##gff-version 3
Q2KJH6	UniProtKB	Signal peptide	1	18	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q2KJH6	UniProtKB	Chain	19	418	.	.	.	ID=PRO_0000253604;Note=Serpin H1	
Q2KJH6	UniProtKB	Motif	415	418	.	.	.	Note=Prevents secretion from ER;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10138	
Q2KJH6	UniProtKB	Site	377	378	.	.	.	Note=Reactive bond homolog;Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q2KJH6	UniProtKB	Modified residue	94	94	.	.	.	Note=N6-succinyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P19324	
Q2KJH6	UniProtKB	Modified residue	141	141	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P50454	
Q2KJH6	UniProtKB	Modified residue	207	207	.	.	.	Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P19324	
Q2KJH6	UniProtKB	Modified residue	296	296	.	.	.	Note=N6-succinyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P19324	
Q2KJH6	UniProtKB	Modified residue	319	319	.	.	.	Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P19324	
Q2KJH6	UniProtKB	Glycosylation	120	120	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q2KJH6	UniProtKB	Glycosylation	125	125	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255