NPT2C_MOUSE
ID NPT2C_MOUSE Reviewed; 601 AA.
AC Q80SU6; Q05AC3;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 124.
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; Synonyms=Npt2c;
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 [GENOMIC DNA / MRNA], FUNCTION, TRANSPORTER ACTIVITY,
RP SUBCELLULAR LOCATION, BIOPHYSICOCHEMICAL PROPERTIES, AND INDUCTION.
RX PubMed=12690469; DOI=10.1007/s00424-003-1010-6;
RA Ohkido I., Segawa H., Yanagida R., Nakamura M., Miyamoto K.;
RT "Cloning, gene structure and dietary regulation of the type-IIc Na/Pi
RT cotransporter in the mouse kidney.";
RL Pflugers Arch. 446:106-115(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 [5]
RP FUNCTION, TRANSPORTER ACTIVITY, STOICHIOMETRY, AND MUTAGENESIS OF GLY-195
RP AND 189-SER--SER-191.
RX PubMed=16113079; DOI=10.1073/pnas.0505882102;
RA Bacconi A., Virkki L.V., Biber J., Murer H., Forster I.C.;
RT "Renouncing electroneutrality is not free of charge: switching on
RT electrogenicity in a Na+-coupled phosphate cotransporter.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:12606-12611(2005).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney;
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 in the renal brush border membrane (PubMed:12690469,
CC PubMed:16113079). The cotransport has a Na(+):Pi stoichiometry of 2:1
CC and is electroneutral (PubMed:16113079). {ECO:0000269|PubMed:12690469,
CC ECO:0000269|PubMed:16113079}.
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:12690469, ECO:0000269|PubMed:16113079};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71260;
CC Evidence={ECO:0000305|PubMed:12690469};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=200 uM for phosphate {ECO:0000269|PubMed:12690469};
CC pH dependence:
CC Optimum pH is 7.5. {ECO:0000269|PubMed:12690469};
CC -!- SUBCELLULAR LOCATION: Apical cell membrane
CC {ECO:0000269|PubMed:12690469}; Multi-pass membrane protein
CC {ECO:0000255}. Note=Localized at the brush border membrane in the
CC kidney. {ECO:0000269|PubMed:12690469}.
CC -!- TISSUE SPECIFICITY: Expressed only in the kidney.
CC {ECO:0000269|PubMed:12690469}.
CC -!- SIMILARITY: Belongs to the SLC34A transporter family. {ECO:0000305}.
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DR EMBL; AB054999; BAB83241.1; -; mRNA.
DR EMBL; AB080134; BAC55069.1; -; Genomic_DNA.
DR EMBL; AL732309; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466542; EDL08215.1; -; Genomic_DNA.
DR EMBL; CH466542; EDL08216.1; -; Genomic_DNA.
DR EMBL; BC125326; AAI25327.1; -; mRNA.
DR EMBL; BC131997; AAI31998.1; -; mRNA.
DR CCDS; CCDS15754.1; -.
DR RefSeq; NP_543130.2; NM_080854.3.
DR RefSeq; XP_006497740.1; XM_006497677.1.
DR RefSeq; XP_006497741.1; XM_006497678.1.
DR AlphaFoldDB; Q80SU6; -.
DR STRING; 10090.ENSMUSP00000006638; -.
DR BindingDB; Q80SU6; -.
DR ChEMBL; CHEMBL4295882; -.
DR GlyGen; Q80SU6; 3 sites.
DR iPTMnet; Q80SU6; -.
DR PhosphoSitePlus; Q80SU6; -.
DR jPOST; Q80SU6; -.
DR PaxDb; Q80SU6; -.
DR PRIDE; Q80SU6; -.
DR ProteomicsDB; 253005; -.
DR Antibodypedia; 18978; 128 antibodies from 21 providers.
DR DNASU; 142681; -.
DR Ensembl; ENSMUST00000006638; ENSMUSP00000006638; ENSMUSG00000006469.
DR GeneID; 142681; -.
DR KEGG; mmu:142681; -.
DR UCSC; uc008iqt.3; mouse.
DR CTD; 142680; -.
DR MGI; MGI:2159410; Slc34a3.
DR VEuPathDB; HostDB:ENSMUSG00000006469; -.
DR eggNOG; ENOG502QTG0; Eukaryota.
DR GeneTree; ENSGT00950000183177; -.
DR HOGENOM; CLU_025063_0_0_1; -.
DR InParanoid; Q80SU6; -.
DR OMA; HDAIPVM; -.
DR OrthoDB; 976094at2759; -.
DR PhylomeDB; Q80SU6; -.
DR TreeFam; TF313981; -.
DR Reactome; R-MMU-427589; Type II Na+/Pi cotransporters.
DR BioGRID-ORCS; 142681; 3 hits in 77 CRISPR screens.
DR PRO; PR:Q80SU6; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q80SU6; protein.
DR Bgee; ENSMUSG00000006469; Expressed in right kidney and 27 other tissues.
DR Genevisible; Q80SU6; MM.
DR GO; GO:0016324; C:apical plasma membrane; IDA:MGI.
DR GO; GO:0005903; C:brush border; IDA:MGI.
DR GO; GO:0031526; C:brush border membrane; IDA:UniProtKB.
DR GO; GO:0031410; C:cytoplasmic vesicle; ISO:MGI.
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; IDA:MGI.
DR GO; GO:0030643; P:cellular phosphate ion homeostasis; ISO:MGI.
DR GO; GO:0006817; P:phosphate ion transport; IDA:MGI.
DR GO; GO:0006814; P:sodium ion transport; ISO:MGI.
DR GO; GO:0044341; P:sodium-dependent phosphate transport; ISO:MGI.
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_0000068618"
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..441
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 442..462
FT /note="Helical; Name=M6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 463..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:0000250|UniProtKB:Q8K4R8"
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"
FT MUTAGEN 189..191
FT /note="SGS->AGA: Change of cotransport Na(+):Pi
FT stoichiometry to 3:1; when associated with D-195."
FT /evidence="ECO:0000269|PubMed:16113079"
FT MUTAGEN 195
FT /note="G->D: Change of cotransport Na(+):Pi stoichiometry
FT to 3:1; when associated with 189-AGA-191."
FT /evidence="ECO:0000269|PubMed:16113079"
FT CONFLICT 353
FT /note="K -> R (in Ref. 1; BAB83241/BAC55069)"
FT /evidence="ECO:0000305"
FT CONFLICT 361
FT /note="K -> R (in Ref. 1; BAB83241/BAC55069)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 601 AA; 63939 MW; 4B7FE1FBC5877AB6 CRC64;
MPNSLAGGQV PNPTLDAFDL VDRSLRNAGI SGSIPGLEEG GTDPWTFSPL KNADQLKEVG
MASRLRRVVS SFLKACGLLG SLYFFICSLD ILSSAFQLLG SKMAGDIFKD NVVLSNPVAG
LVIGVLVTVL VQSSSTSSSI VVSMVASKLL TVQVSVPIIM GVNVGTSITS TLVSMAQSGD
RDEFQRAFSG SAVHGIFNWL TVLVLLPLES ATAALERLSE LALGAASLQP GQQAPDILKA
LTRPFTHLII QLDSSVITSG ITSNTTNSSL IKHWCGFRGE TPQGSSEGCG LFSSCTERNS
SASPEEDRLL CHHLFAGSKL TDLAVGFILL AGSLLVLCVC LVLIVKLLNS VLKGRIAQAV
KTVINADFPF PFGWLSGYLA ILVGAGLTFL LQSSSVFTAA IVPLMGVGVI DLERAYPLFL
GSNIGTTTTA LLAALASPAD MLIFAVQVAL IHFFFNLAGI LLWYLVPVLR LPIPLAKRFG
NLTAQYRWVA IVYLLLTFLL LPLAAFGLSL AGGTVLAAVG GPLVGLVLLI ILVNVLQQHR
PSWLPRCLQS WAWLPLWLHS LEPWDRLVTA CCPCRACSNS PMTSKVAHCY ENPQVIASQQ
L
