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Q80UP8 (S20A2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 88. 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 transporter 2
Alternative name(s):
Phosphate transporter 2
Short name=PiT-2
Solute carrier family 20 member 2
Type III sodium-dependent phosphate transporter
Gene names
Name:Slc20a2
Synonyms:Pit2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length656 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Sodium-phosphate symporter which seems to play a fundamental housekeeping role in phosphate transport by absorbing phosphate from interstitial fluid for normal cellular functions such as cellular metabolism, signal transduction, and nucleic acid and lipid synthesis. In vitro, sodium-dependent phosphate uptake is not siginificantly affected by acidic and alkaline conditions, however sodium-independent phosphate uptake occurs at acidic conditions. May play a role in extracellular matrix, cartilage and vascular calcification. Functions as a retroviral receptor By similarity. Ref.1

Subunit structure

Homodimer By similarity.

Subcellular location

Cell membrane; Multi-pass membrane protein By similarity.

Tissue specificity

Widely expressed including intestine, kidney, heart, liver, brain, testis and skin. Expressed throughout the vertcal crypt-axial axis of intestinal epithelium. Ref.1

Sequence similarities

Belongs to the inorganic phosphate transporter (PiT) (TC 2.A.20) family. [View classification]

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 656656Sodium-dependent phosphate transporter 2
PRO_0000341269

Regions

Topological domain1 – 55Extracellular Potential
Transmembrane6 – 2621Helical; Potential
Topological domain27 – 4620Cytoplasmic Potential
Transmembrane47 – 6721Helical; Potential
Topological domain68 – 8619Extracellular Potential
Topological domain108 – 1092Cytoplasmic Potential
Transmembrane110 – 13021Helical; Potential
Topological domain131 – 14212Extracellular Potential
Transmembrane143 – 16321Helical; Potential
Topological domain164 – 19027Cytoplasmic Potential
Transmembrane191 – 21121Helical; Potential
Topological domain212 – 2132Extracellular Potential
Transmembrane214 – 23421Helical; Potential
Topological domain235 – 483249Cytoplasmic Potential
Transmembrane484 – 50421Helical; Potential
Topological domain505 – 53127Extracellular Potential
Transmembrane532 – 55221Helical; Potential
Topological domain553 – 57220Cytoplasmic Potential
Transmembrane573 – 58715Helical; Potential
Topological domain588 – 5947Extracellular Potential
Transmembrane595 – 61016Helical; Potential
Topological domain611 – 62212Cytoplasmic Potential
Transmembrane623 – 64321Helical; Potential
Topological domain644 – 65512Extracellular Potential

Amino acid modifications

Modified residue2681Phosphoserine Ref.5
Glycosylation811N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict531I → V in AAG28493. Ref.1
Sequence conflict531I → V in BAE42159. Ref.2
Sequence conflict531I → V in BAE33999. Ref.2
Sequence conflict531I → V in AAH46510. Ref.4
Sequence conflict551E → A in AAG28493. Ref.1
Sequence conflict1231I → T in AAG28493. Ref.1
Sequence conflict3871T → A in AAG28493. Ref.1
Sequence conflict4871L → F in AAG28493. Ref.1
Sequence conflict6141A → T in BAE42159. Ref.2
Sequence conflict644 – 65613LLMYI…FSSSR → SFMYGILPYV in AAG28493. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q80UP8 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: 0E4678A705B878CB

FASTA65670,866
        10         20         30         40         50         60 
MAMDGYLWMV ILGFIIAFIL AFSVGANDVA NSFGTAVGSG VVTLRQACIL ASIFETTGSV 

        70         80         90        100        110        120 
LLGAKVGETI RKGIIDVNLY NETVETLMAG EVSAMVGSAV WQLIASFLRL PISGTHCIVG 

       130        140        150        160        170        180 
STIGFSLVAI GPKGVQWMEL VKIVASWFIS PLLSGFMSGV LFILIRMFIL TKEDPVPNGL 

       190        200        210        220        230        240 
QALPLFYAAT IAINVFSIMY TGAPVLGLSL PIWAIALISF GVALLFAFFV WLFVCPWMKR 

       250        260        270        280        290        300 
KIAGRLEKES ALSRASDESL RKVQEAESPG FKELPGAKPS DDSAVPLTSL AGEAVGASEG 

       310        320        330        340        350        360 
TSAGNHPRAS YGRALSMTHG SAKSPISNGT FGFEGHMRND GHVYHTVHKD SGLYKDLLHK 

       370        380        390        400        410        420 
IHVDRGSEEK PTQENNYRLL RRNNSYTCYT AAICGMPVHT TFRASDTSSA PEDSEKLVGD 

       430        440        450        460        470        480 
SVSYSKKRLR YDSYSSYCNA VAEAEIEAEE GGVEMRLASE LADPDRPHED PTEEEKEEKD 

       490        500        510        520        530        540 
SAEVHLLFHF LQVLTACFGS FAHGGNDVSN AIGPLVALWL IYQQGGVTQE AATPVWLLFY 

       550        560        570        580        590        600 
GGVGICTGLW VWGRRVIQTM GKDLTPITPS SGFTIELASA FTVVIASNIG LPVSTTHCKV 

       610        620        630        640        650 
GSVVAVGWIR SRKAVDWRLF RNIFVAWFVT VPVAGLFSAA IMALLMYICG LFSSSR 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and characterization of a type III Na-dependent phosphate cotransporter from mouse intestine."
Bai L., Collins J.F., Ghishan F.K.
Am. J. Physiol. 279:C1135-C1143(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION AS SODIUM-PHOSPHATE SYMPORTER, TISSUE SPECIFICITY.
Strain: C57BL/6.
Tissue: Intestine.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: NOD.
Tissue: Spleen.
[3]"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.
[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].
Strain: FVB/N.
Tissue: Mammary tumor.
[5]"The phagosomal proteome in interferon-gamma-activated macrophages."
Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-268, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF196476 mRNA. Translation: AAG28493.1.
AK157206 mRNA. Translation: BAE33999.1.
AK170985 mRNA. Translation: BAE42159.1.
AC140326 Genomic DNA. No translation available.
AC153017 Genomic DNA. No translation available.
BC046510 mRNA. Translation: AAH46510.1.
CCDSCCDS22178.1.
RefSeqNP_035524.2. NM_011394.3.
XP_006509106.1. XM_006509043.1.
XP_006509107.1. XM_006509044.1.
UniGeneMm.323901.
Mm.378231.

3D structure databases

ProteinModelPortalQ80UP8.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ80UP8. 1 interaction.
MINTMINT-4129248.

PTM databases

PhosphoSiteQ80UP8.

Proteomic databases

PaxDbQ80UP8.
PRIDEQ80UP8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000067786; ENSMUSP00000065935; ENSMUSG00000037656.
GeneID20516.
KEGGmmu:20516.
UCSCuc009ldf.2. mouse.

Organism-specific databases

CTD6575.
MGIMGI:97851. Slc20a2.

Phylogenomic databases

eggNOGCOG0306.
GeneTreeENSGT00390000014879.
HOGENOMHOG000231892.
HOVERGENHBG053358.
InParanoidQ80UP8.
KOK14640.
OMAPYGRAFS.
OrthoDBEOG79KPDT.
TreeFamTF314426.

Gene expression databases

ArrayExpressQ80UP8.
BgeeQ80UP8.
GenevestigatorQ80UP8.

Family and domain databases

InterProIPR001204. Phos_transporter.
[Graphical view]
PANTHERPTHR11101. PTHR11101. 1 hit.
PfamPF01384. PHO4. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSLC20A2. mouse.
NextBio298727.
PROQ80UP8.
SOURCESearch...

Entry information

Entry nameS20A2_MOUSE
AccessionPrimary (citable) accession number: Q80UP8
Secondary accession number(s): E9QLQ8, Q3TBZ8, Q9ES96
Entry history
Integrated into UniProtKB/Swiss-Prot: June 10, 2008
Last sequence update: July 27, 2011
Last modified: July 9, 2014
This is version 88 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