NPT2B_BOVIN
ID NPT2B_BOVIN Reviewed; 693 AA.
AC Q27960;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 93.
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;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TRANSPORTER ACTIVITY.
RC TISSUE=Kidney epithelium;
RX PubMed=7737195; DOI=10.1111/j.1432-1033.1995.tb20341.x;
RA Helps C.R., Murer H., McGiven J.D.;
RT "Cloning, sequence analysis and expression of the cDNA encoding a sodium-
RT dependent phosphate transporter from the bovine renal epithelial cell line
RT NBL-1.";
RL Eur. J. Biochem. 228:927-930(1995).
RN [2]
RP FUNCTION, TRANSPORTER ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP GLYCOSYLATION.
RC TISSUE=Kidney epithelium;
RX PubMed=1915351; DOI=10.1111/j.1432-1033.1991.tb16247.x;
RA Helps C.R., McGivan J.;
RT "Adaptive regulation of Na(+)-dependent phosphate transport in the bovine
RT renal epithelial cell line NBL-1. Identification of the phosphate
RT transporter as a 55-kDa glycoprotein.";
RL Eur. J. Biochem. 200:797-803(1991).
CC -!- FUNCTION: Involved in actively transporting phosphate into cells via
CC Na(+) cotransport. {ECO:0000269|PubMed:1915351,
CC ECO:0000269|PubMed:7737195}.
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:1915351, ECO:0000269|PubMed:7737195};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71256;
CC Evidence={ECO:0000305|PubMed:7737195};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=17.1 uM for phosphate (in the presence of <50 uM inorganic
CC phosphate) {ECO:0000269|PubMed:1915351};
CC KM=36.3 uM for phosphate (in the presence of 10 mM inorganic
CC phosphate) {ECO:0000269|PubMed:1915351};
CC Vmax=2.11 nmol/min/mg enzyme for phosphate (in the presence of <50 uM
CC inorganic phosphate) {ECO:0000269|PubMed:1915351};
CC Vmax=0.98 nmol/min/mg enzyme for phosphate (in the presence of 10 mM
CC inorganic phosphate) {ECO:0000269|PubMed:1915351};
CC -!- SUBCELLULAR LOCATION: Apical cell membrane
CC {ECO:0000250|UniProtKB:Q9DBP0}; Multi-pass membrane protein
CC {ECO:0000255}. Note=Localized at the brush border membranes of
CC enterocytes. {ECO:0000250|UniProtKB:Q9DBP0}.
CC -!- PTM: Glycosylated. {ECO:0000269|PubMed:1915351}.
CC -!- SIMILARITY: Belongs to the SLC34A transporter family. {ECO:0000305}.
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DR EMBL; X81699; CAA57345.1; -; mRNA.
DR PIR; S68972; S49228.
DR RefSeq; NP_777086.1; NM_174661.2.
DR AlphaFoldDB; Q27960; -.
DR STRING; 9913.ENSBTAP00000002023; -.
DR PaxDb; Q27960; -.
DR PeptideAtlas; Q27960; -.
DR PRIDE; Q27960; -.
DR GeneID; 282484; -.
DR KEGG; bta:282484; -.
DR CTD; 10568; -.
DR eggNOG; ENOG502QQ3I; Eukaryota.
DR InParanoid; Q27960; -.
DR OrthoDB; 976094at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0016324; C:apical plasma membrane; IBA:GO_Central.
DR GO; GO:0005903; C:brush border; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; ISS:UniProtKB.
DR GO; GO:0031982; C:vesicle; IBA:GO_Central.
DR GO; GO:0042301; F:phosphate ion binding; ISS:UniProtKB.
DR GO; GO:0031402; F:sodium ion binding; ISS:UniProtKB.
DR GO; GO:0005436; F:sodium:phosphate symporter activity; IDA:UniProtKB.
DR GO; GO:0030643; P:cellular phosphate ion homeostasis; IBA:GO_Central.
DR GO; GO:0006817; P:phosphate ion transport; ISS:UniProtKB.
DR GO; GO:0044341; P:sodium-dependent phosphate transport; IBA:GO_Central.
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..693
FT /note="Sodium-dependent phosphate transport protein 2B"
FT /id="PRO_0000068612"
FT TOPO_DOM 1..89
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 90..110
FT /note="Helical; Name=M1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 111..135
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 136..156
FT /note="Helical; Name=M2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 157..212
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 213..233
FT /note="Helical; Name=M3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 234..361
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 362..382
FT /note="Helical; Name=M4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 383..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..485
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 486..506
FT /note="Helical; Name=M6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 507..525
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 526..546
FT /note="Helical; Name=M7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 547..550
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 551..571
FT /note="Helical; Name=M8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 572..693
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..43
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 307
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 320
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 302..349
FT /evidence="ECO:0000250|UniProtKB:Q06496"
SQ SEQUENCE 693 AA; 75826 MW; 6E1CC17FE5C13213 CRC64;
MAPWPELENS QPTSEKYTVK ADGEQSAKPE KAKETEKDDT GTPITKIELV PSHSTATLIE
EPTEVEDPWD LPELKDTGLK WSERDTKGKI LCVFQGIGKF ILLLVFLYFF VCSLDVLSSA
FQLVGGKVAG KFFNNNSIMS NPLAGMVIGV LVTVLVQSSS TSTSIVVSMV ASSLLPVHAA
IPIIMGANIG TSITNTIVAL MQAGDRKEFR RAFAGATVHD FFNWLSVLVL LPLEAATGYL
ERLTNLVVES FHFKNGEEAP ELLKVITDPF TKLIIQLDKS ILNQIAMNDE SVQNKSMIKI
WCKTFTNVTE RNVTVPSPEN CTSPSLCWTD GLYTWTIKNV TYKENIAKCQ HIFVNFNLSD
AIVGTILLIT SLLILCTCLI LIVKLLGSVL RGQVAAVIKK TINTDFPYPF SWVTGYLAIL
VGAGMTFIVQ SSSVFTSAMT PLIGIGVISI QRAYPLTLGA NIGTTTTAIL AALASPGSTL
KSSLQIALCH FFFNISGIIL WYPIPFTRLP IRLAKGLGNI SSKYRWFAIV YLIVFFLLIP
LAVFGLSLIG WPVLVGVASP IVLVILLVVV LKILQSFCPG SLPQKLRSWD FLPFWMRSLE
PWDKLITSLT SCFQMRCCCC CRVCCRLCCG LCGCSKCCRC TKCSEDLEEG KDEPVKSPEA
FNNLAMDKEA QDGVTKSEVD ASGTKIVSSV TAL
