##gff-version 3
Q29092	UniProtKB	Signal peptide	1	21	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q29092	UniProtKB	Chain	22	804	.	.	.	ID=PRO_0000013600;Note=Endoplasmin	
Q29092	UniProtKB	Region	288	323	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q29092	UniProtKB	Region	750	804	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q29092	UniProtKB	Motif	801	804	.	.	.	Note=Prevents secretion from ER;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q29092	UniProtKB	Compositional bias	290	314	.	.	.	Note=Acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q29092	UniProtKB	Compositional bias	754	796	.	.	.	Note=Acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q29092	UniProtKB	Binding site	107	107	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P41148	
Q29092	UniProtKB	Binding site	149	149	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P41148	
Q29092	UniProtKB	Binding site	162	162	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P41148	
Q29092	UniProtKB	Binding site	199	199	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P41148	
Q29092	UniProtKB	Site	448	448	.	.	.	Note=Important for ATP hydrolysis;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P41148	
Q29092	UniProtKB	Modified residue	64	64	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P14625	
Q29092	UniProtKB	Modified residue	168	168	.	.	.	Note=N6-(2-hydroxyisobutyryl)lysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P14625	
Q29092	UniProtKB	Modified residue	172	172	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q66HD0	
Q29092	UniProtKB	Modified residue	306	306	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P14625	
Q29092	UniProtKB	Modified residue	403	403	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q66HD0	
Q29092	UniProtKB	Modified residue	404	404	.	.	.	Note=N6-succinyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P08113	
Q29092	UniProtKB	Modified residue	447	447	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P14625	
Q29092	UniProtKB	Modified residue	479	479	.	.	.	Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P08113	
Q29092	UniProtKB	Modified residue	633	633	.	.	.	Note=N6-succinyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P08113	
Q29092	UniProtKB	Glycosylation	62	62	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q29092	UniProtKB	Glycosylation	107	107	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q29092	UniProtKB	Glycosylation	217	217	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q29092	UniProtKB	Glycosylation	445	445	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q29092	UniProtKB	Glycosylation	481	481	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q29092	UniProtKB	Glycosylation	502	502	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q29092	UniProtKB	Disulfide bond	138	138	.	.	.	Note=Interchain;Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q29092	UniProtKB	Sequence conflict	48	48	.	.	.	Note=V->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
Q29092	UniProtKB	Sequence conflict	179	179	.	.	.	Note=A->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
Q29092	UniProtKB	Sequence conflict	332	334	.	.	.	Note=DWE->ELG;Ontology_term=ECO:0000305;evidence=ECO:0000305	
Q29092	UniProtKB	Sequence conflict	795	795	.	.	.	Note=E->EFVFQ;Ontology_term=ECO:0000305;evidence=ECO:0000305