##gff-version 3
Q9TT38	UniProtKB	Chain	1	748	.	.	.	ID=PRO_0000345135;Note=Cytosolic phospholipase A2	
Q9TT38	UniProtKB	Domain	6	122	.	.	.	Note=C2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00041	
Q9TT38	UniProtKB	Domain	138	739	.	.	.	Note=PLA2c;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00555	
Q9TT38	UniProtKB	Region	1	178	.	.	.	Note=Phospholipid binding;Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q9TT38	UniProtKB	Region	428	458	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q9TT38	UniProtKB	Active site	228	228	.	.	.	Note=Nucleophile;Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q9TT38	UniProtKB	Active site	548	548	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q9TT38	UniProtKB	Binding site	40	40	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q9TT38	UniProtKB	Binding site	40	40	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q9TT38	UniProtKB	Binding site	41	41	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q9TT38	UniProtKB	Binding site	43	43	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q9TT38	UniProtKB	Binding site	43	43	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q9TT38	UniProtKB	Binding site	65	65	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q9TT38	UniProtKB	Binding site	93	93	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q9TT38	UniProtKB	Binding site	94	94	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q9TT38	UniProtKB	Binding site	95	95	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
Q9TT38	UniProtKB	Modified residue	2	2	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P47712	
Q9TT38	UniProtKB	Modified residue	268	268	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P47712	
Q9TT38	UniProtKB	Modified residue	434	434	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P50393	
Q9TT38	UniProtKB	Modified residue	435	435	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P47712	
Q9TT38	UniProtKB	Modified residue	437	437	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P47712	
Q9TT38	UniProtKB	Modified residue	505	505	.	.	.	Note=Phosphoserine%3B by MAPK;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P47712	
Q9TT38	UniProtKB	Modified residue	514	514	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P50393	
Q9TT38	UniProtKB	Modified residue	726	726	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P47712	
Q9TT38	UniProtKB	Modified residue	728	728	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P47712	
Q9TT38	UniProtKB	Cross-link	540	540	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P47712	
Q9TT38	UniProtKB	Cross-link	605	605	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P47712