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Q3UR32 (P2RX3_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 72. 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:
P2X purinoceptor 3

Short name=P2X3
Alternative name(s):
ATP receptor
Purinergic receptor
Gene names
Name:P2rx3
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length397 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Receptor for ATP that acts as a ligand-gated ion channel By similarity. Ref.4

Subunit structure

Functional P2XRs are organized as homomeric and heteromeric trimers By similarity.

Subcellular location

Membrane; Multi-pass membrane protein By similarity.

Disruption phenotype

Simultaneous knockout of P2rx2 and P2rx3 results in reduced pain-related behaviors in response to intraplantar injection of formalin and reduced urinary bladder reflexes and decreased pelvic afferent nerve activity in response to bladder distension. Neurons have minimal to no response to ATP (Ref.4). Simultaneous knockout of P2rx2 and P2rx3 results in defects in taste responses in the taste nerves and reduced behavioral responses to sweeteners, glutamate and bitter substances (Ref.5). Ref.4 Ref.5

Sequence similarities

Belongs to the P2X receptor family.

Ontologies

Keywords
   Biological processIon transport
Transport
   Cellular componentMembrane
   DomainTransmembrane
Transmembrane helix
   Molecular functionIon channel
Ligand-gated ion channel
Receptor
   PTMDisulfide bond
Glycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processbehavioral response to pain

Inferred from mutant phenotype PubMed 11069181PubMed 11069182. Source: MGI

cation transport

Inferred from mutant phenotype PubMed 11069182. Source: MGI

ion transport

Inferred from mutant phenotype PubMed 11069181. Source: MGI

neuromuscular synaptic transmission

Inferred from mutant phenotype PubMed 12813150. Source: MGI

neuronal action potential

Inferred from electronic annotation. Source: Ensembl

peristalsis

Inferred from mutant phenotype PubMed 12813150. Source: MGI

protein homooligomerization

Inferred from electronic annotation. Source: Ensembl

purinergic nucleotide receptor signaling pathway

Inferred from Biological aspect of Ancestor. Source: GOC

regulation of synaptic plasticity

Inferred from mutant phenotype PubMed 17074061. Source: MGI

response to ATP

Inferred from mutant phenotype PubMed 11069181PubMed 11069182PubMed 11466438PubMed 12813150PubMed 17074061. Source: MGI

response to carbohydrate

Inferred from mutant phenotype Ref.5. Source: MGI

response to cold

Inferred from mutant phenotype PubMed 15927378. Source: MGI

response to heat

Inferred from mutant phenotype PubMed 15927378. Source: MGI

response to hypoxia

Inferred from mutant phenotype PubMed 14672995. Source: MGI

response to mechanical stimulus

Inferred from mutant phenotype PubMed 11466438. Source: MGI

response to organic substance

Inferred from mutant phenotype PubMed 11069181PubMed 11069182. Source: MGI

response to temperature stimulus

Inferred from mutant phenotype PubMed 11069182. Source: MGI

sensory perception of taste

Inferred from genetic interaction Ref.5. Source: MGI

synaptic transmission

Inferred from mutant phenotype PubMed 17074061. Source: MGI

urinary bladder smooth muscle contraction

Inferred from mutant phenotype PubMed 11069181Ref.4. Source: MGI

   Cellular_componentGolgi apparatus

Inferred from electronic annotation. Source: Ensembl

axon

Inferred from direct assay PubMed 11466438. Source: MGI

dendritic spine

Inferred from electronic annotation. Source: Ensembl

integral component of plasma membrane

Inferred from sequence or structural similarity PubMed 9300827. Source: MGI

membrane

Inferred from Biological aspect of Ancestor. Source: RefGenome

membrane raft

Inferred from electronic annotation. Source: Ensembl

neuron projection

Inferred from direct assay PubMed 11466438. Source: MGI

neuronal cell body

Inferred from electronic annotation. Source: Ensembl

receptor complex

Inferred from sequence orthology PubMed 23382219. Source: MGI

rough endoplasmic reticulum

Inferred from electronic annotation. Source: Ensembl

terminal bouton

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionATP binding

Inferred from electronic annotation. Source: Ensembl

extracellular ATP-gated cation channel activity

Inferred from genetic interaction PubMed 15081800. Source: MGI

purinergic nucleotide receptor activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 397397P2X purinoceptor 3
PRO_0000269195

Regions

Topological domain1 – 2222Cytoplasmic Potential
Transmembrane23 – 4321Helical; Name=1; Potential
Topological domain44 – 317274Extracellular Potential
Transmembrane318 – 33821Helical; Name=2; Potential
Topological domain339 – 39759Cytoplasmic Potential

Amino acid modifications

Glycosylation1391N-linked (GlcNAc...) Potential
Glycosylation1701N-linked (GlcNAc...) Potential
Glycosylation1941N-linked (GlcNAc...) Potential
Glycosylation2901N-linked (GlcNAc...) Potential
Disulfide bond107 ↔ 153 By similarity
Disulfide bond116 ↔ 137 By similarity
Disulfide bond122 ↔ 147 By similarity
Disulfide bond203 ↔ 213 By similarity
Disulfide bond247 ↔ 256 By similarity

Experimental info

Sequence conflict2951R → P in AAH23089. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q3UR32 [UniParc].

Last modified October 11, 2005. Version 1.
Checksum: BFB90C740E5DD910

FASTA39744,437
        10         20         30         40         50         60 
MNCISDFFTY ETTKSVVVKS WTIGIINRAV QLLIISYFVG WVFLHEKAYQ VRDTAIESSV 

        70         80         90        100        110        120 
VTKVKGFGRY ANRVMDVSDY VTPPQGTSVF VIITKMIVTE NQMQGFCPEN EEKYRCVSDS 

       130        140        150        160        170        180 
QCGPERFPGG GILTGRCVNY SSVRRTCEIQ GWCPTEVDTV EMPIMMEAEN FTIFIKNSIR 

       190        200        210        220        230        240 
FPLFNFEKGN LLPNLTDKDI KKCRFHPEKA PFCPILRVGD VVKFAGQDFA KLARTGGVLG 

       250        260        270        280        290        300 
IKIGWVCDLD KAWDQCIPKY SFTRLDGVSE KSSVSPGYNF RFAKYYKMEN GSEYRTLLKA 

       310        320        330        340        350        360 
FGIRFDVLVY GNAGKFNIIP TIISSVAAFT SVGVGTVLCD IILLNFLKGA DHYKARKFEE 

       370        380        390 
VTETTLKGTA STNPVFTSDQ ATVEKQSTDS GAYSIGH 

« Hide

References

« Hide 'large scale' references
[1]"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: C57BL/6J.
Tissue: Corpora quadrigemina and Spinal ganglion.
[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]"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.
[4]"P2X2 knockout mice and P2X2/P2X3 double knockout mice reveal a role for the P2X2 receptor subunit in mediating multiple sensory effects of ATP."
Cockayne D.A., Dunn P.M., Zhong Y., Rong W., Hamilton S.G., Knight G.E., Ruan H.Z., Ma B., Yip P., Nunn P., McMahon S.B., Burnstock G., Ford A.P.
J. Physiol. (Lond.) 567:621-639(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE.
[5]"ATP signaling is crucial for communication from taste buds to gustatory nerves."
Finger T.E., Danilova V., Barrows J., Bartel D.L., Vigers A.J., Stone L., Hellekant G., Kinnamon S.C.
Science 310:1495-1499(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK140283 mRNA. Translation: BAE24316.1.
AK141847 mRNA. Translation: BAE24856.1.
AL935159 Genomic DNA. Translation: CAM18192.1.
BC023089 mRNA. Translation: AAH23089.1.
RefSeqNP_663501.2. NM_145526.2.
UniGeneMm.440375.
Mm.448935.

3D structure databases

ProteinModelPortalQ3UR32.
SMRQ3UR32. Positions 24-344.
ModBaseSearch...
MobiDBSearch...

PTM databases

PhosphoSiteQ3UR32.

Proteomic databases

PRIDEQ3UR32.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000028465; ENSMUSP00000028465; ENSMUSG00000027071.
GeneID228139.
KEGGmmu:228139.
UCSCuc008kjr.1. mouse.

Organism-specific databases

CTD5024.
MGIMGI:1097160. P2rx3.

Phylogenomic databases

eggNOGNOG40178.
GeneTreeENSGT00740000115538.
HOGENOMHOG000232042.
HOVERGENHBG053086.
InParanoidA2AW02.
KOK05217.
OMAISYFVGW.
OrthoDBEOG78PV92.
PhylomeDBQ3UR32.
TreeFamTF328633.

Gene expression databases

BgeeQ3UR32.
GenevestigatorQ3UR32.

Family and domain databases

Gene3D2.60.490.10. 1 hit.
InterProIPR003046. P2X3_purnocptor.
IPR027309. P2X_extracellular_dom.
IPR001429. P2X_purnocptor.
[Graphical view]
PANTHERPTHR10125. PTHR10125. 1 hit.
PTHR10125:SF8. PTHR10125:SF8. 1 hit.
PfamPF00864. P2X_receptor. 1 hit.
[Graphical view]
PRINTSPR01310. P2X3RECEPTOR.
PR01307. P2XRECEPTOR.
TIGRFAMsTIGR00863. P2X. 1 hit.
PROSITEPS01212. P2X_RECEPTOR. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio378939.
PROQ3UR32.
SOURCESearch...

Entry information

Entry nameP2RX3_MOUSE
AccessionPrimary (citable) accession number: Q3UR32
Secondary accession number(s): A2AW02, Q8R1U4
Entry history
Integrated into UniProtKB/Swiss-Prot: December 12, 2006
Last sequence update: October 11, 2005
Last modified: April 16, 2014
This is version 72 of the entry and version 1 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