S20A1_MOUSE
ID S20A1_MOUSE Reviewed; 681 AA.
AC Q61609; A2AKR9; Q3U244; Q8CBJ1; Q91YQ9; Q9QVW6;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Sodium-dependent phosphate transporter 1;
DE AltName: Full=Gibbon ape leukemia virus receptor 1;
DE Short=GLVR-1;
DE AltName: Full=Leukemia virus receptor 1 homolog;
DE AltName: Full=Phosphate transporter 1;
DE Short=PiT-1;
DE AltName: Full=Solute carrier family 20 member 1;
GN Name=Slc20a1; Synonyms=Glvr1, Pit1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1531369; DOI=10.1128/jvi.66.3.1635-1640.1992;
RA Johann S.V., Gibbons J.J., O'Hara B.;
RT "GLVR1, a receptor for gibbon ape leukemia virus, is homologous to a
RT phosphate permease of Neurospora crassa and is expressed at high levels in
RT the brain and thymus.";
RL J. Virol. 66:1635-1640(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8046392; DOI=10.1099/0022-1317-75-8-1901;
RA Wilson C.A., Farrell K.B., Eiden M.V.;
RT "Comparison of cDNAs encoding the gibbon ape leukaemia virus receptor from
RT susceptible and non-susceptible murine cells.";
RL J. Gen. Virol. 75:1901-1908(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129/SvJ;
RX PubMed=10689185; DOI=10.1016/s0378-1119(00)00010-x;
RA Palmer G., Manen D., Bonjour J.-P., Caverzasio J.;
RT "Structure of the murine Pit1 phosphate transporter/retrovirus receptor
RT gene and functional characterization of its promoter region.";
RL Gene 244:35-45(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=NOD;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II; TISSUE=Mammary tumor;
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 [7]
RP FUNCTION (MICROBIAL INFECTION).
RX PubMed=1309898; DOI=10.1128/jvi.66.2.1219-1222.1992;
RA Takeuchi Y., Vile R.G., Simpson G., O'Hara B., Collins M.K., Weiss R.A.;
RT "Feline leukemia virus subgroup B uses the same cell surface receptor as
RT gibbon ape leukemia virus.";
RL J. Virol. 66:1219-1222(1992).
RN [8]
RP MUTAGENESIS OF 553-LYS--ALA-560; 553-LYS--GLU-555 AND LYS-553, AND REGION.
RX PubMed=8411375; DOI=10.1128/jvi.67.11.6733-6736.1993;
RA Johann S.V., van Zeijl M., Cekleniak J., O'Hara B.;
RT "Definition of a domain of GLVR1 which is necessary for infection by gibbon
RT ape leukemia virus and which is highly polymorphic between species.";
RL J. Virol. 67:6733-6736(1993).
RN [9]
RP FUNCTION, AND INDUCTION.
RX PubMed=9755124; DOI=10.1152/ajprenal.1998.275.4.f527;
RA Tenenhouse H.S., Roy S., Martel J., Gauthier C.;
RT "Differential expression, abundance, and regulation of Na+-phosphate
RT cotransporter genes in murine kidney.";
RL Am. J. Physiol. 275:F527-F534(1998).
RN [10]
RP FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=9916777; DOI=10.1016/s8756-3282(98)00151-3;
RA Palmer G., Zhao J., Bonjour J.-P., Hofstetter W., Caverzasio J.;
RT "In vivo expression of transcripts encoding the Glvr-1 phosphate
RT transporter/retrovirus receptor during bone development.";
RL Bone 24:1-7(1999).
RN [11]
RP FUNCTION (MICROBIAL INFECTION), AND REGION.
RX PubMed=12097582; DOI=10.1128/jvi.76.15.7683-7693.2002;
RA Farrell K.B., Russ J.L., Murthy R.K., Eiden M.V.;
RT "Reassessing the role of region A in Pit1-mediated viral entry.";
RL J. Virol. 76:7683-7693(2002).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-269 AND SER-273, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Sodium-phosphate symporter which plays a fundamental
CC housekeeping role in phosphate transport, such as absorbing phosphate
CC from interstitial fluid for normal cellular functions such as cellular
CC metabolism, signal transduction, and nucleic acid and lipid synthesis.
CC May play a role in extracellular matrix and cartilage calcification as
CC well as in vascular calcification. {ECO:0000269|PubMed:1531369,
CC ECO:0000269|PubMed:9755124, ECO:0000269|PubMed:9916777}.
CC -!- FUNCTION: (Microbial infection) May function as a retroviral receptor
CC but do not confer infection susceptibility to Gibbon Ape Leukemia Virus
CC (GaLV), Simian sarcoma-associated virus (SSAV) and Feline leukemia
CC virus subgroup B (FeLV-B). {ECO:0000269|PubMed:12097582,
CC ECO:0000269|PubMed:1309898}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC {ECO:0000269|PubMed:9916777}.
CC -!- DEVELOPMENTAL STAGE: Detected at 17 dpc of embryonic development in a
CC subpopulation of early hypertrophic chondrocytes in bone, but not when
CC fully differentiated. {ECO:0000269|PubMed:9916777}.
CC -!- INDUCTION: By growth hormone. {ECO:0000269|PubMed:9755124}.
CC -!- DOMAIN: Region A does not confer susceptibility to infection by Gibbon
CC Ape Leukemia Virus (GaLV) and Feline leukemia virus subgroup B (FeLV-
CC B). Substitution of Human SLC20A1 region A by region A of murine
CC SLC20A1 prevents viral infection.
CC -!- SIMILARITY: Belongs to the inorganic phosphate transporter (PiT) (TC
CC 2.A.20) family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC29234.1; Type=Miscellaneous discrepancy; Note=Intron retention. The sequence differs at the 3'end due to intron retention.; Evidence={ECO:0000305};
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DR EMBL; M73696; AAA74887.1; -; mRNA.
DR EMBL; AF172634; AAF45041.1; -; Genomic_DNA.
DR EMBL; AF172628; AAF45041.1; JOINED; Genomic_DNA.
DR EMBL; AF172629; AAF45041.1; JOINED; Genomic_DNA.
DR EMBL; AF172630; AAF45041.1; JOINED; Genomic_DNA.
DR EMBL; AF172631; AAF45041.1; JOINED; Genomic_DNA.
DR EMBL; AF172632; AAF45041.1; JOINED; Genomic_DNA.
DR EMBL; AF172633; AAF45041.1; JOINED; Genomic_DNA.
DR EMBL; AK035898; BAC29234.1; ALT_SEQ; mRNA.
DR EMBL; AK155506; BAE33298.1; -; mRNA.
DR EMBL; AL772347; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC015085; AAH15085.1; -; mRNA.
DR CCDS; CCDS16722.1; -.
DR PIR; S27868; S27868.
DR RefSeq; NP_001153065.1; NM_001159593.1.
DR RefSeq; NP_056562.1; NM_015747.2.
DR AlphaFoldDB; Q61609; -.
DR SMR; Q61609; -.
DR BioGRID; 203294; 4.
DR STRING; 10090.ENSMUSP00000028880; -.
DR iPTMnet; Q61609; -.
DR PhosphoSitePlus; Q61609; -.
DR EPD; Q61609; -.
DR MaxQB; Q61609; -.
DR PaxDb; Q61609; -.
DR PeptideAtlas; Q61609; -.
DR PRIDE; Q61609; -.
DR ProteomicsDB; 260882; -.
DR Antibodypedia; 33281; 178 antibodies from 28 providers.
DR DNASU; 20515; -.
DR Ensembl; ENSMUST00000028880; ENSMUSP00000028880; ENSMUSG00000027397.
DR Ensembl; ENSMUST00000110315; ENSMUSP00000105944; ENSMUSG00000027397.
DR GeneID; 20515; -.
DR KEGG; mmu:20515; -.
DR UCSC; uc008mhl.2; mouse.
DR CTD; 6574; -.
DR MGI; MGI:108392; Slc20a1.
DR VEuPathDB; HostDB:ENSMUSG00000027397; -.
DR eggNOG; KOG2493; Eukaryota.
DR GeneTree; ENSGT00390000014879; -.
DR HOGENOM; CLU_015355_3_1_1; -.
DR InParanoid; Q61609; -.
DR OMA; MQAFCIA; -.
DR OrthoDB; 712010at2759; -.
DR PhylomeDB; Q61609; -.
DR TreeFam; TF314426; -.
DR BRENDA; 7.3.2.1; 3474.
DR Reactome; R-MMU-427652; Sodium-coupled phosphate cotransporters.
DR BioGRID-ORCS; 20515; 6 hits in 75 CRISPR screens.
DR ChiTaRS; Slc20a1; mouse.
DR PRO; PR:Q61609; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q61609; protein.
DR Bgee; ENSMUSG00000027397; Expressed in pontine nuclear group and 268 other tissues.
DR ExpressionAtlas; Q61609; baseline and differential.
DR Genevisible; Q61609; MM.
DR GO; GO:0016021; C:integral component of membrane; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0005316; F:high-affinity inorganic phosphate:sodium symporter activity; ISO:MGI.
DR GO; GO:0005315; F:inorganic phosphate transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0031214; P:biomineral tissue development; IMP:MGI.
DR GO; GO:0035435; P:phosphate ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0006817; P:phosphate ion transport; ISO:MGI.
DR GO; GO:0006814; P:sodium ion transport; ISO:MGI.
DR InterPro; IPR001204; Phos_transporter.
DR PANTHER; PTHR11101; PTHR11101; 1.
DR Pfam; PF01384; PHO4; 1.
PE 1: Evidence at protein level;
KW Membrane; Phosphate transport; Phosphoprotein; Receptor;
KW Reference proteome; Symport; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..681
FT /note="Sodium-dependent phosphate transporter 1"
FT /id="PRO_0000080772"
FT TRANSMEM 25..45
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 66..86
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 106..126
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 162..182
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 201..221
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 234..254
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 514..534
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 561..581
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 602..622
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 652..672
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 266..295
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 553..560
FT /note="A"
FT MOD_RES 269
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 273
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MUTAGEN 553..560
FT /note="KQEASTKA->DTGDVSSKV: Confers virus infectibility."
FT /evidence="ECO:0000269|PubMed:8411375"
FT MUTAGEN 553..555
FT /note="KQE->DTGD: Confers virus infectibility."
FT /evidence="ECO:0000269|PubMed:8411375"
FT MUTAGEN 553
FT /note="K->DT: Confers virus infectibility."
FT /evidence="ECO:0000269|PubMed:8411375"
FT CONFLICT 190
FT /note="R -> H (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 368
FT /note="T -> A (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 446
FT /note="D -> E (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 490
FT /note="E -> G (in Ref. 6; AAH15085)"
FT /evidence="ECO:0000305"
FT CONFLICT 568
FT /note="L -> P (in Ref. 4; BAE33298)"
FT /evidence="ECO:0000305"
FT CONFLICT 569
FT /note="Y -> T (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 639
FT /note="R -> I (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 672
FT /note="A -> AA (in Ref. 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 681 AA; 74153 MW; F337B0982B5A297D CRC64;
MESTVATITS TLAAVTASAP PKYDNLWMLI LGFIIAFVLA FSVGANDVAN SFGTAVGSGV
VTLKQACILA SIFETVGSAL LGAKVSETIR NGLIDVELYN ETQDLLMAGS VSAMFGSAVW
QLVASFLKLP ISGTHCIVGA TIGFSLVANG QKGVKWSELI KIVMSWFVSP LLSGIMSGIL
FFLVRAFILR KADPVPNGLR ALPIFYACTI GINLFSIMYT GAPLLGFDKL PLWGTILISV
GCAVFCALIV WFFVCPRMKR KIEREVKSSP SESPLMEKKS NLKEDHEETK MAPGDVEHRN
PVSEVVCATG PLRAVVEERT VSFKLGDLEE APERERLPMD LKEETSIDST INGAVQLPNG
NLVQFSQTVS NQINSSGHYQ YHTVHKDSGL YKELLHKLHL AKVGDCMGDS GDKPLRRNNS
YTSYTMAICG MPLDSFRAKE GEQKGDEMET LTWPNADTKK RIRMDSYTSY CNAVSDLHSE
SEMDMSVKAE MGLGDRKGSS GSLEEWYDQD KPEVSLLFQF LQILTACFGS FAHGGNDVSN
AIGPLVALYL VYKQEASTKA ATPIWLLLYG GVGICMGLWV WGRRVIQTMG KDLTPITPSS
GFSIELASAL TVVIASNIGL PISTTHCKVG SVVSVGWLRS KKAVDWRLFR NIFMAWFVTV
PISGVISAAI MAVFKYIILP V
