NPT2B_RAT
ID NPT2B_RAT Reviewed; 695 AA.
AC Q9JJ09; Q8VI55;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 120.
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;
DE Short=rNaPi IIb;
GN Name=Slc34a2;
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], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=Wistar; TISSUE=Lung;
RX PubMed=10880371; DOI=10.1016/s0002-9440(10)64512-9;
RA Hashimoto M., Wang D.-Y., Kamo T., Zhu Y., Tsujiuchi T., Konishi Y.,
RA Tanaka M., Sugimura H.;
RT "Isolation and localization of type IIb Na/Pi cotransporter in the
RT developing rat lung.";
RL Am. J. Pathol. 157:21-27(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Brown Norway; TISSUE=Lung;
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 NUCLEOTIDE SEQUENCE [MRNA] OF 215-466.
RC TISSUE=Intestine;
RA Xu H., Bai L., Collins J.F., Ghishan F.K.;
RT "Molecular cloning and functional characterization of an intestinal sodium-
RT phosphate transporter gene promoter and its gene structure.";
RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION, TRANSPORTER ACTIVITY, SUBCELLULAR LOCATION, AND INDUCTION.
RC STRAIN=Sprague-Dawley;
RX PubMed=12893629; DOI=10.1152/ajpgi.00172.2003;
RA Xu H., Uno J.K., Inouye M., Xu L., Drees J.B., Collins J.F., Ghishan F.K.;
RT "Regulation of intestinal NaPi-IIb cotransporter gene expression by
RT estrogen.";
RL Am. J. Physiol. 285:G1317-G1324(2003).
RN [5]
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: Involved in actively transporting phosphate into cells via
CC Na(+) cotransport. {ECO:0000269|PubMed:12893629}.
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:12893629};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71256;
CC Evidence={ECO:0000305|PubMed:12893629};
CC -!- SUBCELLULAR LOCATION: Apical cell membrane
CC {ECO:0000269|PubMed:12893629}; Multi-pass membrane protein
CC {ECO:0000255}. Note=Localized at the brush border membranes of
CC enterocytes. {ECO:0000250|UniProtKB:Q9DBP0}.
CC -!- TISSUE SPECIFICITY: Highly expressed in the lung, in type II alveolar
CC cells. Moderately expressed in kidney followed by small intestine.
CC {ECO:0000269|PubMed:10880371}.
CC -!- DEVELOPMENTAL STAGE: Appears on embryonic day 16.5 and is expressed
CC thereafter. {ECO:0000269|PubMed:10880371}.
CC -!- INDUCTION: Up-regulated by estrogen. {ECO:0000269|PubMed:12893629}.
CC -!- SIMILARITY: Belongs to the SLC34A transporter family. {ECO:0000305}.
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DR EMBL; AF157026; AAF76291.1; -; mRNA.
DR EMBL; BC070898; AAH70898.1; -; mRNA.
DR EMBL; AF247725; AAL55704.1; -; mRNA.
DR RefSeq; NP_445832.1; NM_053380.2.
DR AlphaFoldDB; Q9JJ09; -.
DR STRING; 10116.ENSRNOP00000050889; -.
DR GlyGen; Q9JJ09; 5 sites.
DR iPTMnet; Q9JJ09; -.
DR PhosphoSitePlus; Q9JJ09; -.
DR PaxDb; Q9JJ09; -.
DR GeneID; 84395; -.
DR KEGG; rno:84395; -.
DR CTD; 10568; -.
DR RGD; 620889; Slc34a2.
DR eggNOG; ENOG502QQ3I; Eukaryota.
DR HOGENOM; CLU_025063_0_0_1; -.
DR InParanoid; Q9JJ09; -.
DR OrthoDB; 976094at2759; -.
DR PhylomeDB; Q9JJ09; -.
DR TreeFam; TF313981; -.
DR Reactome; R-RNO-427589; Type II Na+/Pi cotransporters.
DR Reactome; R-RNO-5683826; Surfactant metabolism.
DR PRO; PR:Q9JJ09; -.
DR Proteomes; UP000002494; Unplaced.
DR Genevisible; Q9JJ09; RN.
DR GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
DR GO; GO:0005903; C:brush border; ISO:RGD.
DR GO; GO:0031526; C:brush border membrane; IDA:RGD.
DR GO; GO:0016021; C:integral component of membrane; ISO:RGD.
DR GO; GO:0031528; C:microvillus membrane; IDA:RGD.
DR GO; GO:0031982; C:vesicle; IBA:GO_Central.
DR GO; GO:0042301; F:phosphate ion binding; ISO:RGD.
DR GO; GO:0019904; F:protein domain specific binding; IPI:RGD.
DR GO; GO:0031402; F:sodium ion binding; ISO:RGD.
DR GO; GO:0005436; F:sodium:phosphate symporter activity; IDA:UniProtKB.
DR GO; GO:0007568; P:aging; IEP:RGD.
DR GO; GO:0030643; P:cellular phosphate ion homeostasis; ISO:RGD.
DR GO; GO:0001701; P:in utero embryonic development; ISO:RGD.
DR GO; GO:0006817; P:phosphate ion transport; ISO:RGD.
DR GO; GO:0032355; P:response to estradiol; IEP:RGD.
DR GO; GO:0043627; P:response to estrogen; ISO:RGD.
DR GO; GO:0009750; P:response to fructose; IEP:RGD.
DR GO; GO:0044341; P:sodium-dependent phosphate transport; IMP:RGD.
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..695
FT /note="Sodium-dependent phosphate transport protein 2B"
FT /id="PRO_0000068616"
FT TOPO_DOM 1..90
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 91..111
FT /note="Helical; Name=M1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 112..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..695
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..43
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 295
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 313
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 340
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"
SQ SEQUENCE 695 AA; 75992 MW; 3FAFB827527E0061 CRC64;
MAPWPELENA HPNPNKFIEG ASGPQSSIPD KDKGTSKTND SGTPVAKIEL LPSYSALVLI
EEPPEGNDPW DLPELQDNGI KWSERDSKGK ILCIFQGIGK FILLLGFLYL FVCSLDVLSS
AFQLVGGKMA GQFFSNNSIM SNPVAGLVIG VLVTVMVQSS STSSSIIVSM VASSLLSVRA
AIPIIMGANI GTSITNTIVA LMQAGDRNEF RRAFAGATVH DFFNWLSVLV LLPLEAATHY
LEKLTNLVLE TFSFQNGEDA PDILKVITDP FTKLIIQLDK KVIQQIAMGD SEAQNKSLIK
IWCKTISNVI EENVTVPSPD NCTSPSYCWT DGIQTWTIQN VTEKENIAKC QHIFVNFSLP
DLAVGIILLT VSLLILCGCL IMIVKLLGSV LRGQVATVIK KTLNTDFPFP FAWLTGYLAI
LVGAGMTFIV QSSSVFTSAM TPLIGIGVIS IERAYPLTLG SNIGTTTTAI LAALASPGNT
LRSSLQIALC HFFFNISGIL LWYPIPFTRL PIRLAKGLGN ISAKYRWFAV FYLIFFFLLT
PLTVFGLSLA GWPVLVGVGV PIILLILLVL CLRMLQARCP RILPLKLRDW NFLPLWMHSL
KPWDNIISLA TSCFQRRCCC CCRVCCRVCC MVCGCKCCRC SKCCKNLEEE EKEQDVPVKA
SGGFDNTAMS KECQDEGKGQ VEVLGMKALS NTTVF
