##gff-version 3
P06762	UniProtKB	Chain	1	289	.	.	.	ID=PRO_0000209690;Note=Heme oxygenase 1	
P06762	UniProtKB	Chain	1	266	.	.	.	ID=PRO_0000455625;Note=Heme oxygenase 1 soluble form;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:1935972;Dbxref=PMID:1935972	
P06762	UniProtKB	Topological domain	1	266	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P09601	
P06762	UniProtKB	Transmembrane	267	289	.	.	.	Note=Helical%3B Anchor for type IV membrane protein;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P06762	UniProtKB	Region	225	261	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
P06762	UniProtKB	Compositional bias	233	261	.	.	.	Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
P06762	UniProtKB	Binding site	18	18	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P09601	
P06762	UniProtKB	Binding site	25	25	.	.	.	Note=Axial binding residue;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P09601	
P06762	UniProtKB	Binding site	134	134	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P09601	
P06762	UniProtKB	Binding site	183	183	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P09601	
P06762	UniProtKB	Site	140	140	.	.	.	Note=Important for catalytic activity;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P09601	
P06762	UniProtKB	Modified residue	229	229	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P09601	
P06762	UniProtKB	Modified residue	242	242	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:22673903;Dbxref=PMID:22673903	
P06762	UniProtKB	Helix	13	29	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1J02	
P06762	UniProtKB	Helix	32	39	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1J02	
P06762	UniProtKB	Helix	44	67	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1J02	
P06762	UniProtKB	Turn	68	70	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1J02	
P06762	UniProtKB	Turn	72	74	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1J02	
P06762	UniProtKB	Helix	75	77	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1J02	
P06762	UniProtKB	Helix	80	83	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1J02	
P06762	UniProtKB	Helix	86	97	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1J02	
P06762	UniProtKB	Helix	101	103	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1J02	
P06762	UniProtKB	Helix	109	124	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1J02	
P06762	UniProtKB	Helix	126	128	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1J02	
P06762	UniProtKB	Helix	129	140	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1J02	
P06762	UniProtKB	Helix	143	155	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1J02	
P06762	UniProtKB	Helix	165	167	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1J02	
P06762	UniProtKB	Helix	175	186	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1J02	
P06762	UniProtKB	Helix	193	221	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1J02