##gff-version 3 P47713 UniProtKB Chain 1 748 . . . ID=PRO_0000187263;Note=Cytosolic phospholipase A2 P47713 UniProtKB Domain 6 122 . . . Note=C2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00041 P47713 UniProtKB Domain 140 739 . . . Note=PLA2c;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00555 P47713 UniProtKB Region 1 178 . . . Note=Phospholipid binding;Ontology_term=ECO:0000305;evidence=ECO:0000305 P47713 UniProtKB Region 427 458 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P47713 UniProtKB Compositional bias 427 457 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P47713 UniProtKB Active site 228 228 . . . Note=Nucleophile;Ontology_term=ECO:0000250;evidence=ECO:0000250 P47713 UniProtKB Active site 548 548 . . . Note=Proton acceptor;Ontology_term=ECO:0000250;evidence=ECO:0000250 P47713 UniProtKB Binding site 40 40 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 P47713 UniProtKB Binding site 40 40 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 P47713 UniProtKB Binding site 41 41 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 P47713 UniProtKB Binding site 43 43 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 P47713 UniProtKB Binding site 43 43 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 P47713 UniProtKB Binding site 65 65 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 P47713 UniProtKB Binding site 93 93 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 P47713 UniProtKB Binding site 94 94 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 P47713 UniProtKB Binding site 95 95 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 P47713 UniProtKB Modified residue 2 2 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P47712 P47713 UniProtKB Modified residue 268 268 . . . Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P47712 P47713 UniProtKB Modified residue 434 434 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P50393 P47713 UniProtKB Modified residue 435 435 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:21183079;Dbxref=PMID:21183079 P47713 UniProtKB Modified residue 437 437 . . . Note=Phosphoserine;Ontology_term=ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:19144319,ECO:0007744|PubMed:21183079;Dbxref=PMID:19144319,PMID:21183079 P47713 UniProtKB Modified residue 505 505 . . . Note=Phosphoserine%3B by MAPK;Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:10978317,ECO:0007744|PubMed:21183079;Dbxref=PMID:10978317,PMID:21183079 P47713 UniProtKB Modified residue 515 515 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P50393 P47713 UniProtKB Modified residue 726 726 . . . Note=Phosphoserine;Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:10978317,ECO:0007744|PubMed:21183079;Dbxref=PMID:10978317,PMID:21183079 P47713 UniProtKB Modified residue 728 728 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:21183079;Dbxref=PMID:21183079 P47713 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 P47713 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