NPT2A_HUMAN
ID NPT2A_HUMAN Reviewed; 639 AA.
AC Q06495; B4DPE3;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 192.
DE RecName: Full=Sodium-dependent phosphate transport protein 2A;
DE Short=Sodium-phosphate transport protein 2A;
DE AltName: Full=Na(+)-dependent phosphate cotransporter 2A;
DE AltName: Full=NaPi-3 {ECO:0000303|PubMed:8327470};
DE AltName: Full=Sodium/phosphate cotransporter 2A;
DE Short=Na(+)/Pi cotransporter 2A;
DE Short=NaPi-2a;
DE AltName: Full=Solute carrier family 34 member 1 {ECO:0000312|HGNC:HGNC:11019};
GN Name=SLC34A1 {ECO:0000312|HGNC:HGNC:11019};
GN Synonyms=NPT2 {ECO:0000250|UniProtKB:Q60825},
GN SLC17A2 {ECO:0000312|HGNC:HGNC:11019};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TRANSPORTER ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE SPECIFICITY.
RC TISSUE=Kidney;
RX PubMed=8327470; DOI=10.1073/pnas.90.13.5979;
RA Magagnin S., Werner A., Markovich D., Sorribas V., Stange G., Biber J.,
RA Murer H.;
RT "Expression cloning of human and rat renal cortex Na/Pi cotransport.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:5979-5983(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Kidney;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [4]
RP INTERACTION WITH SLC9A3R1.
RX PubMed=22506049; DOI=10.1371/journal.pone.0034764;
RA Courbebaisse M., Leroy C., Bakouh N., Salaun C., Beck L., Grandchamp B.,
RA Planelles G., Hall R.A., Friedlander G., Prie D.;
RT "A new human NHERF1 mutation decreases renal phosphate transporter NPT2a
RT expression by a PTH-independent mechanism.";
RL PLoS ONE 7:E34764-E34764(2012).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, TRANSPORTER ACTIVITY, INVOLVEMENT IN
RP HCINF2, VARIANTS HCINF2 91-VAL--ALA-97 DEL; ALA-153; VAL-153; PRO-155;
RP TRP-215; GLY-336; GLU-408 AND ARG-488, AND CHARACTERIZATION OF VARIANTS
RP HCINF2 91-VAL--ALA-97 DEL; ALA-153; VAL-153; PRO-155; GLY-336; GLU-408 AND
RP ARG-488.
RX PubMed=26047794; DOI=10.1681/asn.2014101025;
RA Schlingmann K.P., Ruminska J., Kaufmann M., Dursun I., Patti M., Kranz B.,
RA Pronicka E., Ciara E., Akcay T., Bulus D., Cornelissen E.A., Gawlik A.,
RA Sikora P., Patzer L., Galiano M., Boyadzhiev V., Dumic M., Vivante A.,
RA Kleta R., Dekel B., Levtchenko E., Bindels R.J., Rust S., Forster I.C.,
RA Hernando N., Jones G., Wagner C.A., Konrad M.;
RT "Autosomal-recessive mutations in SLC34A1 encoding sodium-phosphate
RT cotransporter 2A cause idiopathic infantile hypercalcemia.";
RL J. Am. Soc. Nephrol. 27:604-614(2016).
RN [6]
RP VARIANTS NPHLOP1 PHE-48 AND MET-147, CHARACTERIZATION OF VARIANTS NPHLOP1
RP PHE-48 AND MET-147, FUNCTION, AND TRANSPORTER ACTIVITY.
RX PubMed=12324554; DOI=10.1056/nejmoa020028;
RA Prie D., Huart V., Bakouh N., Planelles G., Dellis O., Gerard B., Hulin P.,
RA Benque-Blanchet F., Silve C., Grandchamp B., Friedlander G.;
RT "Nephrolithiasis and osteoporosis associated with hypophosphatemia caused
RT by mutations in the type 2a sodium-phosphate cotransporter.";
RL N. Engl. J. Med. 347:983-991(2002).
RN [7]
RP VARIANT FRTS2 ILE-LEU-VAL-THR-VAL-LEU-VAL-160 INS, CHARACTERIZATION OF
RP VARIANT FRTS2 ILE-LEU-VAL-THR-VAL-LEU-VAL-160 INS, FUNCTION, TRANSPORTER
RP ACTIVITY, AND SUBCELLULAR LOCATION.
RX PubMed=20335586; DOI=10.1056/nejmoa0905647;
RA Magen D., Berger L., Coady M.J., Ilivitzki A., Militianu D., Tieder M.,
RA Selig S., Lapointe J.Y., Zelikovic I., Skorecki K.;
RT "A loss-of-function mutation in NaPi-IIa and renal Fanconi's syndrome.";
RL N. Engl. J. Med. 362:1102-1109(2010).
CC -!- FUNCTION: Involved in actively transporting phosphate into cells via
CC Na(+) cotransport in the renal brush border membrane (PubMed:26047794,
CC PubMed:8327470, PubMed:12324554, PubMed:20335586). The cotransport has
CC a Na(+):Pi stoichiometry of 3:1 and is electrogenic (By similarity).
CC {ECO:0000250|UniProtKB:Q06496, ECO:0000269|PubMed:12324554,
CC ECO:0000269|PubMed:20335586, ECO:0000269|PubMed:26047794,
CC ECO:0000269|PubMed:8327470}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3 Na(+)(out) + phosphate(out) = 3 Na(+)(in) + phosphate(in);
CC Xref=Rhea:RHEA:71255, ChEBI:CHEBI:29101, ChEBI:CHEBI:43474;
CC Evidence={ECO:0000269|PubMed:12324554, ECO:0000269|PubMed:20335586,
CC ECO:0000269|PubMed:26047794, ECO:0000269|PubMed:8327470};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71256;
CC Evidence={ECO:0000305|PubMed:8327470};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.17 mM for phosphate {ECO:0000269|PubMed:8327470};
CC pH dependence:
CC Optimum pH is 8.0. {ECO:0000269|PubMed:8327470};
CC -!- SUBUNIT: Interacts via its C-terminal region with PDZK2 (By
CC similarity). Interacts with SLC9A3R1 (PubMed:22506049).
CC {ECO:0000250|UniProtKB:Q60825, ECO:0000269|PubMed:22506049}.
CC -!- SUBCELLULAR LOCATION: Apical cell membrane
CC {ECO:0000269|PubMed:26047794}; Multi-pass membrane protein
CC {ECO:0000255}. Cell membrane {ECO:0000269|PubMed:20335586}; Multi-pass
CC membrane protein {ECO:0000255}. Note=Localized at the brush border
CC membranes of the proximal tubules. {ECO:0000250|UniProtKB:Q06496}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q06495-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q06495-2; Sequence=VSP_042311;
CC -!- TISSUE SPECIFICITY: Kidney and lung. {ECO:0000269|PubMed:8327470}.
CC -!- DISEASE: Nephrolithiasis/osteoporosis, hypophosphatemic, 1 (NPHLOP1)
CC [MIM:612286]: A disease characterized by decreased renal phosphate
CC absorption, renal phosphate wasting, hypophosphatemia,
CC hyperphosphaturia, hypercalciuria, nephrolithiasis and osteoporosis.
CC {ECO:0000269|PubMed:12324554}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Fanconi renotubular syndrome 2 (FRTS2) [MIM:613388]: A form of
CC Fanconi renotubular syndrome, a disease due to a generalized
CC dysfunction of the proximal kidney tubule resulting in decreased solute
CC and water reabsorption. Patients have polydipsia and polyuria with
CC phosphaturia, glycosuria and aminoaciduria. They may develop
CC hypophosphatemic rickets or osteomalacia, acidosis and a tendency
CC toward dehydration. Some eventually develop renal insufficiency. FRTS2
CC inheritance is autosomal recessive. {ECO:0000269|PubMed:20335586}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
CC -!- DISEASE: Hypercalcemia, infantile, 2 (HCINF2) [MIM:616963]: An
CC autosomal recessive form of hypercalcemia, a disorder characterized by
CC abnormally high level of calcium in the blood, failure to thrive,
CC vomiting, dehydration, and nephrocalcinosis.
CC {ECO:0000269|PubMed:26047794}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the SLC34A transporter family. {ECO:0000305}.
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DR EMBL; L13258; AAA36354.1; -; mRNA.
DR EMBL; AK298299; BAG60555.1; -; mRNA.
DR EMBL; AC145098; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS4418.1; -. [Q06495-1]
DR CCDS; CCDS54953.1; -. [Q06495-2]
DR PIR; B48189; B48189.
DR RefSeq; NP_001161051.1; NM_001167579.1. [Q06495-2]
DR RefSeq; NP_003043.3; NM_003052.4. [Q06495-1]
DR AlphaFoldDB; Q06495; -.
DR BioGRID; 112457; 4.
DR CORUM; Q06495; -.
DR IntAct; Q06495; 1.
DR STRING; 9606.ENSP00000321424; -.
DR BindingDB; Q06495; -.
DR ChEMBL; CHEMBL3769299; -.
DR DrugBank; DB11348; Calcium Phosphate.
DR DrugBank; DB14481; Calcium phosphate dihydrate.
DR DrugBank; DB14502; Sodium phosphate, dibasic.
DR DrugBank; DB09449; Sodium phosphate, monobasic.
DR DrugBank; DB14503; Sodium phosphate, monobasic, unspecified form.
DR TCDB; 2.A.58.1.5; the phosphate:na(+) symporter (pnas) family.
DR GlyGen; Q06495; 3 sites.
DR iPTMnet; Q06495; -.
DR PhosphoSitePlus; Q06495; -.
DR BioMuta; SLC34A1; -.
DR DMDM; 730113; -.
DR MassIVE; Q06495; -.
DR PaxDb; Q06495; -.
DR PeptideAtlas; Q06495; -.
DR PRIDE; Q06495; -.
DR ProteomicsDB; 58454; -. [Q06495-1]
DR ProteomicsDB; 58455; -. [Q06495-2]
DR Antibodypedia; 46041; 158 antibodies from 20 providers.
DR DNASU; 6569; -.
DR Ensembl; ENST00000324417.6; ENSP00000321424.4; ENSG00000131183.11. [Q06495-1]
DR Ensembl; ENST00000512593.5; ENSP00000423022.1; ENSG00000131183.11. [Q06495-2]
DR GeneID; 6569; -.
DR KEGG; hsa:6569; -.
DR MANE-Select; ENST00000324417.6; ENSP00000321424.4; NM_003052.5; NP_003043.3.
DR UCSC; uc003mgk.5; human. [Q06495-1]
DR CTD; 6569; -.
DR DisGeNET; 6569; -.
DR GeneCards; SLC34A1; -.
DR HGNC; HGNC:11019; SLC34A1.
DR HPA; ENSG00000131183; Tissue enriched (kidney).
DR MalaCards; SLC34A1; -.
DR MIM; 182309; gene.
DR MIM; 612286; phenotype.
DR MIM; 613388; phenotype.
DR MIM; 616963; phenotype.
DR neXtProt; NX_Q06495; -.
DR OpenTargets; ENSG00000131183; -.
DR Orphanet; 300547; Autosomal recessive infantile hypercalcemia.
DR Orphanet; 244305; Dominant hypophosphatemia with nephrolithiasis or osteoporosis.
DR Orphanet; 157215; Hereditary hypophosphatemic rickets with hypercalciuria.
DR Orphanet; 3337; Primary Fanconi renotubular syndrome.
DR PharmGKB; PA35887; -.
DR VEuPathDB; HostDB:ENSG00000131183; -.
DR eggNOG; ENOG502QQ3I; Eukaryota.
DR GeneTree; ENSGT00950000183177; -.
DR HOGENOM; CLU_816244_0_0_1; -.
DR InParanoid; Q06495; -.
DR OMA; TWDFLPA; -.
DR PhylomeDB; Q06495; -.
DR TreeFam; TF313981; -.
DR PathwayCommons; Q06495; -.
DR Reactome; R-HSA-427589; Type II Na+/Pi cotransporters.
DR Reactome; R-HSA-5619040; Defective SLC34A1 causes hypophosphatemic nephrolithiasis/osteoporosis 1 (NPHLOP1).
DR Reactome; R-HSA-5683826; Surfactant metabolism.
DR SignaLink; Q06495; -.
DR BioGRID-ORCS; 6569; 9 hits in 1060 CRISPR screens.
DR ChiTaRS; SLC34A1; human.
DR GeneWiki; Sodium/phosphate_cotransporter; -.
DR GenomeRNAi; 6569; -.
DR Pharos; Q06495; Tchem.
DR PRO; PR:Q06495; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q06495; protein.
DR Bgee; ENSG00000131183; Expressed in nephron tubule and 42 other tissues.
DR ExpressionAtlas; Q06495; baseline and differential.
DR Genevisible; Q06495; HS.
DR GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
DR GO; GO:0005903; C:brush border; IBA:GO_Central.
DR GO; GO:0031526; C:brush border membrane; ISS:UniProtKB.
DR GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005768; C:endosome; IEA:Ensembl.
DR GO; GO:0005887; C:integral component of plasma membrane; NAS:UniProtKB.
DR GO; GO:0045121; C:membrane raft; IEA:Ensembl.
DR GO; GO:0072686; C:mitotic spindle; IDA:HPA.
DR GO; GO:0016607; C:nuclear speck; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0031982; C:vesicle; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0030165; F:PDZ domain binding; IEA:Ensembl.
DR GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl.
DR GO; GO:0005436; F:sodium:phosphate symporter activity; IDA:UniProtKB.
DR GO; GO:1901684; P:arsenate ion transmembrane transport; IEA:Ensembl.
DR GO; GO:0030643; P:cellular phosphate ion homeostasis; IBA:GO_Central.
DR GO; GO:0071248; P:cellular response to metal ion; IEA:Ensembl.
DR GO; GO:0071374; P:cellular response to parathyroid hormone stimulus; IEA:Ensembl.
DR GO; GO:0016036; P:cellular response to phosphate starvation; IEA:Ensembl.
DR GO; GO:0072734; P:cellular response to staurosporine; IEA:Ensembl.
DR GO; GO:0097187; P:dentinogenesis; IEA:Ensembl.
DR GO; GO:1901128; P:gentamycin metabolic process; IEA:Ensembl.
DR GO; GO:0009100; P:glycoprotein metabolic process; IEA:Ensembl.
DR GO; GO:0042431; P:indole metabolic process; IEA:Ensembl.
DR GO; GO:0001822; P:kidney development; IEA:Ensembl.
DR GO; GO:0001503; P:ossification; IEA:Ensembl.
DR GO; GO:0055062; P:phosphate ion homeostasis; IDA:UniProtKB.
DR GO; GO:0035435; P:phosphate ion transmembrane transport; IEA:Ensembl.
DR GO; GO:0006817; P:phosphate ion transport; IDA:UniProtKB.
DR GO; GO:0045838; P:positive regulation of membrane potential; IEA:Ensembl.
DR GO; GO:2000187; P:positive regulation of phosphate transmembrane transport; IEA:Ensembl.
DR GO; GO:2000120; P:positive regulation of sodium-dependent phosphate transport; IEA:Ensembl.
DR GO; GO:0046686; P:response to cadmium ion; IDA:UniProtKB.
DR GO; GO:0032355; P:response to estradiol; IEA:Ensembl.
DR GO; GO:0060416; P:response to growth hormone; IEA:Ensembl.
DR GO; GO:0010288; P:response to lead ion; IDA:UniProtKB.
DR GO; GO:0032026; P:response to magnesium ion; IEA:Ensembl.
DR GO; GO:0046689; P:response to mercury ion; IDA:UniProtKB.
DR GO; GO:0035864; P:response to potassium ion; IEA:Ensembl.
DR GO; GO:0097066; P:response to thyroid hormone; IEA:Ensembl.
DR GO; GO:0033189; P:response to vitamin A; IEA:Ensembl.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl.
DR GO; GO:0098719; P:sodium ion import across plasma membrane; IEA:Ensembl.
DR GO; GO:0044341; P:sodium-dependent phosphate transport; IBA:GO_Central.
DR GO; GO:0072350; P:tricarboxylic acid metabolic process; IEA:Ensembl.
DR InterPro; IPR003841; Na/Pi_transpt.
DR InterPro; IPR029848; Na/Pi_transpt_2A.
DR PANTHER; PTHR10010; PTHR10010; 1.
DR PANTHER; PTHR10010:SF21; PTHR10010:SF21; 1.
DR Pfam; PF02690; Na_Pi_cotrans; 2.
DR TIGRFAMs; TIGR01013; 2a58; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Disease variant; Disulfide bond;
KW Glycoprotein; Ion transport; Membrane; Phosphoprotein; Reference proteome;
KW Sodium; Sodium transport; Symport; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..639
FT /note="Sodium-dependent phosphate transport protein 2A"
FT /id="PRO_0000068607"
FT TOPO_DOM 1..103
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q06496"
FT TRANSMEM 104..125
FT /note="Helical; Name=M1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 126..145
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q06496"
FT TRANSMEM 146..163
FT /note="Helical; Name=M2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 164..165
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q06496"
FT TRANSMEM 166..185
FT /note="Helical; Name=M3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 186..347
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q06496"
FT TRANSMEM 348..370
FT /note="Helical; Name=M4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 371..412
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q06496"
FT TRANSMEM 413..436
FT /note="Helical; Name=M5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 437..466
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q06496"
FT TRANSMEM 467..487
FT /note="Helical; Name=M6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 488..513
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q06496"
FT TRANSMEM 514..534
FT /note="Helical; Name=M7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 535..539
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q06496"
FT TRANSMEM 540..561
FT /note="Helical; Name=M8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 562..639
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q06496"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q06496"
FT MOD_RES 34
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q60825"
FT MOD_RES 508
FT /note="Phosphothreonine; by PKC"
FT /evidence="ECO:0000255"
FT MOD_RES 607
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q06496"
FT MOD_RES 623
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q60825"
FT MOD_RES 625
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q60825"
FT CARBOHYD 298
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 323
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 330
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 225..522
FT /evidence="ECO:0000250|UniProtKB:Q06496"
FT DISULFID 306..336
FT /evidence="ECO:0000250|UniProtKB:Q06496"
FT VAR_SEQ 313..639
FT /note="APTSMSRAEANSSQTLGNATMEKCNHIFVDTGLPDLAVGLILLAGSLVLLCT
FT CLILLVKMLNSLLKGQVAKVIQKVINTDFPAPFTWVTGYFAMVVGASMTFVVQSSSVFT
FT SAITPLIGLGVISIERAYPLTLGSNIGTTTTAILAALASPREKLSSAFQIALCHFFFNI
FT SGILLWYPVPCTRLPIRMAKALGKRTAKYRWFAVLYLLVCFLLLPSLVFGISMAGWQVM
FT VGVGTPFGALLAFVVLINVLQSRSPGHLPKWLQTWDFLPRWMHSLKPLDHLITRATLCC
FT ARPEPRSPPLPPRVFLEELPPATPSPRLALPAHHNATRL -> QNLEGREITHFDLRKK
FT QAMEDSSVPHCP (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_042311"
FT VARIANT 48
FT /note="A -> F (in NPHLOP1; causes hypophosphatemic
FT urolithiasis; requires 2 nucleotide substitutions; results
FT in lower phosphate current, decreases affinity for
FT phosphate and decreases phosphate uptake compared to wild-
FT type; shows a dominant-negative effect; dbSNP:rs121918610)"
FT /evidence="ECO:0000269|PubMed:12324554"
FT /id="VAR_024765"
FT VARIANT 91..97
FT /note="Missing (in HCINF2; no change in phosphate transport
FT activity; changed localization to the apical plasma
FT membrane; partial retention inside the cell)"
FT /evidence="ECO:0000269|PubMed:26047794"
FT /id="VAR_077913"
FT VARIANT 147
FT /note="V -> M (in NPHLOP1; causes hypophosphatemic
FT osteoporosis; results in lower phosphate current, decreases
FT affinity for phosphate and decreases phosphate uptake
FT compared to wild-type; shows a dominant-negative effect;
FT dbSNP:rs121918611)"
FT /evidence="ECO:0000269|PubMed:12324554"
FT /id="VAR_024766"
FT VARIANT 153
FT /note="G -> A (in HCINF2; loss of phosphate transport
FT activity; loss of localization to apical plasma membrane;
FT display a complete intracellular retention and no
FT detectable actin colocalization; dbSNP:rs769409705)"
FT /evidence="ECO:0000269|PubMed:26047794"
FT /id="VAR_077914"
FT VARIANT 153
FT /note="G -> V (in HCINF2; loss of phosphate transport
FT activity; loss of localization to apical plasma membrane;
FT display a complete intracellular retention and no
FT detectable actin colocalization; dbSNP:rs769409705)"
FT /evidence="ECO:0000269|PubMed:26047794"
FT /id="VAR_077915"
FT VARIANT 155
FT /note="L -> P (in HCINF2; loss of phosphate transport
FT activity; loss of localization to apical plasma membrane;
FT display a complete intracellular retention and no
FT detectable actin colocalization; dbSNP:rs369770760)"
FT /evidence="ECO:0000269|PubMed:26047794"
FT /id="VAR_077916"
FT VARIANT 160
FT /note="V -> VILVTVLV (in FRTS2; loss of function in the
FT homozygous state; loss of localization to cell membrane)"
FT /evidence="ECO:0000269|PubMed:20335586"
FT /id="VAR_063812"
FT VARIANT 215
FT /note="R -> W (in HCINF2; dbSNP:rs577273266)"
FT /evidence="ECO:0000269|PubMed:26047794"
FT /id="VAR_077917"
FT VARIANT 336
FT /note="C -> G (in HCINF2; loss of phosphate transport
FT activity; loss of localization to apical plasma membrane;
FT display a complete intracellular retention and no
FT detectable actin colocalization; dbSNP:rs876661338)"
FT /evidence="ECO:0000269|PubMed:26047794"
FT /id="VAR_077918"
FT VARIANT 408
FT /note="V -> E (in HCINF2; loss of phosphate transport
FT activity; loss of localization to apical plasma membrane; a
FT complete intracellular retention and no detectable actin
FT colocalization; dbSNP:rs140649226)"
FT /evidence="ECO:0000269|PubMed:26047794"
FT /id="VAR_077919"
FT VARIANT 488
FT /note="W -> R (in HCINF2; loss of phosphate transport
FT activity; loss of localization to apical plasma membrane;
FT display a complete intracellular retention and no
FT detectable actin colocalization)"
FT /evidence="ECO:0000269|PubMed:26047794"
FT /id="VAR_077920"
SQ SEQUENCE 639 AA; 68937 MW; 65D21D968C35D61B CRC64;
MLSYGERLGS PAVSPLPVRG GHVMRGTAFA YVPSPQVLHR IPGTSAYAFP SLGPVALAEH
TCPCGEVLER HEPLPAKLAL EEEQKPESRL VPKLRQAGAM LLKVPLMLTF LYLFVCSLDM
LSSAFQLAGG KVAGDIFKDN AILSNPVAGL VVGILVTVLV QSSSTSTSII VSMVSSGLLE
VSSAIPIIMG SNIGTSVTNT IVALMQAGDR TDFRRAFAGA TVHDCFNWLS VLVLLPLEAA
TGYLHHITRL VVASFNIHGG RDAPDLLKII TEPFTKLIIQ LDESVITSIA TGDESLRNHS
LIQIWCHPDS LQAPTSMSRA EANSSQTLGN ATMEKCNHIF VDTGLPDLAV GLILLAGSLV
LLCTCLILLV KMLNSLLKGQ VAKVIQKVIN TDFPAPFTWV TGYFAMVVGA SMTFVVQSSS
VFTSAITPLI GLGVISIERA YPLTLGSNIG TTTTAILAAL ASPREKLSSA FQIALCHFFF
NISGILLWYP VPCTRLPIRM AKALGKRTAK YRWFAVLYLL VCFLLLPSLV FGISMAGWQV
MVGVGTPFGA LLAFVVLINV LQSRSPGHLP KWLQTWDFLP RWMHSLKPLD HLITRATLCC
ARPEPRSPPL PPRVFLEELP PATPSPRLAL PAHHNATRL
