NPT2C_RAT
ID NPT2C_RAT Reviewed; 601 AA.
AC Q8K4R8;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Sodium-dependent phosphate transport protein 2C;
DE Short=Sodium-phosphate transport protein 2C;
DE AltName: Full=Na(+)-dependent phosphate cotransporter 2C;
DE AltName: Full=Sodium/phosphate cotransporter 2C;
DE Short=Na(+)/Pi cotransporter 2C;
DE Short=NaPi-2c;
DE AltName: Full=Solute carrier family 34 member 3;
GN Name=Slc34a3;
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], DEVELOPMENTAL STAGE, TISSUE SPECIFICITY,
RP FUNCTION, TRANSPORTER ACTIVITY, AND SUBCELLULAR LOCATION.
RC STRAIN=Wistar; TISSUE=Kidney;
RX PubMed=11880379; DOI=10.1074/jbc.m200943200;
RA Segawa H., Kaneko I., Takahashi A., Kuwahata M., Ito M., Ohkido I.,
RA Tatsumi S., Miyamoto K.;
RT "Growth-related renal type II Na/Pi cotransporter.";
RL J. Biol. Chem. 277:19665-19672(2002).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4, AND IDENTIFICATION BY MASS
RP 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 in the renal brush border membrane (PubMed:11880379).
CC The cotransport has a Na(+):Pi stoichiometry of 2:1 and is
CC electroneutral (By similarity). {ECO:0000250|UniProtKB:Q80SU6,
CC ECO:0000269|PubMed:11880379}.
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:11880379};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71260;
CC Evidence={ECO:0000305|PubMed:11880379};
CC -!- SUBCELLULAR LOCATION: Apical cell membrane
CC {ECO:0000269|PubMed:11880379}; Multi-pass membrane protein
CC {ECO:0000255}. Note=Localized at the brush border membrane in the
CC kidney. {ECO:0000269|PubMed:11880379}.
CC -!- TISSUE SPECIFICITY: Highly expressed in the kidney. Not found in any of
CC the other tested tissues. {ECO:0000269|PubMed:11880379}.
CC -!- DEVELOPMENTAL STAGE: Highest kidney expression is found in weaning rat
CC followed by adult. Lowest expression is found in suckling rat.
CC {ECO:0000269|PubMed:11880379}.
CC -!- SIMILARITY: Belongs to the SLC34A transporter family. {ECO:0000305}.
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DR EMBL; AB077042; BAB96817.1; -; mRNA.
DR RefSeq; NP_647554.1; NM_139338.2.
DR AlphaFoldDB; Q8K4R8; -.
DR IntAct; Q8K4R8; 1.
DR STRING; 10116.ENSRNOP00000014060; -.
DR BindingDB; Q8K4R8; -.
DR ChEMBL; CHEMBL4295898; -.
DR GlyGen; Q8K4R8; 4 sites.
DR iPTMnet; Q8K4R8; -.
DR PhosphoSitePlus; Q8K4R8; -.
DR PaxDb; Q8K4R8; -.
DR PRIDE; Q8K4R8; -.
DR GeneID; 246234; -.
DR KEGG; rno:246234; -.
DR UCSC; RGD:708551; rat.
DR CTD; 142680; -.
DR RGD; 708551; Slc34a3.
DR eggNOG; ENOG502QTG0; Eukaryota.
DR InParanoid; Q8K4R8; -.
DR PhylomeDB; Q8K4R8; -.
DR Reactome; R-RNO-427589; Type II Na+/Pi cotransporters.
DR PRO; PR:Q8K4R8; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0016324; C:apical plasma membrane; IDA:RGD.
DR GO; GO:0005903; C:brush border; ISO:RGD.
DR GO; GO:0031526; C:brush border membrane; IDA:UniProtKB.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:RGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031982; C:vesicle; IBA:GO_Central.
DR GO; GO:0005436; F:sodium:phosphate symporter activity; IMP:RGD.
DR GO; GO:0030643; P:cellular phosphate ion homeostasis; ISO:RGD.
DR GO; GO:0006817; P:phosphate ion transport; IMP:RGD.
DR GO; GO:0032026; P:response to magnesium ion; IEP:RGD.
DR GO; GO:0031667; P:response to nutrient levels; IEP:RGD.
DR GO; GO:0006814; P:sodium ion transport; ISO:RGD.
DR GO; GO:0044341; P:sodium-dependent phosphate transport; IMP:RGD.
DR InterPro; IPR003841; Na/Pi_transpt.
DR InterPro; IPR029850; Na/Pi_transpt_2C.
DR PANTHER; PTHR10010; PTHR10010; 1.
DR PANTHER; PTHR10010:SF35; PTHR10010:SF35; 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 Phosphoprotein; Reference proteome; Sodium; Sodium transport; Symport;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..601
FT /note="Sodium-dependent phosphate transport protein 2C"
FT /id="PRO_0000068619"
FT TOPO_DOM 1..75
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 76..96
FT /note="Helical; Name=M1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 97..110
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 111..131
FT /note="Helical; Name=M2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 132..187
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 188..208
FT /note="Helical; Name=M3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 209..324
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 325..345
FT /note="Helical; Name=M4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 346..369
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 370..390
FT /note="Helical; Name=M5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 391..447
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 448..468
FT /note="Helical; Name=M6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 469..487
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 488..508
FT /note="Helical; Name=M7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 509..512
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 513..533
FT /note="Helical; Name=M8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 534..601
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOD_RES 4
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT CARBOHYD 210
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 264
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 267
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 299
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 275..311
FT /evidence="ECO:0000250|UniProtKB:Q06496"
SQ SEQUENCE 601 AA; 63846 MW; 0F77AD6BFB4755A8 CRC64;
MPNSLAGDQV PNPTLDAIGL VDWSLRNAGT SGSTPGLEEG GTDPWTFSQL KNTDQLKEVG
TASKLHQVVS GFLKACGLLG SLYFFICSLD ILSSAFQLLG SKMAGDIFKD NVVLSNPVAG
LVIGVVVTVL VQSSSTSSSI VVSMVASKSL TVQASVPIIM GVNVGTSITS TLVSMAQSGD
RDEFQRAFGG SAVHGIFNWL TVLVLLPLEN ATAALERLSE LALGAASLQP GGQAPDILKA
LTRPFTHLII QLDSSVVTSS ITSNTTNSSL IKHWCGFRGE TPQGSSEECD LSGSCTERNS
SASPGEDRLL CHHLFAGSEL TDLAVGFILL AGSLLVLCVC LVLIVKLLNS VLRGRIAQAV
KTVINADFPF PFGWLSGYLA ILVGAGLTFL LQSSSVFTAA IVPLMGVGVI NLERAYPLFL
GSNIGTTTTA LLAALASPAD TLLFAVQVAL IHFFFNLAGI LLWYLVPVLR LPIPLAKRFG
DLTAQYRWVA IVYLLLTFLL LPLAAFGLSL AGGSVLAAVG GPLVGLVLLI ILVNVLQRHR
PSWLPRRLQS WAWLPLWLHS LEPWDRLVTG CCPFKAYSNS HMTSKVAHCY ENPQVIASQQ
L
