ID   S20A2_RAT               Reviewed;         656 AA.
AC   Q63488;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   27-MAR-2024, entry version 134.
DE   RecName: Full=Sodium-dependent phosphate transporter 2;
DE   AltName: Full=Phosphate transporter 2;
DE            Short=PiT-2;
DE   AltName: Full=Receptor for amphotropic viruses 1;
DE            Short=RAM-1;
DE   AltName: Full=Solute carrier family 20 member 2;
GN   Name=Slc20a2; Synonyms=Pit2, Ram1;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=8278411; DOI=10.1073/pnas.91.1.78;
RA   Miller D.G., Edwards R.H., Miller A.D.;
RT   "Cloning of the cellular receptor for amphotropic murine retroviruses
RT   reveals homology to that for gibbon ape leukemia virus.";
RL   Proc. Natl. Acad. Sci. U.S.A. 91:78-82(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Heart;
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   [3]
RP   FUNCTION AS SODIUM-PHOSPHATE SYMPORTER, TISSUE SPECIFICITY, AND TRANSPORTER
RP   ACTIVITY.
RX   PubMed=8041748; DOI=10.1073/pnas.91.15.7071;
RA   Kavanaugh M.P., Miller D.G., Zhang W., Law W., Kozak S.L., Kabat D.,
RA   Miller A.D.;
RT   "Cell-surface receptors for gibbon ape leukemia virus and amphotropic
RT   murine retrovirus are inducible sodium-dependent phosphate symporters.";
RL   Proc. Natl. Acad. Sci. U.S.A. 91:7071-7075(1994).
RN   [4]
RP   FUNCTION, TRANSPORTER ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP   AND INDUCTION.
RX   PubMed=19073637; DOI=10.1152/ajprenal.90623.2008;
RA   Villa-Bellosta R., Ravera S., Sorribas V., Stange G., Levi M., Murer H.,
RA   Biber J., Forster I.C.;
RT   "The Na+-Pi cotransporter PiT-2 (SLC20A2) is expressed in the apical
RT   membrane of rat renal proximal tubules and regulated by dietary Pi.";
RL   Am. J. Physiol. 296:F691-F699(2009).
RN   [5]
RP   SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=20526720; DOI=10.1007/s00424-010-0841-1;
RA   Picard N., Capuano P., Stange G., Mihailova M., Kaissling B., Murer H.,
RA   Biber J., Wagner C.A.;
RT   "Acute parathyroid hormone differentially regulates renal brush border
RT   membrane phosphate cotransporters.";
RL   Pflugers Arch. 460:677-687(2010).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-253; SER-256 AND SER-259, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
CC   -!- FUNCTION: Sodium-phosphate symporter which preferentially transports
CC       the monovalent form of phosphate with a stoichiometry of two sodium
CC       ions per phosphate ion (PubMed:8041748, PubMed:19073637). Plays a
CC       critical role in the determination of bone quality and strength by
CC       providing phosphate for bone mineralization (By similarity). Required
CC       to maintain normal cerebrospinal fluid phosphate levels (By
CC       similarity). Mediates phosphate-induced calcification of vascular
CC       smooth muscle cells (VCMCs) and can functionally compensate for loss of
CC       SLC20A1 in VCMCs (By similarity). {ECO:0000250|UniProtKB:Q08357,
CC       ECO:0000269|PubMed:19073637, ECO:0000269|PubMed:8041748}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 Na(+)(out) + phosphate(out) = 2 Na(+)(in) + phosphate(in);
CC         Xref=Rhea:RHEA:71259, ChEBI:CHEBI:29101, ChEBI:CHEBI:43474;
CC         Evidence={ECO:0000269|PubMed:19073637, ECO:0000269|PubMed:8041748};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q08357}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20526720};
CC       Multi-pass membrane protein {ECO:0000255}. Apical cell membrane
CC       {ECO:0000269|PubMed:19073637}; Multi-pass membrane protein
CC       {ECO:0000255}. Note=Localized at the brush border membranes of the
CC       proximal tubules (PubMed:19073637, PubMed:20526720). Parathyroid
CC       hormone decreases its abundance in brush border membrane
CC       (PubMed:20526720). {ECO:0000269|PubMed:19073637,
CC       ECO:0000269|PubMed:20526720}.
CC   -!- TISSUE SPECIFICITY: Kidney (at protein level) (PubMed:20526720,
CC       PubMed:19073637). Widely expressed with highest levels in liver, heart
CC       and brain (PubMed:8041748). {ECO:0000269|PubMed:19073637,
CC       ECO:0000269|PubMed:20526720, ECO:0000269|PubMed:8041748}.
CC   -!- INDUCTION: Down-regulated by high phosphate diet.
CC       {ECO:0000269|PubMed:19073637}.
CC   -!- SIMILARITY: Belongs to the inorganic phosphate transporter (PiT)
CC       (TC 2.A.20) family. {ECO:0000305}.
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DR   EMBL; L19931; AAA16532.1; -; mRNA.
DR   EMBL; BC070908; AAH70908.1; -; mRNA.
DR   PIR; A49579; A49579.
DR   RefSeq; NP_058919.1; NM_017223.2.
DR   RefSeq; XP_008769573.1; XM_008771351.2.
DR   RefSeq; XP_008769574.1; XM_008771352.2.
DR   RefSeq; XP_017455543.1; XM_017600054.1.
DR   AlphaFoldDB; Q63488; -.
DR   SMR; Q63488; -.
DR   BioGRID; 248142; 1.
DR   STRING; 10116.ENSRNOP00000026418; -.
DR   GlyCosmos; Q63488; 1 site, No reported glycans.
DR   GlyGen; Q63488; 1 site.
DR   iPTMnet; Q63488; -.
DR   PhosphoSitePlus; Q63488; -.
DR   PaxDb; 10116-ENSRNOP00000026418; -.
DR   Ensembl; ENSRNOT00000026418.8; ENSRNOP00000026418.7; ENSRNOG00000019490.8.
DR   Ensembl; ENSRNOT00055012939; ENSRNOP00055010323; ENSRNOG00055007711.
DR   Ensembl; ENSRNOT00060048842; ENSRNOP00060040750; ENSRNOG00060028072.
DR   Ensembl; ENSRNOT00065014003; ENSRNOP00065010447; ENSRNOG00065008781.
DR   GeneID; 29502; -.
DR   KEGG; rno:29502; -.
DR   UCSC; RGD:3699; rat.
DR   AGR; RGD:3699; -.
DR   CTD; 6575; -.
DR   RGD; 3699; Slc20a2.
DR   eggNOG; KOG2493; Eukaryota.
DR   GeneTree; ENSGT00390000014879; -.
DR   HOGENOM; CLU_015355_3_1_1; -.
DR   InParanoid; Q63488; -.
DR   OMA; AWKTGNA; -.
DR   OrthoDB; 5488632at2759; -.
DR   PhylomeDB; Q63488; -.
DR   Reactome; R-RNO-427652; Sodium-coupled phosphate cotransporters.
DR   PRO; PR:Q63488; -.
DR   Proteomes; UP000002494; Chromosome 16.
DR   Bgee; ENSRNOG00000019490; Expressed in heart and 20 other cell types or tissues.
DR   ExpressionAtlas; Q63488; baseline and differential.
DR   GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
DR   GO; GO:0031526; C:brush border membrane; IDA:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR   GO; GO:0005315; F:inorganic phosphate transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:0005436; F:sodium:phosphate symporter activity; IDA:UniProtKB.
DR   GO; GO:0001618; F:virus receptor activity; ISO:RGD.
DR   GO; GO:0035435; P:phosphate ion transmembrane transport; IBA:GO_Central.
DR   GO; GO:0030501; P:positive regulation of bone mineralization; ISS:UniProtKB.
DR   InterPro; IPR001204; Phos_transporter.
DR   PANTHER; PTHR11101; PHOSPHATE TRANSPORTER; 1.
DR   PANTHER; PTHR11101:SF80; SODIUM-DEPENDENT PHOSPHATE TRANSPORTER 2; 1.
DR   Pfam; PF01384; PHO4; 1.
DR   Genevisible; Q63488; RN.
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_0000341270"
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..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..586
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        587..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:0000250"
FT   TRANSMEM        623..643
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        644..655
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         253
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         256
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         259
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         268
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q08357"
FT   MOD_RES         316
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q08357"
FT   MOD_RES         385
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q08357"
FT   CARBOHYD        81
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   656 AA;  70748 MW;  448AAB3EC5D64DC1 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 RKVQEAESPV FKELPGAKAS DDSAVPLTSL AGEAAGASEG
     TSAGNHPRAS YGRALSMTHG SAKSPISNGT FGFEGHMRND GHVYHTVHKD SGLYKDLLHK
     IHVDKGPEEK PAQENNYRLL RRNNSYTCYT AAICGMPVHA TFRASDTSSA PEDSEKLVGD
     TVSYSKKRLR YDSYSSYCNA VAEAEIEAEE GGVEMRLASE LTDPDQPHED PAEDEKEEKD
     SAEVHLLFHF LQVLTACFGS FAHGGNDVSN AIGPLVALWL IYKQGGVTQE AATPVWLLFY
     GGVGICTGLW VWGRRVIQTM GKDLTPITPS SGFTIELASA FTVVIASNIG LPVSTTHCKV
     GSVVAVGWIR SRKAVDWRLF RNIFIAWFVT VPVAGLFSAA IMALLMYICG FVSSSR
//