##gff-version 3
P08712	UniProtKB	Chain	1	400	.	.	.	ID=PRO_0000062926;Note=Endoplasmin	
P08712	UniProtKB	Region	346	400	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
P08712	UniProtKB	Motif	397	400	.	.	.	Note=Prevents secretion from ER	
P08712	UniProtKB	Compositional bias	350	389	.	.	.	Note=Acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
P08712	UniProtKB	Site	45	45	.	.	.	Note=Important for ATP hydrolysis;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P41148	
P08712	UniProtKB	Modified residue	1	1	.	.	.	Note=N6-succinyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P08113	
P08712	UniProtKB	Modified residue	44	44	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P14625	
P08712	UniProtKB	Modified residue	76	76	.	.	.	Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P08113	
P08712	UniProtKB	Modified residue	230	230	.	.	.	Note=N6-succinyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P08113	
P08712	UniProtKB	Modified residue	379	379	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P14625	
P08712	UniProtKB	Glycosylation	42	42	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P08712	UniProtKB	Glycosylation	78	78	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P08712	UniProtKB	Glycosylation	99	99	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P08712	UniProtKB	Non-terminal residue	1	1	.	.	.	.