##gff-version 3 O14494 UniProtKB Chain 1 284 . . . ID=PRO_0000220905;Note=Phospholipid phosphatase 1 O14494 UniProtKB Topological domain 1 6 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q61469 O14494 UniProtKB Transmembrane 7 27 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 O14494 UniProtKB Topological domain 28 53 . . . Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q61469 O14494 UniProtKB Transmembrane 54 74 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 O14494 UniProtKB Topological domain 75 94 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q61469 O14494 UniProtKB Transmembrane 95 115 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 O14494 UniProtKB Topological domain 116 164 . . . Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q61469 O14494 UniProtKB Transmembrane 165 185 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 O14494 UniProtKB Topological domain 186 199 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q61469 O14494 UniProtKB Transmembrane 200 220 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 O14494 UniProtKB Topological domain 221 229 . . . Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q61469 O14494 UniProtKB Transmembrane 230 250 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 O14494 UniProtKB Topological domain 251 284 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q61469 O14494 UniProtKB Region 120 128 . . . Note=Phosphatase sequence motif I;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O34349 O14494 UniProtKB Region 168 171 . . . Note=Phosphatase sequence motif II;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O34349 O14494 UniProtKB Region 216 227 . . . Note=Phosphatase sequence motif III;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O34349 O14494 UniProtKB Region 260 284 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite O14494 UniProtKB Motif 5 7 . . . Note=PDZ-binding%3B involved in localization to the apical cell membrane;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14527693;Dbxref=PMID:14527693 O14494 UniProtKB Compositional bias 269 284 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite O14494 UniProtKB Active site 171 171 . . . Note=Proton donors;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O34349 O14494 UniProtKB Active site 223 223 . . . Note=Nucleophile;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O34349 O14494 UniProtKB Site 227 227 . . . Note=Stabilizes the active site histidine for nucleophilic attack;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O34349 O14494 UniProtKB Glycosylation 142 142 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 O14494 UniProtKB Alternative sequence 21 70 . . . ID=VSP_009651;Note=In isoform 2. GLPFAILTSRHTPFQRGVFCNDESIKYPYKEDTIPYALLGGIIIPFSIIV->SMPMAVLKLGQIYPFQRGFFCKDNSINYPYHDSTVTSTVLILVGVGLPISS;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:9570154;Dbxref=PMID:9570154 O14494 UniProtKB Mutagenesis 217 217 . . . Note=Decreased lipid phosphatase activity. R->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15461590;Dbxref=PMID:15461590 O14494 UniProtKB Sequence conflict 27 27 . . . Note=L->FTSRHI;Ontology_term=ECO:0000305;evidence=ECO:0000305 O14494 UniProtKB Sequence conflict 91 91 . . . Note=R->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 O14494 UniProtKB Sequence conflict 55 55 . . . Note=V->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 O14494 UniProtKB Sequence conflict 56 56 . . . Note=T->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 O14494 UniProtKB Sequence conflict 69 69 . . . Note=I->V;Ontology_term=ECO:0000305;evidence=ECO:0000305