##gff-version 3
Q4G0M1	UniProtKB	Signal peptide	1	28	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q4G0M1	UniProtKB	Chain	29	354	.	.	.	ID=PRO_0000340250;Note=Erythroferrone	
Q4G0M1	UniProtKB	Domain	199	354	.	.	.	Note=C1q;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00368	
Q4G0M1	UniProtKB	Region	26	123	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q4G0M1	UniProtKB	Site	333	333	.	.	.	Note=Required for correct protein folding in the endoplasmic reticulum;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q6PGN1	
Q4G0M1	UniProtKB	Modified residue	111	111	.	.	.	Note=Hydroxyproline;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q6PGN1	
Q4G0M1	UniProtKB	Modified residue	113	113	.	.	.	Note=Hydroxyproline;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q6PGN1	
Q4G0M1	UniProtKB	Modified residue	114	114	.	.	.	Note=Hydroxyproline;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q6PGN1	
Q4G0M1	UniProtKB	Modified residue	116	116	.	.	.	Note=Hydroxyproline;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q6PGN1	
Q4G0M1	UniProtKB	Modified residue	117	117	.	.	.	Note=Hydroxyproline;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q6PGN1	
Q4G0M1	UniProtKB	Modified residue	119	119	.	.	.	Note=Hydroxyproline;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q6PGN1	
Q4G0M1	UniProtKB	Glycosylation	243	243	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000250,ECO:0000255;evidence=ECO:0000250|UniProtKB:Q6PGN1,ECO:0000255	
Q4G0M1	UniProtKB	Glycosylation	295	295	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000250,ECO:0000255;evidence=ECO:0000250|UniProtKB:Q6PGN1,ECO:0000255	
Q4G0M1	UniProtKB	Glycosylation	333	333	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q4G0M1	UniProtKB	Sequence conflict	220	229	.	.	.	Note=ALHELGVYYL->SRGDHPCPSQ;Ontology_term=ECO:0000305;evidence=ECO:0000305