##gff-version 3
O46647	UniProtKB	Signal peptide	1	27	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
O46647	UniProtKB	Chain	28	475	.	.	.	ID=PRO_0000017777;Note=Lipoprotein lipase	
O46647	UniProtKB	Domain	341	464	.	.	.	Note=PLAT;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00152	
O46647	UniProtKB	Region	32	53	.	.	.	Note=Interaction with GPIHBP1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P06858	
O46647	UniProtKB	Region	417	421	.	.	.	Note=Important for interaction with lipoprotein particles;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P06858	
O46647	UniProtKB	Region	430	434	.	.	.	Note=Important for heparin binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P06858	
O46647	UniProtKB	Region	443	467	.	.	.	Note=Interaction with GPIHBP1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P06858	
O46647	UniProtKB	Active site	159	159	.	.	.	Note=Nucleophile;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P06858	
O46647	UniProtKB	Active site	183	183	.	.	.	Note=Charge relay system;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10037	
O46647	UniProtKB	Active site	268	268	.	.	.	Note=Charge relay system;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10037	
O46647	UniProtKB	Binding site	194	194	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P06858	
O46647	UniProtKB	Binding site	197	197	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P06858	
O46647	UniProtKB	Binding site	199	199	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P06858	
O46647	UniProtKB	Binding site	202	202	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P06858	
O46647	UniProtKB	Modified residue	121	121	.	.	.	Note=3'-nitrotyrosine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q06000	
O46647	UniProtKB	Modified residue	191	191	.	.	.	Note=3'-nitrotyrosine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q06000	
O46647	UniProtKB	Modified residue	343	343	.	.	.	Note=3'-nitrotyrosine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q06000	
O46647	UniProtKB	Glycosylation	70	70	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
O46647	UniProtKB	Glycosylation	386	386	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
O46647	UniProtKB	Disulfide bond	54	67	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00152	
O46647	UniProtKB	Disulfide bond	243	266	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00152	
O46647	UniProtKB	Disulfide bond	291	310	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00152	
O46647	UniProtKB	Disulfide bond	302	305	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00152	
O46647	UniProtKB	Disulfide bond	445	465	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00152	
O46647	UniProtKB	Natural variant	241	241	.	.	.	Note=In chylomicronemia syndrome%3B no lipase activity. P->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9852258;Dbxref=PMID:9852258