##gff-version 3
P29457	UniProtKB	Signal peptide	1	17	.	.	.	Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:1654327,ECO:0000269|PubMed:2158279;Dbxref=PMID:1654327,PMID:2158279	
P29457	UniProtKB	Chain	18	417	.	.	.	ID=PRO_0000032518;Note=Serpin H1	
P29457	UniProtKB	Motif	414	417	.	.	.	Note=Prevents secretion from ER;Ontology_term=ECO:0000305;evidence=ECO:0000305	
P29457	UniProtKB	Site	376	377	.	.	.	Note=Reactive bond homolog;Ontology_term=ECO:0000250;evidence=ECO:0000250	
P29457	UniProtKB	Modified residue	93	93	.	.	.	Note=N6-succinyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P19324	
P29457	UniProtKB	Modified residue	140	140	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P50454	
P29457	UniProtKB	Modified residue	206	206	.	.	.	Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P19324	
P29457	UniProtKB	Modified residue	295	295	.	.	.	Note=N6-succinyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P19324	
P29457	UniProtKB	Modified residue	318	318	.	.	.	Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P19324	
P29457	UniProtKB	Glycosylation	119	119	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P29457	UniProtKB	Glycosylation	124	124	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P29457	UniProtKB	Glycosylation	394	394	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255