##gff-version 3 Q06495 UniProtKB Chain 1 639 . . . ID=PRO_0000068607;Note=Sodium-dependent phosphate transport protein 2A Q06495 UniProtKB Topological domain 1 103 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q06496 Q06495 UniProtKB Transmembrane 104 125 . . . Note=Helical%3B Name%3DM1;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q06495 UniProtKB Topological domain 126 145 . . . Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q06496 Q06495 UniProtKB Transmembrane 146 163 . . . Note=Helical%3B Name%3DM2;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q06495 UniProtKB Topological domain 164 165 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q06496 Q06495 UniProtKB Transmembrane 166 185 . . . Note=Helical%3B Name%3DM3;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q06495 UniProtKB Topological domain 186 347 . . . Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q06496 Q06495 UniProtKB Transmembrane 348 370 . . . Note=Helical%3B Name%3DM4;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q06495 UniProtKB Topological domain 371 412 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q06496 Q06495 UniProtKB Transmembrane 413 436 . . . Note=Helical%3B Name%3DM5;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q06495 UniProtKB Topological domain 437 466 . . . Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q06496 Q06495 UniProtKB Transmembrane 467 487 . . . Note=Helical%3B Name%3DM6;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q06495 UniProtKB Topological domain 488 513 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q06496 Q06495 UniProtKB Transmembrane 514 534 . . . Note=Helical%3B Name%3DM7;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q06495 UniProtKB Topological domain 535 539 . . . Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q06496 Q06495 UniProtKB Transmembrane 540 561 . . . Note=Helical%3B Name%3DM8;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q06495 UniProtKB Topological domain 562 639 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q06496 Q06495 UniProtKB Modified residue 14 14 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q06496 Q06495 UniProtKB Modified residue 34 34 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q60825 Q06495 UniProtKB Modified residue 508 508 . . . Note=Phosphothreonine%3B by PKC;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q06495 UniProtKB Modified residue 607 607 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q06496 Q06495 UniProtKB Modified residue 623 623 . . . Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q60825 Q06495 UniProtKB Modified residue 625 625 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q60825 Q06495 UniProtKB Glycosylation 298 298 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q06495 UniProtKB Glycosylation 323 323 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q06495 UniProtKB Glycosylation 330 330 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q06495 UniProtKB Disulfide bond 225 522 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q06496 Q06495 UniProtKB Disulfide bond 306 336 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q06496 Q06495 UniProtKB Alternative sequence 313 639 . . . ID=VSP_042311;Note=In isoform 2. APTSMSRAEANSSQTLGNATMEKCNHIFVDTGLPDLAVGLILLAGSLVLLCTCLILLVKMLNSLLKGQVAKVIQKVINTDFPAPFTWVTGYFAMVVGASMTFVVQSSSVFTSAITPLIGLGVISIERAYPLTLGSNIGTTTTAILAALASPREKLSSAFQIALCHFFFNISGILLWYPVPCTRLPIRMAKALGKRTAKYRWFAVLYLLVCFLLLPSLVFGISMAGWQVMVGVGTPFGALLAFVVLINVLQSRSPGHLPKWLQTWDFLPRWMHSLKPLDHLITRATLCCARPEPRSPPLPPRVFLEELPPATPSPRLALPAHHNATRL->QNLEGREITHFDLRKKQAMEDSSVPHCP;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:14702039;Dbxref=PMID:14702039 Q06495 UniProtKB Natural variant 48 48 . . . ID=VAR_024765;Note=In NPHLOP1%3B causes hypophosphatemic urolithiasis%3B results in lower phosphate current%2C decreases affinity for phosphate and decreases phosphate uptake compared to wild-type%3B shows a dominant-negative effect%3B requires 2 nucleotide substitutions. A->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12324554;Dbxref=dbSNP:rs121918610,PMID:12324554 Q06495 UniProtKB Natural variant 91 97 . . . ID=VAR_077913;Note=In HCINF2%3B no change in phosphate transport activity%3B changed localization to the apical plasma membrane%3B partial retention inside the cell. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26047794;Dbxref=PMID:26047794 Q06495 UniProtKB Natural variant 147 147 . . . ID=VAR_024766;Note=In NPHLOP1%3B causes hypophosphatemic osteoporosis%3B results in lower phosphate current%2C decreases affinity for phosphate and decreases phosphate uptake compared to wild-type%3B shows a dominant-negative effect. V->M;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12324554;Dbxref=dbSNP:rs121918611,PMID:12324554 Q06495 UniProtKB Natural variant 153 153 . . . ID=VAR_077914;Note=In HCINF2%3B loss of phosphate transport activity%3B loss of localization to apical plasma membrane%3B display a complete intracellular retention and no detectable actin colocalization. G->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26047794;Dbxref=dbSNP:rs769409705,PMID:26047794 Q06495 UniProtKB Natural variant 153 153 . . . ID=VAR_077915;Note=In HCINF2%3B loss of phosphate transport activity%3B loss of localization to apical plasma membrane%3B display a complete intracellular retention and no detectable actin colocalization. G->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26047794;Dbxref=dbSNP:rs769409705,PMID:26047794 Q06495 UniProtKB Natural variant 155 155 . . . ID=VAR_077916;Note=In HCINF2%3B loss of phosphate transport activity%3B loss of localization to apical plasma membrane%3B display a complete intracellular retention and no detectable actin colocalization. L->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26047794;Dbxref=dbSNP:rs369770760,PMID:26047794 Q06495 UniProtKB Natural variant 160 160 . . . ID=VAR_063812;Note=In FRTS2%3B loss of function in the homozygous state%3B loss of localization to cell membrane. V->VILVTVLV;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20335586;Dbxref=PMID:20335586 Q06495 UniProtKB Natural variant 215 215 . . . ID=VAR_077917;Note=In HCINF2. R->W;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26047794;Dbxref=dbSNP:rs577273266,PMID:26047794 Q06495 UniProtKB Natural variant 336 336 . . . ID=VAR_077918;Note=In HCINF2%3B loss of phosphate transport activity%3B loss of localization to apical plasma membrane%3B display a complete intracellular retention and no detectable actin colocalization. C->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26047794;Dbxref=dbSNP:rs876661338,PMID:26047794 Q06495 UniProtKB Natural variant 408 408 . . . ID=VAR_077919;Note=In HCINF2%3B loss of phosphate transport activity%3B loss of localization to apical plasma membrane%3B a complete intracellular retention and no detectable actin colocalization. V->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26047794;Dbxref=dbSNP:rs140649226,PMID:26047794 Q06495 UniProtKB Natural variant 488 488 . . . ID=VAR_077920;Note=In HCINF2%3B loss of phosphate transport activity%3B loss of localization to apical plasma membrane%3B display a complete intracellular retention and no detectable actin colocalization. W->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26047794;Dbxref=PMID:26047794