ID   NPT2B_MOUSE             Reviewed;         697 AA.
AC   Q9DBP0; Q9Z290;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   02-SEP-2026, entry version 151.
DE   RecName: Full=Sodium-dependent phosphate transport protein 2B;
DE            Short=Sodium-phosphate transport protein 2B;
DE   AltName: Full=Na(+)-dependent phosphate cotransporter 2B;
DE   AltName: Full=Sodium/phosphate cotransporter 2B;
DE            Short=Na(+)/Pi cotransporter 2B;
DE            Short=NaPi-2b;
DE   AltName: Full=Solute carrier family 34 member 2;
GN   Name=Slc34a2; Synonyms=Npt2b;
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, TRANSPORTER ACTIVITY,
RP   BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, AND SUBCELLULAR
RP   LOCATION.
RC   STRAIN=NMRI; TISSUE=Small intestine;
RX   PubMed=9826740; DOI=10.1073/pnas.95.24.14564;
RA   Hilfiker H., Hattenhauer O., Traebert M., Forster I.C., Murer H., Biber J.;
RT   "Characterization of a murine type II sodium-phosphate cotransporter
RT   expressed in mammalian small intestine.";
RL   Proc. Natl. Acad. Sci. U.S.A. 95:14564-14569(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Lung;
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 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   [4]
RP   INDUCTION, TISSUE SPECIFICITY, FUNCTION, TRANSPORTER ACTIVITY, AND
RP   SUBCELLULAR LOCATION.
RC   STRAIN=NMRI;
RX   PubMed=15701623; DOI=10.1152/ajpgi.00167.2004;
RA   Radanovic T., Wagner C.A., Murer H., Biber J.;
RT   "Regulation of intestinal phosphate transport. I. Segmental expression and
RT   adaptation to low-P(i) diet of the type IIb Na(+)-P(i) cotransporter in
RT   mouse small intestine.";
RL   Am. J. Physiol. 288:G496-G500(2005).
RN   [5]
RP   INDUCTION, FUNCTION, TRANSPORTER ACTIVITY, SUBCELLULAR LOCATION, AND TISSUE
RP   SPECIFICITY.
RX   PubMed=15701624; DOI=10.1152/ajpgi.00168.2004;
RA   Stauber A., Radanovic T., Stange G., Murer H., Wagner C.A., Biber J.;
RT   "Regulation of intestinal phosphate transport. II. Metabolic acidosis
RT   stimulates Na(+)-dependent phosphate absorption and expression of the
RT   Na(+)-P(i) cotransporter NaPi-IIb in small intestine.";
RL   Am. J. Physiol. 288:G501-G506(2005).
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Lung;
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: Involved in actively transporting phosphate into cells via
CC       Na(+) cotransport. {ECO:0000269|PubMed:15701623,
CC       ECO:0000269|PubMed:15701624, ECO:0000269|PubMed:9826740}.
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:15701623, ECO:0000269|PubMed:15701624,
CC         ECO:0000269|PubMed:9826740};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71256;
CC         Evidence={ECO:0000305|PubMed:9826740};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=50 mM for phosphate {ECO:0000269|PubMed:9826740};
CC         KM=33 mM for sodium {ECO:0000269|PubMed:9826740};
CC       pH dependence:
CC         Optimum pH is 6.0. {ECO:0000269|PubMed:9826740};
CC   -!- SUBCELLULAR LOCATION: Apical cell membrane
CC       {ECO:0000269|PubMed:15701623, ECO:0000269|PubMed:15701624,
CC       ECO:0000269|PubMed:9826740}; Multi-pass membrane protein {ECO:0000255}.
CC       Note=Localized at the brush border membranes of enterocytes.
CC       {ECO:0000269|PubMed:15701623, ECO:0000269|PubMed:15701624,
CC       ECO:0000269|PubMed:9826740}.
CC   -!- TISSUE SPECIFICITY: Highly abundant in the ileum of small intestine,
CC       whereas it is almost absent in the duodenum and in the jejunum.
CC       {ECO:0000269|PubMed:15701623, ECO:0000269|PubMed:15701624,
CC       ECO:0000269|PubMed:9826740}.
CC   -!- INDUCTION: Up-regulated in the entire small intestine by low-phosphate
CC       diet. Up-regulated by metabolic acidosis. {ECO:0000269|PubMed:15701623,
CC       ECO:0000269|PubMed:15701624}.
CC   -!- SIMILARITY: Belongs to the SLC34A transporter family. {ECO:0000305}.
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DR   EMBL; AF081499; AAC80007.1; -; mRNA.
DR   EMBL; AK004832; BAB23600.1; -; mRNA.
DR   EMBL; AK145599; BAE26533.1; -; mRNA.
DR   EMBL; BC096369; AAH96369.1; -; mRNA.
DR   CCDS; CCDS19291.1; -.
DR   RefSeq; NP_035532.2; NM_011402.3.
DR   AlphaFoldDB; Q9DBP0; -.
DR   SMR; Q9DBP0; -.
DR   BioGRID; 203310; 2.
DR   FunCoup; Q9DBP0; 41.
DR   STRING; 10090.ENSMUSP00000092380; -.
DR   GlyCosmos; Q9DBP0; 4 sites, No reported glycans.
DR   GlyGen; Q9DBP0; 4 sites.
DR   iPTMnet; Q9DBP0; -.
DR   PhosphoSitePlus; Q9DBP0; -.
DR   SwissPalm; Q9DBP0; -.
DR   jPOST; Q9DBP0; -.
DR   PaxDb; 10090-ENSMUSP00000092380; -.
DR   ProteomicsDB; 293957; -.
DR   Antibodypedia; 51936; 174 antibodies from 29 providers.
DR   DNASU; 20531; -.
DR   Ensembl; ENSMUST00000094787.8; ENSMUSP00000092380.5; ENSMUSG00000029188.15.
DR   GeneID; 20531; -.
DR   KEGG; mmu:20531; -.
DR   UCSC; uc008xla.2; mouse.
DR   AGR; MGI:1342284; -.
DR   CTD; 10568; -.
DR   MGI; MGI:1342284; Slc34a2.
DR   VEuPathDB; HostDB:ENSMUSG00000029188; -.
DR   eggNOG; ENOG502QQ3I; Eukaryota.
DR   GeneTree; ENSGT00950000183177; -.
DR   HOGENOM; CLU_025063_0_0_1; -.
DR   InParanoid; Q9DBP0; -.
DR   OMA; GCPKCCR; -.
DR   OrthoDB; 76259at2759; -.
DR   PhylomeDB; Q9DBP0; -.
DR   Reactome; R-MMU-427589; Type II Na+/Pi cotransporters.
DR   Reactome; R-MMU-5683826; Surfactant metabolism.
DR   BioGRID-ORCS; 20531; 0 hits in 81 CRISPR screens.
DR   PRO; PR:Q9DBP0; -.
DR   Proteomes; UP000000589; Chromosome 5.
DR   RNAct; Q9DBP0; protein.
DR   Bgee; ENSMUSG00000029188; Expressed in left lung and 83 other cell types or tissues.
DR   ExpressionAtlas; Q9DBP0; baseline and differential.
DR   GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
DR   GO; GO:0005903; C:brush border; IDA:MGI.
DR   GO; GO:0031526; C:brush border membrane; ISO:GO_Central.
DR   GO; GO:0005829; C:cytosol; ISO:GO_Central.
DR   GO; GO:0016020; C:membrane; ISO:GO_Central.
DR   GO; GO:0031528; C:microvillus membrane; ISO:GO_Central.
DR   GO; GO:0005654; C:nucleoplasm; ISO:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; ISO:GO_Central.
DR   GO; GO:0031982; C:vesicle; IBA:GO_Central.
DR   GO; GO:0042301; F:phosphate ion binding; ISO:GO_Central.
DR   GO; GO:0019904; F:protein domain specific binding; ISO:GO_Central.
DR   GO; GO:0031402; F:sodium ion binding; ISO:GO_Central.
DR   GO; GO:0005436; F:sodium:phosphate symporter activity; IDA:UniProtKB.
DR   GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR   GO; GO:0030643; P:intracellular phosphate ion homeostasis; ISO:GO_Central.
DR   GO; GO:0006817; P:phosphate ion transport; IDA:MGI.
DR   GO; GO:0043627; P:response to estrogen; IEA:Ensembl.
DR   GO; GO:0044341; P:sodium-dependent phosphate transport; ISO:GO_Central.
DR   InterPro; IPR003841; Na/Pi_transpt.
DR   NCBIfam; TIGR01013; 2a58; 1.
DR   NCBIfam; NF037997; Na_Pi_symport; 1.
DR   PANTHER; PTHR10010:SF23; SODIUM-DEPENDENT PHOSPHATE TRANSPORT PROTEIN 2B; 1.
DR   PANTHER; PTHR10010; SOLUTE CARRIER FAMILY 34 SODIUM PHOSPHATE , MEMBER 2-RELATED; 1.
DR   Pfam; PF02690; Na_Pi_cotrans; 2.
PE   1: Evidence at protein level;
KW   Cell membrane; Disulfide bond; Glycoprotein; Ion transport; Membrane;
KW   Reference proteome; Sodium; Sodium transport; Symport; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..697
FT                   /note="Sodium-dependent phosphate transport protein 2B"
FT                   /id="PRO_0000068614"
FT   TOPO_DOM        1..91
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        92..112
FT                   /note="Helical; Name=M1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        113..136
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        137..157
FT                   /note="Helical; Name=M2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        158..213
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        214..234
FT                   /note="Helical; Name=M3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        235..363
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        364..384
FT                   /note="Helical; Name=M4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        385..408
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        409..429
FT                   /note="Helical; Name=M5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        430..486
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        487..507
FT                   /note="Helical; Name=M6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        508..526
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        527..547
FT                   /note="Helical; Name=M7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        548..551
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        552..572
FT                   /note="Helical; Name=M8"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        573..696
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          1..45
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        295
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        308
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        321
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        356
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        303..350
FT                   /evidence="ECO:0000250|UniProtKB:Q06496"
FT   CONFLICT        81
FT                   /note="K -> R (in Ref. 1; AAC80007)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        155
FT                   /note="V -> L (in Ref. 1; AAC80007)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        622
FT                   /note="Missing (in Ref. 1)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   697 AA;  76245 MW;  2A7B9384857EF16F CRC64;
     MAPWPELENA QPNPGKFIEG ASGPQSSIPA KDKEASKTND NGTPVAKTEL LPSYSALVLI
     EEHPEGTDPW DLPELQDTGI KWSERDTKGK TLCIFQGVGK FILLLGFLYL FVCSLDVLSS
     AFQLVGGKVA GQFFSNNSIM SNPVAGLVIG VLVTVMVQSS STSSSIIVSM VASSLLTVRA
     AIPIIMGANI GTSITNTIVA LMQAGDRNEF RRAFAGATVH DFFNWLSVFV LLPLEAATHY
     LEILTNLVLE TFKFQNGEDA PDILKVITDP FTKLIIQLDK KVIQQIAMGD SAAQNKSLIK
     IWCKSITNVT EMNVTVPSTD NCTSPSYCWT DGIQTWTIQN VTQKENIAKC QHIFVNFSLP
     DLAVGIILLT VSLVVLCGCL IMIVKLLGSV LRGQVATVIK KTLNTDFPFP FAWLTGYLAI
     LVGAGMTFIV QSSSVFTSAM TPLIGIGVIS IERAYPLTLG SNIGTTTTAI LAALASPGNT
     LRSSLQIALC HFFFNISGIL LWYPIPFTRL PIRLAKGLGN ISAKYRWFAV FYLIFFFFVT
     PLTVFGLSLA GWPVLVGVGV PIILLLLLVL CLRMLQFRCP RILPLKLRDW NFLPLWMHSL
     KPWDNVISLA TTCFQRRCCC CCRVCCRVCC MVCGCKCCRC SKCCRDQGEE EEEKEQDIPV
     KASGAFDNAA MSKECQDEGK GQVEVLSMKA LSNTTVF
//