##gff-version 3 P47013 UniProtKB Chain 1 409 . . . ID=PRO_0000203037;Note=Dihydrosphingosine 1-phosphate phosphatase LCB3 P47013 UniProtKB Topological domain 1 86 . . . Note=Lumenal;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258 P47013 UniProtKB Transmembrane 87 107 . . . Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255 P47013 UniProtKB Topological domain 108 112 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258 P47013 UniProtKB Transmembrane 113 133 . . . Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255 P47013 UniProtKB Topological domain 134 182 . . . Note=Lumenal;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258 P47013 UniProtKB Transmembrane 183 203 . . . Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255 P47013 UniProtKB Topological domain 204 207 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258 P47013 UniProtKB Transmembrane 208 228 . . . Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255 P47013 UniProtKB Topological domain 229 245 . . . Note=Lumenal;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258 P47013 UniProtKB Transmembrane 246 266 . . . Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255 P47013 UniProtKB Topological domain 267 276 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258 P47013 UniProtKB Transmembrane 277 297 . . . Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255 P47013 UniProtKB Topological domain 298 315 . . . Note=Lumenal;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258 P47013 UniProtKB Transmembrane 316 336 . . . Note=Helical%3B Name%3D7;Ontology_term=ECO:0000255;evidence=ECO:0000255 P47013 UniProtKB Topological domain 337 384 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16847258;Dbxref=PMID:16847258 P47013 UniProtKB Transmembrane 385 405 . . . Note=Helical%3B Name%3D8;Ontology_term=ECO:0000255;evidence=ECO:0000255 P47013 UniProtKB Topological domain 406 409 . . . Note=Lumenal;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16847258;Dbxref=PMID:16847258 P47013 UniProtKB Region 15 35 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P47013 UniProtKB Region 128 136 . . . Note=Phosphatase sequence motif I;Ontology_term=ECO:0000305;evidence=ECO:0000305 P47013 UniProtKB Region 157 160 . . . Note=Phosphatase sequence motif II;Ontology_term=ECO:0000305;evidence=ECO:0000305 P47013 UniProtKB Region 203 214 . . . Note=Phosphatase sequence motif III;Ontology_term=ECO:0000305;evidence=ECO:0000305 P47013 UniProtKB Active site 160 160 . . . Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P0A924 P47013 UniProtKB Active site 210 210 . . . Note=Nucleophile;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P0A924 P47013 UniProtKB Site 214 214 . . . Note=Stabilizes the active site histidine for nucleophilic attack;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P0A924 P47013 UniProtKB Modified residue 16 16 . . . Note=Phosphothreonine;Ontology_term=ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:17330950,ECO:0007744|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 P47013 UniProtKB Modified residue 18 18 . . . Note=Phosphoserine;Ontology_term=ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:17330950,ECO:0007744|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198 P47013 UniProtKB Mutagenesis 128 128 . . . Note=Impairs dihydrosphingosine 1-phosphate phosphatase activity. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12786943;Dbxref=PMID:12786943 P47013 UniProtKB Mutagenesis 160 160 . . . Note=Impairs dihydrosphingosine 1-phosphate phosphatase activity. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12786943;Dbxref=PMID:12786943 P47013 UniProtKB Mutagenesis 210 210 . . . Note=Impairs dihydrosphingosine 1-phosphate phosphatase activity. H->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12786943;Dbxref=PMID:12786943