##gff-version 3
O18750	UniProtKB	Chain	1	716	.	.	.	ID=PRO_0000062927;Note=Endoplasmin	
O18750	UniProtKB	Region	211	244	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
O18750	UniProtKB	Region	664	716	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
O18750	UniProtKB	Motif	713	716	.	.	.	Note=Prevents secretion from ER;Ontology_term=ECO:0000255;evidence=ECO:0000255	
O18750	UniProtKB	Compositional bias	215	235	.	.	.	Note=Acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
O18750	UniProtKB	Compositional bias	668	700	.	.	.	Note=Acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
O18750	UniProtKB	Compositional bias	701	716	.	.	.	Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
O18750	UniProtKB	Binding site	28	28	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P41148	
O18750	UniProtKB	Binding site	70	70	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P41148	
O18750	UniProtKB	Binding site	83	83	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P41148	
O18750	UniProtKB	Binding site	120	120	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P41148	
O18750	UniProtKB	Site	368	368	.	.	.	Note=Important for ATP hydrolysis;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P41148	
O18750	UniProtKB	Modified residue	89	89	.	.	.	Note=N6-(2-hydroxyisobutyryl)lysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P14625	
O18750	UniProtKB	Modified residue	93	93	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q66HD0	
O18750	UniProtKB	Modified residue	323	323	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q66HD0	
O18750	UniProtKB	Modified residue	324	324	.	.	.	Note=N6-succinyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P08113	
O18750	UniProtKB	Modified residue	367	367	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P14625	
O18750	UniProtKB	Modified residue	399	399	.	.	.	Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P08113	
O18750	UniProtKB	Modified residue	552	552	.	.	.	Note=N6-succinyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P08113	
O18750	UniProtKB	Modified residue	696	696	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P14625	
O18750	UniProtKB	Glycosylation	28	28	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
O18750	UniProtKB	Glycosylation	138	138	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
O18750	UniProtKB	Glycosylation	365	365	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
O18750	UniProtKB	Glycosylation	421	421	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
O18750	UniProtKB	Disulfide bond	59	59	.	.	.	Note=Interchain;Ontology_term=ECO:0000250;evidence=ECO:0000250	
O18750	UniProtKB	Non-terminal residue	1	1	.	.	.	.