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Protein

P2X purinoceptor 3

Gene

P2rx3

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

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

GO - Molecular functioni

  • ATP binding Source: InterPro
  • extracellular ATP-gated cation channel activity Source: MGI
  • purinergic nucleotide receptor activity Source: GO_Central

GO - Biological processi

  • behavioral response to pain Source: MGI
  • cation transport Source: MGI
  • ion transport Source: MGI
  • neuromuscular synaptic transmission Source: MGI
  • neuronal action potential Source: Ensembl
  • peristalsis Source: MGI
  • protein homooligomerization Source: Ensembl
  • purinergic nucleotide receptor signaling pathway Source: GOC
  • regulation of synaptic plasticity Source: MGI
  • response to ATP Source: MGI
  • response to carbohydrate Source: MGI
  • response to cold Source: MGI
  • response to heat Source: MGI
  • response to hypoxia Source: MGI
  • response to mechanical stimulus Source: MGI
  • response to organic substance Source: MGI
  • response to temperature stimulus Source: MGI
  • sensory perception of taste Source: MGI
  • synaptic transmission Source: MGI
  • urinary bladder smooth muscle contraction Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Ion channel, Ligand-gated ion channel, Receptor

Keywords - Biological processi

Ion transport, Transport

Names & Taxonomyi

Protein namesi
Recommended name:
P2X purinoceptor 3
Short name:
P2X3
Alternative name(s):
ATP receptor
Purinergic receptor
Gene namesi
Name:P2rx3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:1097160. P2rx3.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 2222CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei23 – 4321Helical; Name=1Sequence AnalysisAdd
BLAST
Topological domaini44 – 317274ExtracellularSequence AnalysisAdd
BLAST
Transmembranei318 – 33821Helical; Name=2Sequence AnalysisAdd
BLAST
Topological domaini339 – 39759CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  • axon Source: MGI
  • dendritic spine Source: Ensembl
  • Golgi apparatus Source: Ensembl
  • integral component of nuclear inner membrane Source: GO_Central
  • integral component of plasma membrane Source: MGI
  • membrane raft Source: Ensembl
  • neuronal cell body Source: Ensembl
  • neuron projection Source: MGI
  • receptor complex Source: MGI
  • rough endoplasmic reticulum Source: Ensembl
  • terminal bouton Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Disruption phenotypei

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 (PubMed:15961431). 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 (PubMed:16322458).2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 397397P2X purinoceptor 3PRO_0000269195Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi107 ↔ 153By similarity
Disulfide bondi116 ↔ 137By similarity
Disulfide bondi122 ↔ 147By similarity
Glycosylationi139 – 1391N-linked (GlcNAc...)Sequence Analysis
Glycosylationi170 – 1701N-linked (GlcNAc...)Sequence Analysis
Glycosylationi194 – 1941N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi203 ↔ 213By similarity
Disulfide bondi247 ↔ 256By similarity
Glycosylationi290 – 2901N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiQ3UR32.
PRIDEiQ3UR32.

PTM databases

PhosphoSiteiQ3UR32.

Expressioni

Gene expression databases

BgeeiQ3UR32.
ExpressionAtlasiQ3UR32. baseline and differential.
GenevisibleiQ3UR32. MM.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000028465.

Structurei

3D structure databases

ProteinModelPortaliQ3UR32.
SMRiQ3UR32. Positions 24-344.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the P2X receptor family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG40178.
GeneTreeiENSGT00390000016028.
HOGENOMiHOG000232042.
HOVERGENiHBG053086.
InParanoidiQ3UR32.
KOiK05217.
OMAiVGWVFLH.
OrthoDBiEOG78PV92.
PhylomeDBiQ3UR32.
TreeFamiTF328633.

Family and domain databases

Gene3Di2.60.490.10. 1 hit.
InterProiIPR003046. P2X3_purnocptor.
IPR027309. P2X_extracellular_dom.
IPR001429. P2X_purnocptor.
[Graphical view]
PANTHERiPTHR10125. PTHR10125. 1 hit.
PTHR10125:SF8. PTHR10125:SF8. 1 hit.
PfamiPF00864. P2X_receptor. 1 hit.
[Graphical view]
PIRSFiPIRSF005713. P2X_purinoceptor. 1 hit.
PRINTSiPR01310. P2X3RECEPTOR.
PR01307. P2XRECEPTOR.
TIGRFAMsiTIGR00863. P2X. 1 hit.
PROSITEiPS01212. P2X_RECEPTOR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q3UR32-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNCISDFFTY ETTKSVVVKS WTIGIINRAV QLLIISYFVG WVFLHEKAYQ
60 70 80 90 100
VRDTAIESSV VTKVKGFGRY ANRVMDVSDY VTPPQGTSVF VIITKMIVTE
110 120 130 140 150
NQMQGFCPEN EEKYRCVSDS QCGPERFPGG GILTGRCVNY SSVRRTCEIQ
160 170 180 190 200
GWCPTEVDTV EMPIMMEAEN FTIFIKNSIR FPLFNFEKGN LLPNLTDKDI
210 220 230 240 250
KKCRFHPEKA PFCPILRVGD VVKFAGQDFA KLARTGGVLG IKIGWVCDLD
260 270 280 290 300
KAWDQCIPKY SFTRLDGVSE KSSVSPGYNF RFAKYYKMEN GSEYRTLLKA
310 320 330 340 350
FGIRFDVLVY GNAGKFNIIP TIISSVAAFT SVGVGTVLCD IILLNFLKGA
360 370 380 390
DHYKARKFEE VTETTLKGTA STNPVFTSDQ ATVEKQSTDS GAYSIGH
Length:397
Mass (Da):44,437
Last modified:October 11, 2005 - v1
Checksum:iBFB90C740E5DD910
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti295 – 2951R → P in AAH23089 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK140283 mRNA. Translation: BAE24316.1.
AK141847 mRNA. Translation: BAE24856.1.
AL935159 Genomic DNA. Translation: CAM18192.1.
BC023089 mRNA. Translation: AAH23089.1.
CCDSiCCDS16200.1.
RefSeqiNP_663501.2. NM_145526.2.
UniGeneiMm.440375.
Mm.448935.

Genome annotation databases

EnsembliENSMUST00000028465; ENSMUSP00000028465; ENSMUSG00000027071.
GeneIDi228139.
KEGGimmu:228139.
UCSCiuc008kjr.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK140283 mRNA. Translation: BAE24316.1.
AK141847 mRNA. Translation: BAE24856.1.
AL935159 Genomic DNA. Translation: CAM18192.1.
BC023089 mRNA. Translation: AAH23089.1.
CCDSiCCDS16200.1.
RefSeqiNP_663501.2. NM_145526.2.
UniGeneiMm.440375.
Mm.448935.

3D structure databases

ProteinModelPortaliQ3UR32.
SMRiQ3UR32. Positions 24-344.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000028465.

Chemistry

ChEMBLiCHEMBL2401608.
GuidetoPHARMACOLOGYi480.

PTM databases

PhosphoSiteiQ3UR32.

Proteomic databases

MaxQBiQ3UR32.
PRIDEiQ3UR32.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000028465; ENSMUSP00000028465; ENSMUSG00000027071.
GeneIDi228139.
KEGGimmu:228139.
UCSCiuc008kjr.1. mouse.

Organism-specific databases

CTDi5024.
MGIiMGI:1097160. P2rx3.

Phylogenomic databases

eggNOGiNOG40178.
GeneTreeiENSGT00390000016028.
HOGENOMiHOG000232042.
HOVERGENiHBG053086.
InParanoidiQ3UR32.
KOiK05217.
OMAiVGWVFLH.
OrthoDBiEOG78PV92.
PhylomeDBiQ3UR32.
TreeFamiTF328633.

Miscellaneous databases

NextBioi378939.
PROiQ3UR32.
SOURCEiSearch...

Gene expression databases

BgeeiQ3UR32.
ExpressionAtlasiQ3UR32. baseline and differential.
GenevisibleiQ3UR32. MM.

Family and domain databases

Gene3Di2.60.490.10. 1 hit.
InterProiIPR003046. P2X3_purnocptor.
IPR027309. P2X_extracellular_dom.
IPR001429. P2X_purnocptor.
[Graphical view]
PANTHERiPTHR10125. PTHR10125. 1 hit.
PTHR10125:SF8. PTHR10125:SF8. 1 hit.
PfamiPF00864. P2X_receptor. 1 hit.
[Graphical view]
PIRSFiPIRSF005713. P2X_purinoceptor. 1 hit.
PRINTSiPR01310. P2X3RECEPTOR.
PR01307. P2XRECEPTOR.
TIGRFAMsiTIGR00863. P2X. 1 hit.
PROSITEiPS01212. P2X_RECEPTOR. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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.

Entry informationi

Entry nameiP2RX3_MOUSE
AccessioniPrimary (citable) accession number: Q3UR32
Secondary accession number(s): A2AW02, Q8R1U4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 12, 2006
Last sequence update: October 11, 2005
Last modified: June 24, 2015
This is version 82 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.