S20A2_MOUSE
ID S20A2_MOUSE Reviewed; 656 AA.
AC Q80UP8; E9QLQ8; Q3TBZ8; Q9ES96;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Sodium-dependent phosphate transporter 2;
DE AltName: Full=Phosphate transporter 2;
DE Short=PiT-2;
DE AltName: Full=Solute carrier family 20 member 2;
DE AltName: Full=Type III sodium-dependent phosphate transporter;
GN Name=Slc20a2; Synonyms=Pit2;
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], FUNCTION AS SODIUM-PHOSPHATE SYMPORTER, AND
RP TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J; TISSUE=Intestine;
RX PubMed=11003594; DOI=10.1152/ajpcell.2000.279.4.c1135;
RA Bai L., Collins J.F., Ghishan F.K.;
RT "Cloning and characterization of a type III Na-dependent phosphate
RT cotransporter from mouse intestine.";
RL Am. J. Physiol. 279:C1135-C1143(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=NOD; TISSUE=Spleen;
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; 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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-268, AND IDENTIFICATION BY
RP 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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-385, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Spleen, and
RC Testis;
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 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 (By similarity). {ECO:0000250,
CC ECO:0000269|PubMed:11003594}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Widely expressed including intestine, kidney,
CC heart, liver, brain, testis and skin. Expressed throughout the vertcal
CC crypt-axial axis of intestinal epithelium.
CC {ECO:0000269|PubMed:11003594}.
CC -!- SIMILARITY: Belongs to the inorganic phosphate transporter (PiT) (TC
CC 2.A.20) family. {ECO:0000305}.
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DR EMBL; AF196476; AAG28493.1; -; mRNA.
DR EMBL; AK157206; BAE33999.1; -; mRNA.
DR EMBL; AK170985; BAE42159.1; -; mRNA.
DR EMBL; AC140326; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC153017; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC046510; AAH46510.1; -; mRNA.
DR CCDS; CCDS22178.1; -.
DR RefSeq; NP_035524.2; NM_011394.3.
DR RefSeq; XP_006509106.1; XM_006509043.2.
DR RefSeq; XP_006509107.1; XM_006509044.1.
DR AlphaFoldDB; Q80UP8; -.
DR SMR; Q80UP8; -.
DR STRING; 10090.ENSMUSP00000065935; -.
DR GlyGen; Q80UP8; 1 site.
DR iPTMnet; Q80UP8; -.
DR PhosphoSitePlus; Q80UP8; -.
DR SwissPalm; Q80UP8; -.
DR MaxQB; Q80UP8; -.
DR PaxDb; Q80UP8; -.
DR PeptideAtlas; Q80UP8; -.
DR PRIDE; Q80UP8; -.
DR ProteomicsDB; 260752; -.
DR Antibodypedia; 11470; 159 antibodies from 28 providers.
DR DNASU; 20516; -.
DR Ensembl; ENSMUST00000067786; ENSMUSP00000065935; ENSMUSG00000037656.
DR GeneID; 20516; -.
DR KEGG; mmu:20516; -.
DR UCSC; uc009ldf.2; mouse.
DR CTD; 6575; -.
DR MGI; MGI:97851; Slc20a2.
DR VEuPathDB; HostDB:ENSMUSG00000037656; -.
DR eggNOG; KOG2493; Eukaryota.
DR GeneTree; ENSGT00390000014879; -.
DR HOGENOM; CLU_015355_3_1_1; -.
DR InParanoid; Q80UP8; -.
DR OMA; PIGWAMR; -.
DR OrthoDB; 712010at2759; -.
DR PhylomeDB; Q80UP8; -.
DR TreeFam; TF314426; -.
DR Reactome; R-MMU-427652; Sodium-coupled phosphate cotransporters.
DR BioGRID-ORCS; 20516; 4 hits in 72 CRISPR screens.
DR ChiTaRS; Slc20a2; mouse.
DR PRO; PR:Q80UP8; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q80UP8; protein.
DR Bgee; ENSMUSG00000037656; Expressed in molar tooth and 243 other tissues.
DR ExpressionAtlas; Q80UP8; baseline and differential.
DR Genevisible; Q80UP8; MM.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005315; F:inorganic phosphate transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015293; F:symporter activity; IEA:UniProtKB-KW.
DR GO; GO:0035435; P:phosphate ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0006814; P:sodium ion transport; IEA:UniProtKB-KW.
DR InterPro; IPR001204; Phos_transporter.
DR PANTHER; PTHR11101; PTHR11101; 1.
DR Pfam; PF01384; PHO4; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Glycoprotein; 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..656
FT /note="Sodium-dependent phosphate transporter 2"
FT /id="PRO_0000341269"
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 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..483
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 484..504
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 505..531
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 532..552
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 553..572
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 573..587
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 588..594
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 595..610
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 611..622
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 623..643
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 644..655
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REGION 257..283
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 459..478
FT /note="Disordered"
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:0000250|UniProtKB:Q08357"
FT MOD_RES 259
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q08357"
FT MOD_RES 268
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 316
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q08357"
FT MOD_RES 385
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CARBOHYD 81
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 53
FT /note="I -> V (in Ref. 1; AAG28493, 2; BAE42159/BAE33999
FT and 4; AAH46510)"
FT /evidence="ECO:0000305"
FT CONFLICT 55
FT /note="E -> A (in Ref. 1; AAG28493)"
FT /evidence="ECO:0000305"
FT CONFLICT 123
FT /note="I -> T (in Ref. 1; AAG28493)"
FT /evidence="ECO:0000305"
FT CONFLICT 387
FT /note="T -> A (in Ref. 1; AAG28493)"
FT /evidence="ECO:0000305"
FT CONFLICT 487
FT /note="L -> F (in Ref. 1; AAG28493)"
FT /evidence="ECO:0000305"
FT CONFLICT 614
FT /note="A -> T (in Ref. 2; BAE42159)"
FT /evidence="ECO:0000305"
FT CONFLICT 644..656
FT /note="LLMYICGLFSSSR -> SFMYGILPYV (in Ref. 1; AAG28493)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 656 AA; 70866 MW; 0E4678A705B878CB CRC64;
MAMDGYLWMV ILGFIIAFIL AFSVGANDVA NSFGTAVGSG VVTLRQACIL ASIFETTGSV
LLGAKVGETI RKGIIDVNLY NETVETLMAG EVSAMVGSAV WQLIASFLRL PISGTHCIVG
STIGFSLVAI GPKGVQWMEL VKIVASWFIS PLLSGFMSGV LFILIRMFIL TKEDPVPNGL
QALPLFYAAT IAINVFSIMY TGAPVLGLSL PIWAIALISF GVALLFAFFV WLFVCPWMKR
KIAGRLEKES ALSRASDESL RKVQEAESPG FKELPGAKPS DDSAVPLTSL AGEAVGASEG
TSAGNHPRAS YGRALSMTHG SAKSPISNGT FGFEGHMRND GHVYHTVHKD SGLYKDLLHK
IHVDRGSEEK PTQENNYRLL RRNNSYTCYT AAICGMPVHT TFRASDTSSA PEDSEKLVGD
SVSYSKKRLR YDSYSSYCNA VAEAEIEAEE GGVEMRLASE LADPDRPHED PTEEEKEEKD
SAEVHLLFHF LQVLTACFGS FAHGGNDVSN AIGPLVALWL IYQQGGVTQE AATPVWLLFY
GGVGICTGLW VWGRRVIQTM GKDLTPITPS SGFTIELASA FTVVIASNIG LPVSTTHCKV
GSVVAVGWIR SRKAVDWRLF RNIFVAWFVT VPVAGLFSAA IMALLMYICG LFSSSR
