##gff-version 3
P42837	UniProtKB	Chain	1	879	.	.	.	ID=PRO_0000209742;Note=Polyphosphoinositide phosphatase	
P42837	UniProtKB	Domain	166	528	.	.	.	Note=SAC;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00183	
P42837	UniProtKB	Region	761	879	.	.	.	Note=Required for vacuolar localization	
P42837	UniProtKB	Modified residue	829	829	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:18407956;Dbxref=PMID:18407956	
P42837	UniProtKB	Mutagenesis	59	59	.	.	.	Note=Defective activation of FAB1. I->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17572665;Dbxref=PMID:17572665	
P42837	UniProtKB	Mutagenesis	469	469	.	.	.	Note=Partially defective in both hyperosmotic shock-induced PtdIns(3%2C5)P2 elevation and turnover. D->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16492811;Dbxref=PMID:16492811	
P42837	UniProtKB	Mutagenesis	519	519	.	.	.	Note=In FIG4-1%3B loss of catalytic activity in vitro. Almost 3-fold increase in PtdIns(3%2C5)P2 level in vivo. Partially defective in both hyperosmotic shock-induced PtdIns(3%2C5)P2 elevation and turnover. G->R;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11950935,ECO:0000269|PubMed:14528018,ECO:0000269|PubMed:16492811;Dbxref=PMID:11950935,PMID:14528018,PMID:16492811