##gff-version 3
Q99JY8	UniProtKB	Chain	1	312	.	.	.	ID=PRO_0000220913;Note=Phospholipid phosphatase 3	
Q99JY8	UniProtKB	Topological domain	1	33	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16099422;Dbxref=PMID:16099422	
Q99JY8	UniProtKB	Transmembrane	34	54	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q99JY8	UniProtKB	Topological domain	55	85	.	.	.	Note=Extracellular;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16099422;Dbxref=PMID:16099422	
Q99JY8	UniProtKB	Transmembrane	86	106	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q99JY8	UniProtKB	Topological domain	107	123	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16099422;Dbxref=PMID:16099422	
Q99JY8	UniProtKB	Transmembrane	124	144	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q99JY8	UniProtKB	Topological domain	145	194	.	.	.	Note=Extracellular;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16099422;Dbxref=PMID:16099422	
Q99JY8	UniProtKB	Transmembrane	195	215	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q99JY8	UniProtKB	Topological domain	216	226	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16099422;Dbxref=PMID:16099422	
Q99JY8	UniProtKB	Transmembrane	227	244	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q99JY8	UniProtKB	Topological domain	245	258	.	.	.	Note=Extracellular;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16099422;Dbxref=PMID:16099422	
Q99JY8	UniProtKB	Transmembrane	259	279	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q99JY8	UniProtKB	Topological domain	280	312	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16099422;Dbxref=PMID:16099422	
Q99JY8	UniProtKB	Region	149	157	.	.	.	Note=Phosphatase sequence motif I;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O34349	
Q99JY8	UniProtKB	Region	197	200	.	.	.	Note=Phosphatase sequence motif II;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O34349	
Q99JY8	UniProtKB	Region	245	256	.	.	.	Note=Phosphatase sequence motif III;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O34349	
Q99JY8	UniProtKB	Region	276	312	.	.	.	Note=Mediates interaction with CTNND1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O14495	
Q99JY8	UniProtKB	Motif	109	110	.	.	.	Note=Dityrosine basolateral targeting motif;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O14495	
Q99JY8	UniProtKB	Motif	183	185	.	.	.	Note=Integrin-binding motif;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16099422;Dbxref=PMID:16099422	
Q99JY8	UniProtKB	Active site	200	200	.	.	.	Note=Proton donors;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O34349	
Q99JY8	UniProtKB	Active site	252	252	.	.	.	Note=Nucleophile;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O34349	
Q99JY8	UniProtKB	Site	256	256	.	.	.	Note=Stabilizes the active site histidine for nucleophilic attack;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O34349	
Q99JY8	UniProtKB	Modified residue	19	19	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O14495	
Q99JY8	UniProtKB	Glycosylation	171	171	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q99JY8	UniProtKB	Sequence conflict	187	187	.	.	.	Note=S->C;Ontology_term=ECO:0000305;evidence=ECO:0000305