##gff-version 3
Q99574	UniProtKB	Signal peptide	1	16	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q99574	UniProtKB	Chain	17	410	.	.	.	ID=PRO_0000032521;Note=Neuroserpin	
Q99574	UniProtKB	Site	362	363	.	.	.	Note=Reactive bond;Ontology_term=ECO:0000269,ECO:0000305;evidence=ECO:0000269|PubMed:19265707,ECO:0000305|PubMed:19285087;Dbxref=PMID:19265707,PMID:19285087	
Q99574	UniProtKB	Glycosylation	157	157	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q99574	UniProtKB	Glycosylation	321	321	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q99574	UniProtKB	Glycosylation	401	401	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q99574	UniProtKB	Glycosylation	403	403	.	.	.	Note=O-linked (Xyl...) (chondroitin sulfate) serine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25326458;Dbxref=PMID:25326458	
Q99574	UniProtKB	Natural variant	49	49	.	.	.	ID=VAR_008520;Note=In FENIB%3B Syracuse%3B decreased protein stability%3B decreased proteinase inhibitor activity%3B increased tendency to form polymers. S->P;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10517635,ECO:0000269|PubMed:11880376;Dbxref=dbSNP:rs121909051,PMID:10517635,PMID:11880376	
Q99574	UniProtKB	Natural variant	52	52	.	.	.	ID=VAR_008521;Note=In FENIB%3B Portland. S->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10517635;Dbxref=PMID:10517635	
Q99574	UniProtKB	Mutagenesis	161	161	.	.	.	Note=Increases protein stability and abolishes tendency to form polymers. No effect on inhibitory activity. N->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19285087;Dbxref=PMID:19285087	
Q99574	UniProtKB	Mutagenesis	162	162	.	.	.	Note=Increases protein stability and abolishes tendency to form polymers. No effect on inhibitory activity. L->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19285087;Dbxref=PMID:19285087	
Q99574	UniProtKB	Mutagenesis	163	163	.	.	.	Note=Increases protein stability and decreases tendency to form polymers. No effect on inhibitory activity. V->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19285087;Dbxref=PMID:19285087	
Q99574	UniProtKB	Mutagenesis	289	289	.	.	.	Note=Slightly decreases inhibitory activity. No effect on thermal stability. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26329378;Dbxref=PMID:26329378	
Q99574	UniProtKB	Mutagenesis	340	340	.	.	.	Note=Increases protein stability and decreases tendency to form polymers. No effect on inhibitory activity. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19285087;Dbxref=PMID:19285087	
Q99574	UniProtKB	Sequence conflict	70	70	.	.	.	Note=K->E;Ontology_term=ECO:0000305;evidence=ECO:0000305	
Q99574	UniProtKB	Sequence conflict	326	326	.	.	.	Note=S->Y;Ontology_term=ECO:0000305;evidence=ECO:0000305	
Q99574	UniProtKB	Helix	25	40	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3F02	
Q99574	UniProtKB	Beta strand	46	48	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3F02	
Q99574	UniProtKB	Helix	50	63	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3F02	
Q99574	UniProtKB	Helix	66	76	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3F02	
Q99574	UniProtKB	Helix	86	91	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3F02	
Q99574	UniProtKB	Turn	101	103	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3FGQ	
Q99574	UniProtKB	Beta strand	105	115	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3F02	
Q99574	UniProtKB	Helix	122	132	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3F02	
Q99574	UniProtKB	Beta strand	135	139	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3F02	
Q99574	UniProtKB	Helix	144	157	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3F02	
Q99574	UniProtKB	Turn	158	161	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3F02	
Q99574	UniProtKB	Helix	169	171	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3F02	
Q99574	UniProtKB	Beta strand	176	192	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3F02	
Q99574	UniProtKB	Helix	196	198	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3F02	
Q99574	UniProtKB	Beta strand	200	205	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3F02	
Q99574	UniProtKB	Beta strand	211	229	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3F02	
Q99574	UniProtKB	Beta strand	238	246	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3F02	
Q99574	UniProtKB	Beta strand	249	257	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3F02	
Q99574	UniProtKB	Helix	264	267	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3F02	
Q99574	UniProtKB	Helix	268	270	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3F02	
Q99574	UniProtKB	Helix	273	282	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3F02	
Q99574	UniProtKB	Beta strand	284	293	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3F02	
Q99574	UniProtKB	Beta strand	295	302	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3F02	
Q99574	UniProtKB	Helix	303	310	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3F02	
Q99574	UniProtKB	Helix	314	316	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3F02	
Q99574	UniProtKB	Turn	323	325	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3F02	
Q99574	UniProtKB	Beta strand	331	344	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3F02	
Q99574	UniProtKB	Beta strand	346	361	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3F02	
Q99574	UniProtKB	Beta strand	369	371	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3F02	
Q99574	UniProtKB	Beta strand	376	382	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3F02	
Q99574	UniProtKB	Turn	383	385	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3F02	
Q99574	UniProtKB	Beta strand	388	395	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3F02