##gff-version 3 O88488 UniProtKB Signal peptide 1 18 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 O88488 UniProtKB Chain 19 2302 . . . ID=PRO_5000054322;Note=Phosphatidylinositol phosphatase PTPRQ O88488 UniProtKB Topological domain 19 1908 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 O88488 UniProtKB Transmembrane 1909 1929 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 O88488 UniProtKB Topological domain 1930 2302 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 O88488 UniProtKB Domain 60 155 . . . Note=Fibronectin type-III 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00316 O88488 UniProtKB Domain 159 254 . . . Note=Fibronectin type-III 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00316 O88488 UniProtKB Domain 310 398 . . . Note=Fibronectin type-III 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00316 O88488 UniProtKB Domain 401 501 . . . Note=Fibronectin type-III 4;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00316 O88488 UniProtKB Domain 474 566 . . . Note=Fibronectin type-III 5;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00316 O88488 UniProtKB Domain 570 665 . . . Note=Fibronectin type-III 6;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00316 O88488 UniProtKB Domain 670 759 . . . Note=Fibronectin type-III 7;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00316 O88488 UniProtKB Domain 764 854 . . . Note=Fibronectin type-III 8;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00316 O88488 UniProtKB Domain 859 948 . . . Note=Fibronectin type-III 9;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00316 O88488 UniProtKB Domain 953 1053 . . . Note=Fibronectin type-III 10;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00316 O88488 UniProtKB Domain 1058 1151 . . . Note=Fibronectin type-III 11;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00316 O88488 UniProtKB Domain 1156 1243 . . . Note=Fibronectin type-III 12;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00316 O88488 UniProtKB Domain 1248 1341 . . . Note=Fibronectin type-III 13;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00316 O88488 UniProtKB Domain 1345 1431 . . . Note=Fibronectin type-III 14;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00316 O88488 UniProtKB Domain 1435 1539 . . . Note=Fibronectin type-III 15;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00316 O88488 UniProtKB Domain 1544 1642 . . . Note=Fibronectin type-III 16;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00316 O88488 UniProtKB Domain 1647 1748 . . . Note=Fibronectin type-III 17;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00316 O88488 UniProtKB Domain 2006 2262 . . . Note=Tyrosine-protein phosphatase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00160 O88488 UniProtKB Active site 2203 2203 . . . Note=Phosphocysteine intermediate;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00160,ECO:0000255|PROSITE-ProRule:PRU10044 O88488 UniProtKB Glycosylation 54 54 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 O88488 UniProtKB Glycosylation 162 162 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 O88488 UniProtKB Glycosylation 169 169 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 O88488 UniProtKB Glycosylation 318 318 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 O88488 UniProtKB Glycosylation 354 354 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 O88488 UniProtKB Glycosylation 389 389 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 O88488 UniProtKB Glycosylation 733 733 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 O88488 UniProtKB Glycosylation 746 746 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 O88488 UniProtKB Glycosylation 904 904 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 O88488 UniProtKB Glycosylation 998 998 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 O88488 UniProtKB Glycosylation 1010 1010 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 O88488 UniProtKB Glycosylation 1040 1040 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 O88488 UniProtKB Glycosylation 1251 1251 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 O88488 UniProtKB Glycosylation 1256 1256 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 O88488 UniProtKB Glycosylation 1805 1805 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 O88488 UniProtKB Mutagenesis 2171 2171 . . . Note=Enhances the tyrosine-protein phosphatase activity but abolishes the phosphatidylinositol phosphatase activity. E->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12802008;Dbxref=PMID:12802008 O88488 UniProtKB Mutagenesis 2203 2203 . . . Note=Abolishes the weak tyrosine-protein phosphatase activity. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12802008;Dbxref=PMID:12802008