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Q80SU6 (NPT2C_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 74. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Sodium-dependent phosphate transport protein 2C

Short name=Sodium-phosphate transport protein 2C
Alternative name(s):
Na(+)-dependent phosphate cotransporter 2C
Sodium/phosphate cotransporter 2C
Short name=Na(+)/Pi cotransporter 2C
Short name=NaPi-2c
Solute carrier family 34 member 3
Gene names
Name:Slc34a3
Synonyms:Npt2c
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length601 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May be involved in actively transporting phosphate into cells via Na+ cotransport in the renal brush border membrane. Probably mediates 20-30% of the apical influx.

Subcellular location

Membrane; Multi-pass membrane protein.

Tissue specificity

Observed only in kidney.

Miscellaneous

The cotransport has a Na+:Pi stoichiometry of 2:1 and is electroneutral.

Sequence similarities

Belongs to the SLC34A transporter family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 601601Sodium-dependent phosphate transport protein 2C
PRO_0000068618

Regions

Topological domain1 – 7575Cytoplasmic Potential
Transmembrane76 – 9621Helical; Name=M1; Potential
Topological domain97 – 11014Extracellular Potential
Transmembrane111 – 13121Helical; Name=M2; Potential
Topological domain132 – 18756Cytoplasmic Potential
Transmembrane188 – 20821Helical; Name=M3; Potential
Topological domain209 – 324116Extracellular Potential
Transmembrane325 – 34521Helical; Name=M4; Potential
Topological domain346 – 36924Cytoplasmic Potential
Transmembrane370 – 39021Helical; Name=M5; Potential
Topological domain391 – 44151Extracellular Potential
Transmembrane442 – 46221Helical; Name=M6; Potential
Topological domain463 – 48725Cytoplasmic Potential
Transmembrane488 – 50821Helical; Name=M7; Potential
Topological domain509 – 5124Extracellular Potential
Transmembrane513 – 53321Helical; Name=M8; Potential
Topological domain534 – 60168Cytoplasmic Potential
Compositional bias426 – 4294Poly-Thr

Amino acid modifications

Glycosylation2641N-linked (GlcNAc...) Potential
Glycosylation2671N-linked (GlcNAc...) Potential
Glycosylation2991N-linked (GlcNAc...) Potential
Disulfide bond275 ↔ 311 By similarity

Experimental info

Mutagenesis189 – 1913SGS → AGA: Change of cotransport Na(+):Pi stoichiometry to 3:1; when associated with D-195. Ref.5
Mutagenesis1951G → D: Change of cotransport Na(+):Pi stoichiometry to 3:1; when associated with 189-AGA-191. Ref.5
Sequence conflict3531K → R in BAB83241. Ref.1
Sequence conflict3531K → R in BAC55069. Ref.1
Sequence conflict3611K → R in BAB83241. Ref.1
Sequence conflict3611K → R in BAC55069. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q80SU6 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: 4B7FE1FBC5877AB6

FASTA60163,939
        10         20         30         40         50         60 
MPNSLAGGQV PNPTLDAFDL VDRSLRNAGI SGSIPGLEEG GTDPWTFSPL KNADQLKEVG 

        70         80         90        100        110        120 
MASRLRRVVS SFLKACGLLG SLYFFICSLD ILSSAFQLLG SKMAGDIFKD NVVLSNPVAG 

       130        140        150        160        170        180 
LVIGVLVTVL VQSSSTSSSI VVSMVASKLL TVQVSVPIIM GVNVGTSITS TLVSMAQSGD 

       190        200        210        220        230        240 
RDEFQRAFSG SAVHGIFNWL TVLVLLPLES ATAALERLSE LALGAASLQP GQQAPDILKA 

       250        260        270        280        290        300 
LTRPFTHLII QLDSSVITSG ITSNTTNSSL IKHWCGFRGE TPQGSSEGCG LFSSCTERNS 

       310        320        330        340        350        360 
SASPEEDRLL CHHLFAGSKL TDLAVGFILL AGSLLVLCVC LVLIVKLLNS VLKGRIAQAV 

       370        380        390        400        410        420 
KTVINADFPF PFGWLSGYLA ILVGAGLTFL LQSSSVFTAA IVPLMGVGVI DLERAYPLFL 

       430        440        450        460        470        480 
GSNIGTTTTA LLAALASPAD MLIFAVQVAL IHFFFNLAGI LLWYLVPVLR LPIPLAKRFG 

       490        500        510        520        530        540 
NLTAQYRWVA IVYLLLTFLL LPLAAFGLSL AGGTVLAAVG GPLVGLVLLI ILVNVLQQHR 

       550        560        570        580        590        600 
PSWLPRCLQS WAWLPLWLHS LEPWDRLVTA CCPCRACSNS PMTSKVAHCY ENPQVIASQQ 


L 

« Hide

References

« Hide 'large scale' references
[1]"Cloning, gene structure and dietary regulation of the type-IIc Na/Pi cotransporter in the mouse kidney."
Ohkido I., Segawa H., Yanagida R., Nakamura M., Miyamoto K.
Pflugers Arch. 446:106-115(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], CHARACTERIZATION, INDUCTION.
[2]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[3]Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[5]"Renouncing electroneutrality is not free of charge: switching on electrogenicity in a Na+-coupled phosphate cotransporter."
Bacconi A., Virkki L.V., Biber J., Murer H., Forster I.C.
Proc. Natl. Acad. Sci. U.S.A. 102:12606-12611(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF GLY-195 AND 189-SER--SER-191.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB054999 mRNA. Translation: BAB83241.1.
AB080134 Genomic DNA. Translation: BAC55069.1.
AL732309 Genomic DNA. Translation: CAM14672.1.
CH466542 Genomic DNA. Translation: EDL08215.1.
CH466542 Genomic DNA. Translation: EDL08216.1.
BC125326 mRNA. Translation: AAI25327.1.
BC131997 mRNA. Translation: AAI31998.1.
CCDSCCDS15754.1.
RefSeqNP_543130.2. NM_080854.3.
XP_006497740.1. XM_006497677.1.
XP_006497741.1. XM_006497678.1.
UniGeneMm.346652.
Mm.490356.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000006638.

PTM databases

PhosphoSiteQ80SU6.

Proteomic databases

PaxDbQ80SU6.
PRIDEQ80SU6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000006638; ENSMUSP00000006638; ENSMUSG00000006469.
GeneID142681.
KEGGmmu:142681.
UCSCuc008iqt.3. mouse.

Organism-specific databases

CTD142680.
MGIMGI:2159410. Slc34a3.

Phylogenomic databases

eggNOGCOG1283.
GeneTreeENSGT00390000005032.
HOGENOMHOG000006550.
HOVERGENHBG006527.
InParanoidQ05AC3.
KOK14683.
OMALIKRWCG.
OrthoDBEOG72ZCDP.
TreeFamTF313981.

Gene expression databases

BgeeQ80SU6.
GenevestigatorQ80SU6.

Family and domain databases

InterProIPR003841. Na/Pi_transpt.
[Graphical view]
PfamPF02690. Na_Pi_cotrans. 2 hits.
[Graphical view]
TIGRFAMsTIGR01013. 2a58. 1 hit.
ProtoNetSearch...

Other

NextBio370049.
PROQ80SU6.
SOURCESearch...

Entry information

Entry nameNPT2C_MOUSE
AccessionPrimary (citable) accession number: Q80SU6
Secondary accession number(s): Q05AC3
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: July 27, 2011
Last modified: July 9, 2014
This is version 74 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot