProtKB	Glycosylation	714	714	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q9BQS7	UniProtKB	Glycosylation	758	758	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q9BQS7	UniProtKB	Glycosylation	829	829	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q9BQS7	UniProtKB	Glycosylation	873	873	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q9BQS7	UniProtKB	Glycosylation	931	931	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q9BQS7	UniProtKB	Disulfide bond	180	206	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q9BQS7	UniProtKB	Disulfide bond	285	366	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q9BQS7	UniProtKB	Disulfide bond	534	560	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q9BQS7	UniProtKB	Disulfide bond	637	718	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q9BQS7	UniProtKB	Disulfide bond	877	903	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q9BQS7	UniProtKB	Alternative sequence	1	267	.	.	.	ID=VSP_047332;Note=In isoform 4. Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305	
Q9BQS7	UniProtKB	Alternative sequence	1	1	.	.	.	ID=VSP_047331;Note=In isoform 3. M->MTQTLPYHLSLLNVLFPGPCSRHFKFRRGKCAQPAWRKVSAPSQDLLITKVMWAM;Ontology_term=ECO:0000305;evidence=ECO:0000305	
Q9BQS7	UniProtKB	Alternative sequence	1082	1082	.	.	.	ID=VSP_011627;Note=In isoform 2. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:12975309;Dbxref=PMID:12975309	
Q9BQS7	UniProtKB	Natural variant	595	595	.	.	.	ID=VAR_024379;Note=A->T;Dbxref=dbSNP:rs17216603	
Q9BQS7	UniProtKB	Sequence conflict	55	56	.	.	.	Note=DI->QR;Ontology_term=ECO:0000305;evidence=ECO:0000305	
Q9BQS7	UniProtKB	Sequence conflict	222	222	.	.	.	Note=V->T;Ontology_term=ECO:0000305;evidence=ECO:0000305