##gff-version 3
Q64285	UniProtKB	Signal peptide	1	20	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q64285	UniProtKB	Chain	21	599	.	.	.	ID=PRO_0000008632;Note=Bile salt-activated lipase	
Q64285	UniProtKB	Repeat	559	569	.	.	.	Note=1	
Q64285	UniProtKB	Repeat	570	580	.	.	.	Note=2	
Q64285	UniProtKB	Repeat	581	588	.	.	.	Note=3	
Q64285	UniProtKB	Region	553	599	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q64285	UniProtKB	Region	559	588	.	.	.	Note=4 X 11 AA tandem repeats%2C O-glycosylated region	
Q64285	UniProtKB	Active site	214	214	.	.	.	Note=Acyl-ester intermediate;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10039	
Q64285	UniProtKB	Active site	340	340	.	.	.	Note=Charge relay system;Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q64285	UniProtKB	Active site	455	455	.	.	.	Note=Charge relay system;Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q64285	UniProtKB	Glycosylation	207	207	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q64285	UniProtKB	Glycosylation	325	325	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q64285	UniProtKB	Disulfide bond	84	100	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q64285	UniProtKB	Disulfide bond	266	277	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250