S20A2_HUMAN
ID S20A2_HUMAN Reviewed; 652 AA.
AC Q08357;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Sodium-dependent phosphate transporter 2;
DE AltName: Full=Gibbon ape leukemia virus receptor 2;
DE Short=GLVR-2;
DE AltName: Full=Phosphate transporter 2;
DE Short=PiT-2;
DE Short=Pit2;
DE Short=hPit2;
DE AltName: Full=Solute carrier family 20 member 2;
GN Name=SLC20A2; Synonyms=GLVR2, PIT2;
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], AND FUNCTION AS RETROVIRAL RECEPTOR.
RC TISSUE=Placenta;
RX PubMed=8302848; DOI=10.1073/pnas.91.3.1168;
RA van Zeijl M., Johann S.V., Closs E., Cunningham J., Eddy R., Shows T.B.,
RA O'Hara B.;
RT "A human amphotropic retrovirus receptor is a second member of the gibbon
RT ape leukemia virus receptor family.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:1168-1172(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP TOPOLOGY, GLYCOSYLATION AT ASN-81, AND MUTAGENESIS OF ASN-81.
RX PubMed=11356966; DOI=10.1128/jvi.75.12.5584-5592.2001;
RA Salauen C., Rodrigues P., Heard J.M.;
RT "Transmembrane topology of PiT-2, a phosphate transporter-retrovirus
RT receptor.";
RL J. Virol. 75:5584-5592(2001).
RN [5]
RP TOPOLOGY, SUBCELLULAR LOCATION, AND INDUCTION.
RX PubMed=9151850; DOI=10.1128/jvi.71.6.4564-4570.1997;
RA Chien M.L., Foster J.L., Douglas J.L., Garcia J.V.;
RT "The amphotropic murine leukemia virus receptor gene encodes a 71-
RT kilodalton protein that is induced by phosphate depletion.";
RL J. Virol. 71:4564-4570(1997).
RN [6]
RP FUNCTION AS RETROVIRAL RECEPTOR.
RX PubMed=11435563; DOI=10.1128/jvi.75.15.6841-6849.2001;
RA Sugai J., Eiden M., Anderson M.M., Van Hoeven N., Meiering C.D.,
RA Overbaugh J.;
RT "Identification of envelope determinants of feline leukemia virus subgroup
RT B that permit infection and gene transfer to cells expressing human Pit1 or
RT Pit2.";
RL J. Virol. 75:6841-6849(2001).
RN [7]
RP FUNCTION AS SODIUM-PHOSPHATE SYMPORTER, SUBUNIT, AND MUTAGENESIS OF GLU-55
RP AND GLU-575.
RX PubMed=12205090; DOI=10.1074/jbc.m207096200;
RA Boettger P., Pedersen L.;
RT "Two highly conserved glutamate residues critical for type III sodium-
RT dependent phosphate transport revealed by uncoupling transport function
RT from retroviral receptor function.";
RL J. Biol. Chem. 277:42741-42747(2002).
RN [8]
RP FUNCTION AS SODIUM-PHOSPHATE SYMPORTER, SUBUNIT, MUTAGENESIS OF ASP-506,
RP AND CHARACTERIZATION OF VARIANT IBGC1 ASN-28.
RX PubMed=15955065; DOI=10.1111/j.1742-4658.2005.04720.x;
RA Boettger P., Pedersen L.;
RT "Evolutionary and experimental analyses of inorganic phosphate transporter
RT PiT family reveals two related signature sequences harboring highly
RT conserved aspartic acids critical for sodium-dependent phosphate transport
RT function of human PiT2.";
RL FEBS J. 272:3060-3074(2005).
RN [9]
RP FUNCTION AS SODIUM-PHOSPHATE SYMPORTER, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP MUTAGENESIS OF GLU-55; GLU-91 AND GLU-575.
RX PubMed=16790504; DOI=10.1152/ajpcell.00015.2006;
RA Boettger P., Hede S.E., Grunnet M., Hoyer B., Klaerke D.A., Pedersen L.;
RT "Characterization of transport mechanisms and determinants critical for
RT Na+-dependent Pi symport of the PiT family paralogs human PiT1 and PiT2.";
RL Am. J. Physiol. 291:C1377-C1387(2006).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-268, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-256; SER-259; SER-268;
RP SER-316 AND SER-385, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-259 AND SER-316, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [14]
RP VARIANTS IBGC1 VAL-42 DEL; ARG-498; LYS-575; MET-595; TRP-601 AND LEU-601,
RP AND CHARACTERIZATION OF VARIANTS IBGC1 VAL-42 DEL; ARG-498; LYS-575;
RP MET-595; TRP-601 AND LEU-601.
RX PubMed=22327515; DOI=10.1038/ng.1077;
RA Wang C., Li Y., Shi L., Ren J., Patti M., Wang T., de Oliveira J.R.,
RA Sobrido M.J., Quintans B., Baquero M., Cui X., Zhang X.Y., Wang L., Xu H.,
RA Wang J., Yao J., Dai X., Liu J., Zhang L., Ma H., Gao Y., Ma X., Feng S.,
RA Liu M., Wang Q.K., Forster I.C., Zhang X., Liu J.Y.;
RT "Mutations in SLC20A2 link familial idiopathic basal ganglia calcification
RT with phosphate homeostasis.";
RL Nat. Genet. 44:254-256(2012).
RN [15]
RP INVOLVEMENT IN IBGC1.
RX PubMed=23406454; DOI=10.1111/ene.12044;
RA Lemos R.R., Oliveira M.F., Oliveira J.R.;
RT "Reporting a new mutation at the SLC20A2 gene in familial idiopathic basal
RT ganglia calcification.";
RL Eur. J. Neurol. 20:E43-43(2013).
RN [16]
RP VARIANTS IBGC1 LEU-11; ASN-28 AND PRO-62.
RX PubMed=23939468; DOI=10.1016/j.gene.2013.07.071;
RA Chen W.J., Yao X.P., Zhang Q.J., Ni W., He J., Li H.F., Liu X.Y.,
RA Zhao G.X., Murong S.X., Wang N., Wu Z.Y.;
RT "Novel SLC20A2 mutations identified in southern Chinese patients with
RT idiopathic basal ganglia calcification.";
RL Gene 529:159-162(2013).
RN [17]
RP VARIANTS IBGC1 GLN-382; GLN-502; LEU-568 AND LEU-601.
RX PubMed=23334463; DOI=10.1007/s10048-012-0349-2;
RA Hsu S.C., Sears R.L., Lemos R.R., Quintans B., Huang A., Spiteri E.,
RA Nevarez L., Mamah C., Zatz M., Pierce K.D., Fullerton J.M., Adair J.C.,
RA Berner J.E., Bower M., Brodaty H., Carmona O., Dobricic V., Fogel B.L.,
RA Garcia-Estevez D., Goldman J., Goudreau J.L., Hopfer S., Jankovic M.,
RA Jauma S., Jen J.C., Kirdlarp S., Klepper J., Kostic V., Lang A.E.,
RA Linglart A., Maisenbacher M.K., Manyam B.V., Mazzoni P., Miedzybrodzka Z.,
RA Mitarnun W., Mitchell P.B., Mueller J., Novakovic I., Paucar M.,
RA Paulson H., Simpson S.A., Svenningsson P., Tuite P., Vitek J.,
RA Wetchaphanphesat S., Williams C., Yang M., Schofield P.R.,
RA de Oliveira J.R., Sobrido M.J., Geschwind D.H., Coppola G.;
RT "Mutations in SLC20A2 are a major cause of familial idiopathic basal
RT ganglia calcification.";
RL Neurogenetics 14:11-22(2013).
RN [18]
RP VARIANTS IBGC1 ASN-28; LEU-184; SER-194 AND SER-571.
RX PubMed=24065723; DOI=10.1093/brain/awt255;
RG French IBGC Study Group;
RA Nicolas G., Pottier C., Charbonnier C., Guyant-Marechal L., Le Ber I.,
RA Pariente J., Labauge P., Ayrignac X., Defebvre L., Maltete D.,
RA Martinaud O., Lefaucheur R., Guillin O., Wallon D., Chaumette B.,
RA Rondepierre P., Derache N., Fromager G., Schaeffer S., Krystkowiak P.,
RA Verny C., Jurici S., Sauvee M., Verin M., Lebouvier T., Rouaud O.,
RA Thauvin-Robinet C., Rousseau S., Rovelet-Lecrux A., Frebourg T.,
RA Campion D., Hannequin D.;
RT "Phenotypic spectrum of probable and genetically-confirmed idiopathic basal
RT ganglia calcification.";
RL Brain 136:3395-3407(2013).
RN [19]
RP VARIANTS IBGC1 TRP-434 AND MET-595.
RX PubMed=25284758; DOI=10.1002/mds.26053;
RA Taglia I., Mignarri A., Olgiati S., Menci E., Petrocelli P.L.,
RA Breedveld G.J., Scaglione C., Martinelli P., Federico A., Bonifati V.,
RA Dotti M.T.;
RT "Primary familial brain calcification: Genetic analysis and clinical
RT spectrum.";
RL Mov. Disord. 29:1691-1695(2014).
RN [20]
RP VARIANTS IBGC1 VAL-51; HIS-71; MET-115 AND ARG-637.
RX PubMed=24463626; DOI=10.1212/wnl.0000000000000143;
RA Yamada M., Tanaka M., Takagi M., Kobayashi S., Taguchi Y., Takashima S.,
RA Tanaka K., Touge T., Hatsuta H., Murayama S., Hayashi Y., Kaneko M.,
RA Ishiura H., Mitsui J., Atsuta N., Sobue G., Shimozawa N., Inuzuka T.,
RA Tsuji S., Hozumi I.;
RT "Evaluation of SLC20A2 mutations that cause idiopathic basal ganglia
RT calcification in Japan.";
RL Neurology 82:705-712(2014).
CC -!- FUNCTION: Sodium-phosphate symporter which seems to play a fundamental
CC housekeeping role in phosphate transport by absorbing phosphate from
CC interstitial fluid for normal cellular functions such as cellular
CC metabolism, signal transduction, and nucleic acid and lipid synthesis.
CC In vitro, sodium-dependent phosphate uptake is not significantly
CC affected by acidic and alkaline conditions, however sodium-independent
CC phosphate uptake occurs at acidic conditions. May play a role in
CC extracellular matrix, cartilage and vascular calcification. Functions
CC as a retroviral receptor and confers human cells susceptibility to
CC infection to amphotropic murine leukemia virus (A-MuLV), 10A1 murine
CC leukemia virus (10A1 MLV) and some feline leukemia virus subgroup B
CC (FeLV-B) variants. {ECO:0000269|PubMed:11435563,
CC ECO:0000269|PubMed:12205090, ECO:0000269|PubMed:15955065,
CC ECO:0000269|PubMed:16790504, ECO:0000269|PubMed:8302848}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:12205090,
CC ECO:0000269|PubMed:15955065}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:9151850};
CC Multi-pass membrane protein {ECO:0000269|PubMed:9151850}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC -!- INDUCTION: Increased by phosphate depletion in osteosarcoma cell lines.
CC {ECO:0000269|PubMed:9151850}.
CC -!- DISEASE: Basal ganglia calcification, idiopathic, 1 (IBGC1)
CC [MIM:213600]: A form of basal ganglia calcification, an autosomal
CC dominant condition characterized by symmetric calcification in the
CC basal ganglia and other brain regions. Affected individuals can either
CC be asymptomatic or show a wide spectrum of neuropsychiatric symptoms,
CC including parkinsonism, dystonia, tremor, ataxia, dementia, psychosis,
CC seizures, and chronic headache. Serum levels of calcium, phosphate,
CC alkaline phosphatase and parathyroid hormone are normal. The
CC neuropathological hallmark of the disease is vascular and pericapillary
CC calcification, mainly of calcium phosphate, in the affected brain
CC areas. {ECO:0000269|PubMed:15955065, ECO:0000269|PubMed:22327515,
CC ECO:0000269|PubMed:23334463, ECO:0000269|PubMed:23406454,
CC ECO:0000269|PubMed:23939468, ECO:0000269|PubMed:24065723,
CC ECO:0000269|PubMed:24463626, ECO:0000269|PubMed:25284758}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the inorganic phosphate transporter (PiT) (TC
CC 2.A.20) family. {ECO:0000305}.
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DR EMBL; L20852; AAA18018.1; -; mRNA.
DR EMBL; AK291202; BAF83891.1; -; mRNA.
DR EMBL; BC028600; AAH28600.1; -; mRNA.
DR CCDS; CCDS6132.1; -.
DR PIR; A37000; A37000.
DR RefSeq; NP_001244109.1; NM_001257180.1.
DR RefSeq; NP_001244110.1; NM_001257181.1.
DR RefSeq; NP_006740.1; NM_006749.4.
DR RefSeq; XP_005273670.1; XM_005273613.3.
DR RefSeq; XP_016869237.1; XM_017013748.1.
DR AlphaFoldDB; Q08357; -.
DR SMR; Q08357; -.
DR BioGRID; 112463; 71.
DR IntAct; Q08357; 16.
DR MINT; Q08357; -.
DR STRING; 9606.ENSP00000340465; -.
DR BindingDB; Q08357; -.
DR ChEMBL; CHEMBL4295806; -.
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.20.2.3; the inorganic phosphate transporter (pit) family.
DR GlyGen; Q08357; 1 site.
DR iPTMnet; Q08357; -.
DR PhosphoSitePlus; Q08357; -.
DR BioMuta; SLC20A2; -.
DR DMDM; 74735615; -.
DR EPD; Q08357; -.
DR jPOST; Q08357; -.
DR MassIVE; Q08357; -.
DR MaxQB; Q08357; -.
DR PaxDb; Q08357; -.
DR PeptideAtlas; Q08357; -.
DR PRIDE; Q08357; -.
DR ProteomicsDB; 58600; -.
DR Antibodypedia; 11470; 159 antibodies from 28 providers.
DR DNASU; 6575; -.
DR Ensembl; ENST00000342228.7; ENSP00000340465.3; ENSG00000168575.10.
DR Ensembl; ENST00000520179.5; ENSP00000429712.1; ENSG00000168575.10.
DR Ensembl; ENST00000520262.6; ENSP00000429754.1; ENSG00000168575.10.
DR GeneID; 6575; -.
DR KEGG; hsa:6575; -.
DR MANE-Select; ENST00000520262.6; ENSP00000429754.1; NM_001257180.2; NP_001244109.1.
DR UCSC; uc003xpe.5; human.
DR CTD; 6575; -.
DR DisGeNET; 6575; -.
DR GeneCards; SLC20A2; -.
DR GeneReviews; SLC20A2; -.
DR HGNC; HGNC:10947; SLC20A2.
DR HPA; ENSG00000168575; Tissue enhanced (skeletal).
DR MalaCards; SLC20A2; -.
DR MIM; 158378; gene.
DR MIM; 213600; phenotype.
DR neXtProt; NX_Q08357; -.
DR OpenTargets; ENSG00000168575; -.
DR Orphanet; 1980; Bilateral striopallidodentate calcinosis.
DR PharmGKB; PA35834; -.
DR VEuPathDB; HostDB:ENSG00000168575; -.
DR eggNOG; KOG2493; Eukaryota.
DR GeneTree; ENSGT00390000014879; -.
DR HOGENOM; CLU_015355_3_1_1; -.
DR InParanoid; Q08357; -.
DR OMA; IVYDNRV; -.
DR OrthoDB; 712010at2759; -.
DR PhylomeDB; Q08357; -.
DR TreeFam; TF314426; -.
DR BioCyc; MetaCyc:ENSG00000168575-MON; -.
DR PathwayCommons; Q08357; -.
DR Reactome; R-HSA-427652; Sodium-coupled phosphate cotransporters.
DR Reactome; R-HSA-5619111; Defective SLC20A2 causes idiopathic basal ganglia calcification 1 (IBGC1).
DR SignaLink; Q08357; -.
DR BioGRID-ORCS; 6575; 10 hits in 1076 CRISPR screens.
DR ChiTaRS; SLC20A2; human.
DR GeneWiki; SLC20A2; -.
DR GenomeRNAi; 6575; -.
DR Pharos; Q08357; Tbio.
DR PRO; PR:Q08357; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; Q08357; protein.
DR Bgee; ENSG00000168575; Expressed in left lobe of thyroid gland and 196 other tissues.
DR ExpressionAtlas; Q08357; baseline and differential.
DR Genevisible; Q08357; HS.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR GO; GO:0016020; C:membrane; TAS:ProtInc.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0005315; F:inorganic phosphate transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0038023; F:signaling receptor activity; TAS:ProtInc.
DR GO; GO:0005436; F:sodium:phosphate symporter activity; TAS:Reactome.
DR GO; GO:0001618; F:virus receptor activity; IEA:UniProtKB-KW.
DR GO; GO:0006811; P:ion transport; TAS:Reactome.
DR GO; GO:0035435; P:phosphate ion transmembrane transport; IBA:GO_Central.
DR InterPro; IPR001204; Phos_transporter.
DR PANTHER; PTHR11101; PTHR11101; 1.
DR Pfam; PF01384; PHO4; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Disease variant; Glycoprotein;
KW Host cell receptor for virus entry; Host-virus interaction; Ion transport;
KW Membrane; Phosphate transport; Phosphoprotein; Receptor;
KW Reference proteome; Sodium; Sodium transport; Symport; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..652
FT /note="Sodium-dependent phosphate transporter 2"
FT /id="PRO_0000341268"
FT TOPO_DOM 1..5
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 6..26
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 27..46
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 47..67
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 68..86
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 87..107
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 108..109
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 110..130
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 131..142
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 143..163
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 164..190
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 191..211
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 212..213
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 214..234
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 235..482
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 483..503
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 504..530
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 531..551
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 552..571
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 572..586
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 587..593
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 594..609
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 610..621
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 622..642
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 643..652
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REGION 273..307
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 458..477
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 290..304
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 253
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q63488"
FT MOD_RES 256
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 259
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 268
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 316
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 385
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CARBOHYD 81
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:11356966"
FT VARIANT 11
FT /note="I -> L (in IBGC1; dbSNP:rs201836672)"
FT /evidence="ECO:0000269|PubMed:23939468"
FT /id="VAR_072255"
FT VARIANT 28
FT /note="D -> N (in IBGC1; Impairs phosphate transport; no
FT effect on retroviral receptor function;
FT dbSNP:rs1554561099)"
FT /evidence="ECO:0000269|PubMed:15955065,
FT ECO:0000269|PubMed:23939468, ECO:0000269|PubMed:24065723"
FT /id="VAR_072256"
FT VARIANT 42
FT /note="Missing (in IBGC1; substantially impaired phosphate
FT transport)"
FT /evidence="ECO:0000269|PubMed:22327515"
FT /id="VAR_067545"
FT VARIANT 51
FT /note="A -> V (in IBGC1)"
FT /evidence="ECO:0000269|PubMed:24463626"
FT /id="VAR_072257"
FT VARIANT 62
FT /note="L -> P (in IBGC1)"
FT /evidence="ECO:0000269|PubMed:23939468"
FT /id="VAR_072258"
FT VARIANT 71
FT /note="R -> H (in IBGC1)"
FT /evidence="ECO:0000269|PubMed:24463626"
FT /id="VAR_072259"
FT VARIANT 115
FT /note="T -> M (in IBGC1; dbSNP:rs775911275)"
FT /evidence="ECO:0000269|PubMed:24463626"
FT /id="VAR_072260"
FT VARIANT 184
FT /note="P -> L (in IBGC1; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:24065723"
FT /id="VAR_075396"
FT VARIANT 194
FT /note="N -> S (in IBGC1; unknown pathological significance;
FT dbSNP:rs748252183)"
FT /evidence="ECO:0000269|PubMed:24065723"
FT /id="VAR_075397"
FT VARIANT 382
FT /note="R -> Q (in IBGC1; dbSNP:rs200010919)"
FT /evidence="ECO:0000269|PubMed:23334463"
FT /id="VAR_072261"
FT VARIANT 434
FT /note="S -> W (in IBGC1; dbSNP:rs1357615935)"
FT /evidence="ECO:0000269|PubMed:25284758"
FT /id="VAR_072262"
FT VARIANT 498
FT /note="G -> R (in IBGC1; substantially impaired phosphate
FT transport)"
FT /evidence="ECO:0000269|PubMed:22327515"
FT /id="VAR_067546"
FT VARIANT 502
FT /note="H -> Q (in IBGC1)"
FT /evidence="ECO:0000269|PubMed:23334463"
FT /id="VAR_072263"
FT VARIANT 568
FT /note="P -> L (in IBGC1; dbSNP:rs763252801)"
FT /evidence="ECO:0000269|PubMed:23334463"
FT /id="VAR_072264"
FT VARIANT 571
FT /note="G -> S (in IBGC1; dbSNP:rs1388992742)"
FT /evidence="ECO:0000269|PubMed:24065723"
FT /id="VAR_075398"
FT VARIANT 575
FT /note="E -> K (in IBGC1; substantially impaired phosphate
FT transport; dbSNP:rs387906653)"
FT /evidence="ECO:0000269|PubMed:22327515"
FT /id="VAR_067547"
FT VARIANT 595
FT /note="T -> M (in IBGC1; substantially impaired phosphate
FT transport; dbSNP:rs387906654)"
FT /evidence="ECO:0000269|PubMed:22327515,
FT ECO:0000269|PubMed:25284758"
FT /id="VAR_067548"
FT VARIANT 601
FT /note="S -> L (in IBGC1; substantially impaired phosphate
FT transport; dbSNP:rs387906652)"
FT /evidence="ECO:0000269|PubMed:22327515,
FT ECO:0000269|PubMed:23334463"
FT /id="VAR_067549"
FT VARIANT 601
FT /note="S -> W (in IBGC1; substantially impaired phosphate
FT transport; dbSNP:rs387906652)"
FT /evidence="ECO:0000269|PubMed:22327515"
FT /id="VAR_067550"
FT VARIANT 637
FT /note="S -> R (in IBGC1)"
FT /evidence="ECO:0000269|PubMed:24463626"
FT /id="VAR_072265"
FT MUTAGEN 55
FT /note="E->D,K: Abolishes sodium-dependent phosphate
FT transport; no effect on retroviral receptor function."
FT /evidence="ECO:0000269|PubMed:12205090,
FT ECO:0000269|PubMed:16790504"
FT MUTAGEN 55
FT /note="E->Q: Abolishes phosphate but not sodium uptake;
FT when associated with Q-91 and Q-575."
FT /evidence="ECO:0000269|PubMed:12205090,
FT ECO:0000269|PubMed:16790504"
FT MUTAGEN 81
FT /note="N->V: Abolishes N-glycosylation."
FT /evidence="ECO:0000269|PubMed:11356966"
FT MUTAGEN 91
FT /note="E->Q: Abolishes phosphate but not sodium uptake;
FT when associated with Q-55 and Q-575."
FT /evidence="ECO:0000269|PubMed:16790504"
FT MUTAGEN 506
FT /note="D->N: Impairs phosphate transport; no effect on
FT retroviral receptor function."
FT /evidence="ECO:0000269|PubMed:15955065"
FT MUTAGEN 575
FT /note="E->D,K: Abolishes sodium-dependent phosphate
FT transport; no effect on retroviral receptor function."
FT /evidence="ECO:0000269|PubMed:12205090,
FT ECO:0000269|PubMed:16790504"
FT MUTAGEN 575
FT /note="E->Q: Abolishes phosphate but not sodium uptake;
FT when associated with Q-55 and Q-91."
FT /evidence="ECO:0000269|PubMed:12205090,
FT ECO:0000269|PubMed:16790504"
SQ SEQUENCE 652 AA; 70392 MW; A0A870C7927DE39C CRC64;
MAMDEYLWMV ILGFIIAFIL AFSVGANDVA NSFGTAVGSG VVTLRQACIL ASIFETTGSV
LLGAKVGETI RKGIIDVNLY NETVETLMAG EVSAMVGSAV WQLIASFLRL PISGTHCIVG
STIGFSLVAI GTKGVQWMEL VKIVASWFIS PLLSGFMSGL LFVLIRIFIL KKEDPVPNGL
RALPVFYAAT IAINVFSIMY TGAPVLGLVL PMWAIALISF GVALLFAFFV WLFVCPWMRR
KITGKLQKEG ALSRVSDESL SKVQEAESPV FKELPGAKAN DDSTIPLTGA AGETLGTSEG
TSAGSHPRAA YGRALSMTHG SVKSPISNGT FGFDGHTRSD GHVYHTVHKD SGLYKDLLHK
IHIDRGPEEK PAQESNYRLL RRNNSYTCYT AAICGLPVHA TFRAADSSAP EDSEKLVGDT
VSYSKKRLRY DSYSSYCNAV AEAEIEAEEG GVEMKLASEL ADPDQPREDP AEEEKEEKDA
PEVHLLFHFL QVLTACFGSF AHGGNDVSNA IGPLVALWLI YKQGGVTQEA ATPVWLLFYG
GVGICTGLWV WGRRVIQTMG KDLTPITPSS GFTIELASAF TVVIASNIGL PVSTTHCKVG
SVVAVGWIRS RKAVDWRLFR NIFVAWFVTV PVAGLFSAAV MALLMYGILP YV
