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Q08357 (S20A2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 108. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | 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):
Gibbon ape leukemia virus receptor 2
Short name=GLVR-2
Phosphate transporter 2
Short name=PiT-2
Short name=Pit2
Short name=hPit2
Solute carrier family 20 member 2
Gene names
Name:SLC20A2
Synonyms:GLVR2, PIT2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length652 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 and confers human cells susceptibility to infection to amphotropic murine leukemia virus (A-MuLV), 10A1 murine leukemia virus (10A1 MLV) and some feline leukemia virus subgroup B (FeLV-B) variants. Ref.1 Ref.6 Ref.7 Ref.8 Ref.9

Subunit structure

Homodimer. Ref.7 Ref.8

Subcellular location

Cell membrane; Multi-pass membrane protein Ref.5.

Tissue specificity

Ubiquitously expressed.

Induction

Increased by phosphate depletion in osteosarcoma cell lines. Ref.5

Involvement in disease

Basal ganglia calcification, idiopathic, 1 (IBGC1) [MIM:213600]: A form of basal ganglia calcification, an autosomal dominant condition characterized by symmetric calcification in the basal ganglia and other brain regions. Affected individuals can either be asymptomatic or show a wide spectrum of neuropsychiatric symptoms, including parkinsonism, dystonia, tremor, ataxia, dementia, psychosis, seizures, and chronic headache. Serum levels of calcium, phosphate, alkaline phosphatase and parathyroid hormone are normal. The neuropathological hallmark of the disease is vascular and pericapillary calcification, mainly of calcium phosphate, in the affected brain areas.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.12

Sequence similarities

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

Ontologies

Keywords
   Biological processHost-virus interaction
Ion transport
Phosphate transport
Sodium transport
Symport
Transport
   Cellular componentCell membrane
Membrane
   DiseaseDisease mutation
   DomainTransmembrane
Transmembrane helix
   LigandSodium
   Molecular functionHost cell receptor for virus entry
Receptor
   PTMGlycoprotein
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_procession transport

Traceable author statement. Source: Reactome

phosphate ion transmembrane transport

Traceable author statement Ref.1. Source: GOC

sodium ion transmembrane transport

Traceable author statement Ref.1. Source: GOC

transmembrane transport

Traceable author statement. Source: Reactome

transport

Traceable author statement Ref.1. Source: ProtInc

viral process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentextracellular vesicular exosome

Inferred from direct assay PubMed 19199708. Source: UniProt

integral component of plasma membrane

Traceable author statement Ref.1. Source: ProtInc

membrane

Traceable author statement Ref.1. Source: ProtInc

plasma membrane

Traceable author statement. Source: Reactome

   Molecular_functioninorganic phosphate transmembrane transporter activity

Inferred from electronic annotation. Source: InterPro

receptor activity

Traceable author statement Ref.1. Source: ProtInc

sodium:phosphate symporter activity

Traceable author statement Ref.1. Source: ProtInc

virus receptor activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 652652Sodium-dependent phosphate transporter 2
PRO_0000341268

Regions

Topological domain1 – 55Extracellular Potential
Transmembrane6 – 2621Helical; Potential
Topological domain27 – 4620Cytoplasmic Potential
Transmembrane47 – 6721Helical; Potential
Topological domain68 – 8619Extracellular Potential
Transmembrane87 – 10721Helical; 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 – 482248Cytoplasmic Potential
Transmembrane483 – 50321Helical; Potential
Topological domain504 – 53027Extracellular Potential
Transmembrane531 – 55121Helical; Potential
Topological domain552 – 57120Cytoplasmic Potential
Transmembrane572 – 58615Helical; Potential
Topological domain587 – 5937Extracellular Potential
Transmembrane594 – 60916Helical; Potential
Topological domain610 – 62112Cytoplasmic Potential
Transmembrane622 – 64221Helical; Potential
Topological domain643 – 65210Extracellular Potential

Amino acid modifications

Modified residue2681Phosphoserine Ref.11
Glycosylation811N-linked (GlcNAc...) Ref.4

Natural variations

Natural variant421Missing in IBGC1; substantially impaired phosphate transport. Ref.12
VAR_067545
Natural variant4981G → R in IBGC1; substantially impaired phosphate transport. Ref.12
VAR_067546
Natural variant5751E → K in IBGC1; substantially impaired phosphate transport. Ref.12
VAR_067547
Natural variant5951T → M in IBGC1; substantially impaired phosphate transport. Ref.12
VAR_067548
Natural variant6011S → L in IBGC1; substantially impaired phosphate transport. Ref.12
VAR_067549
Natural variant6011S → W in IBGC1; substantially impaired phosphate transport. Ref.12
VAR_067550

Experimental info

Mutagenesis281D → N: Impairs phosphate transport; no effect on retroviral receptor function. Ref.8
Mutagenesis551E → D or K: Abolishes sodium-dependent phosphate transport; no effect on retroviral receptor function. Ref.7 Ref.9
Mutagenesis551E → Q: Abolishes phosphate but not sodium uptake; when associated with Q-91 and Q-575. Ref.7 Ref.9
Mutagenesis811N → V: Abolishes N-glycosylation. Ref.4
Mutagenesis911E → Q: Abolishes phosphate but not sodium uptake; when associated with Q-55 and Q-575. Ref.9
Mutagenesis5061D → N: Impairs phosphate transport; no effect on retroviral receptor function. Ref.8
Mutagenesis5751E → D or K: Abolishes sodium-dependent phosphate transport; no effect on retroviral receptor function. Ref.7 Ref.9
Mutagenesis5751E → Q: Abolishes phosphate but not sodium uptake; when associated with Q-55 and Q-91. Ref.7 Ref.9

Sequences

Sequence LengthMass (Da)Tools
Q08357 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: A0A870C7927DE39C

FASTA65270,392
        10         20         30         40         50         60 
MAMDEYLWMV ILGFIIAFIL AFSVGANDVA NSFGTAVGSG VVTLRQACIL ASIFETTGSV 

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

       130        140        150        160        170        180 
STIGFSLVAI GTKGVQWMEL VKIVASWFIS PLLSGFMSGL LFVLIRIFIL KKEDPVPNGL 

       190        200        210        220        230        240 
RALPVFYAAT IAINVFSIMY TGAPVLGLVL PMWAIALISF GVALLFAFFV WLFVCPWMRR 

       250        260        270        280        290        300 
KITGKLQKEG ALSRVSDESL SKVQEAESPV FKELPGAKAN DDSTIPLTGA AGETLGTSEG 

       310        320        330        340        350        360 
TSAGSHPRAA YGRALSMTHG SVKSPISNGT FGFDGHTRSD GHVYHTVHKD SGLYKDLLHK 

       370        380        390        400        410        420 
IHIDRGPEEK PAQESNYRLL RRNNSYTCYT AAICGLPVHA TFRAADSSAP EDSEKLVGDT 

       430        440        450        460        470        480 
VSYSKKRLRY DSYSSYCNAV AEAEIEAEEG GVEMKLASEL ADPDQPREDP AEEEKEEKDA 

       490        500        510        520        530        540 
PEVHLLFHFL QVLTACFGSF AHGGNDVSNA IGPLVALWLI YKQGGVTQEA ATPVWLLFYG 

       550        560        570        580        590        600 
GVGICTGLWV WGRRVIQTMG KDLTPITPSS GFTIELASAF TVVIASNIGL PVSTTHCKVG 

       610        620        630        640        650 
SVVAVGWIRS RKAVDWRLFR NIFVAWFVTV PVAGLFSAAV MALLMYGILP YV 

« Hide

References

« Hide 'large scale' references
[1]"A human amphotropic retrovirus receptor is a second member of the gibbon ape leukemia virus receptor family."
van Zeijl M., Johann S.V., Closs E., Cunningham J., Eddy R., Shows T.B., O'Hara B.
Proc. Natl. Acad. Sci. U.S.A. 91:1168-1172(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION AS RETROVIRAL RECEPTOR.
Tissue: Placenta.
[2]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]"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.
[4]"Transmembrane topology of PiT-2, a phosphate transporter-retrovirus receptor."
Salauen C., Rodrigues P., Heard J.M.
J. Virol. 75:5584-5592(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: TOPOLOGY, GLYCOSYLATION AT ASN-81, MUTAGENESIS OF ASN-81.
[5]"The amphotropic murine leukemia virus receptor gene encodes a 71-kilodalton protein that is induced by phosphate depletion."
Chien M.L., Foster J.L., Douglas J.L., Garcia J.V.
J. Virol. 71:4564-4570(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: TOPOLOGY, SUBCELLULAR LOCATION, INDUCTION.
[6]"Identification of envelope determinants of feline leukemia virus subgroup B that permit infection and gene transfer to cells expressing human Pit1 or Pit2."
Sugai J., Eiden M., Anderson M.M., Van Hoeven N., Meiering C.D., Overbaugh J.
J. Virol. 75:6841-6849(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS RETROVIRAL RECEPTOR.
[7]"Two highly conserved glutamate residues critical for type III sodium-dependent phosphate transport revealed by uncoupling transport function from retroviral receptor function."
Boettger P., Pedersen L.
J. Biol. Chem. 277:42741-42747(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS SODIUM-PHOSPHATE SYMPORTER, SUBUNIT, MUTAGENESIS OF GLU-55 AND GLU-575.
[8]"Evolutionary and experimental analyses of inorganic phosphate transporter PiT family reveals two related signature sequences harboring highly conserved aspartic acids critical for sodium-dependent phosphate transport function of human PiT2."
Boettger P., Pedersen L.
FEBS J. 272:3060-3074(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS SODIUM-PHOSPHATE SYMPORTER, SUBUNIT, MUTAGENESIS OF ASP-28 AND ASP-506.
[9]"Characterization of transport mechanisms and determinants critical for Na+-dependent Pi symport of the PiT family paralogs human PiT1 and PiT2."
Boettger P., Hede S.E., Grunnet M., Hoyer B., Klaerke D.A., Pedersen L.
Am. J. Physiol. 291:C1377-C1387(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS SODIUM-PHOSPHATE SYMPORTER, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF GLU-55; GLU-91 AND GLU-575.
[10]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-268, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"Mutations in SLC20A2 link familial idiopathic basal ganglia calcification with phosphate homeostasis."
Wang C., Li Y., Shi L., Ren J., Patti M., Wang T., de Oliveira J.R., Sobrido M.J., Quintans B., Baquero M., Cui X., Zhang X.Y., Wang L., Xu H., Wang J., Yao J., Dai X., Liu J. expand/collapse author list , Zhang L., Ma H., Gao Y., Ma X., Feng S., Liu M., Wang Q.K., Forster I.C., Zhang X., Liu J.Y.
Nat. Genet. 44:254-256(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS IBGC1 VAL-42 DEL; ARG-498; LYS-575; MET-595; TRP-601 AND LEU-601, CHARACTERIZATION OF VARIANTS IBGC1 VAL-42 DEL; ARG-498; LYS-575; MET-595; TRP-601 AND LEU-601.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L20852 mRNA. Translation: AAA18018.1.
AK291202 mRNA. Translation: BAF83891.1.
BC028600 mRNA. Translation: AAH28600.1.
PIRA37000.
RefSeqNP_001244109.1. NM_001257180.1.
NP_001244110.1. NM_001257181.1.
NP_006740.1. NM_006749.4.
XP_005273670.1. XM_005273613.1.
UniGeneHs.653173.
Hs.654763.

3D structure databases

ProteinModelPortalQ08357.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112463. 1 interaction.
STRING9606.ENSP00000340465.

Protein family/group databases

TCDB2.A.20.2.3. the inorganic phosphate transporter (pit) family.

PTM databases

PhosphoSiteQ08357.

Polymorphism databases

DMDM74735615.

Proteomic databases

PaxDbQ08357.
PRIDEQ08357.

Protocols and materials databases

DNASU6575.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000342228; ENSP00000340465; ENSG00000168575.
ENST00000520179; ENSP00000429712; ENSG00000168575.
ENST00000520262; ENSP00000429754; ENSG00000168575.
GeneID6575.
KEGGhsa:6575.
UCSCuc003xpe.4. human.

Organism-specific databases

CTD6575.
GeneCardsGC08M042291.
HGNCHGNC:10947. SLC20A2.
HPAHPA026540.
MIM158378. gene.
213600. phenotype.
neXtProtNX_Q08357.
Orphanet1980. Bilateral striopallidodentate calcinosis.
PharmGKBPA35834.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0306.
HOGENOMHOG000231892.
HOVERGENHBG053358.
InParanoidQ08357.
KOK14640.
OMAIFTACAM.
OrthoDBEOG79KPDT.
PhylomeDBQ08357.
TreeFamTF314426.

Enzyme and pathway databases

ReactomeREACT_15518. Transmembrane transport of small molecules.

Gene expression databases

ArrayExpressQ08357.
BgeeQ08357.
CleanExHS_SLC20A2.
GenevestigatorQ08357.

Family and domain databases

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

Other

ChiTaRSSLC20A2. human.
GeneWikiSLC20A2.
GenomeRNAi6575.
NextBio25583.
PROQ08357.
SOURCESearch...

Entry information

Entry nameS20A2_HUMAN
AccessionPrimary (citable) accession number: Q08357
Entry history
Integrated into UniProtKB/Swiss-Prot: June 10, 2008
Last sequence update: November 1, 1996
Last modified: April 16, 2014
This is version 108 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 8

Human chromosome 8: entries, gene names and cross-references to MIM