NPT2B_MOUSE
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 03-AUG-2022, entry version 134.
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 BioGRID; 203310; 2.
DR STRING; 10090.ENSMUSP00000092380; -.
DR GlyGen; Q9DBP0; 4 sites.
DR iPTMnet; Q9DBP0; -.
DR PhosphoSitePlus; Q9DBP0; -.
DR jPOST; Q9DBP0; -.
DR MaxQB; Q9DBP0; -.
DR PaxDb; Q9DBP0; -.
DR PRIDE; Q9DBP0; -.
DR ProteomicsDB; 293957; -.
DR Antibodypedia; 51936; 155 antibodies from 25 providers.
DR DNASU; 20531; -.
DR Ensembl; ENSMUST00000094787; ENSMUSP00000092380; ENSMUSG00000029188.
DR GeneID; 20531; -.
DR KEGG; mmu:20531; -.
DR UCSC; uc008xla.2; mouse.
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; 976094at2759; -.
DR PhylomeDB; Q9DBP0; -.
DR TreeFam; TF313981; -.
DR Reactome; R-MMU-427589; Type II Na+/Pi cotransporters.
DR Reactome; R-MMU-5683826; Surfactant metabolism.
DR BioGRID-ORCS; 20531; 0 hits in 76 CRISPR screens.
DR PRO; PR:Q9DBP0; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q9DBP0; protein.
DR Bgee; ENSMUSG00000029188; Expressed in left lung and 81 other tissues.
DR ExpressionAtlas; Q9DBP0; baseline and differential.
DR Genevisible; Q9DBP0; MM.
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:MGI.
DR GO; GO:0016021; C:integral component of membrane; ISO:MGI.
DR GO; GO:0031528; C:microvillus membrane; ISO:MGI.
DR GO; GO:0031982; C:vesicle; IBA:GO_Central.
DR GO; GO:0042301; F:phosphate ion binding; ISO:MGI.
DR GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
DR GO; GO:0031402; F:sodium ion binding; ISO:MGI.
DR GO; GO:0005436; F:sodium:phosphate symporter activity; IDA:UniProtKB.
DR GO; GO:0030643; P:cellular phosphate ion homeostasis; ISO:MGI.
DR GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
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:MGI.
DR InterPro; IPR003841; Na/Pi_transpt.
DR InterPro; IPR029852; Na/Pi_transpt_2B.
DR PANTHER; PTHR10010; PTHR10010; 1.
DR PANTHER; PTHR10010:SF23; PTHR10010:SF23; 1.
DR Pfam; PF02690; Na_Pi_cotrans; 2.
DR TIGRFAMs; TIGR01013; 2a58; 1.
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
