P2RX3_MOUSE
ID P2RX3_MOUSE Reviewed; 397 AA.
AC Q3UR32; A2AW02; Q8R1U4;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=P2X purinoceptor 3;
DE Short=P2X3;
DE AltName: Full=ATP receptor;
DE AltName: Full=Purinergic receptor;
GN Name=P2rx3;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Corpora quadrigemina, and Spinal ganglion;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=15961431; DOI=10.1113/jphysiol.2005.088435;
RA Cockayne D.A., Dunn P.M., Zhong Y., Rong W., Hamilton S.G., Knight G.E.,
RA Ruan H.Z., Ma B., Yip P., Nunn P., McMahon S.B., Burnstock G., Ford A.P.;
RT "P2X2 knockout mice and P2X2/P2X3 double knockout mice reveal a role for
RT the P2X2 receptor subunit in mediating multiple sensory effects of ATP.";
RL J. Physiol. (Lond.) 567:621-639(2005).
RN [5]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=16322458; DOI=10.1126/science.1118435;
RA Finger T.E., Danilova V., Barrows J., Bartel D.L., Vigers A.J., Stone L.,
RA Hellekant G., Kinnamon S.C.;
RT "ATP signaling is crucial for communication from taste buds to gustatory
RT nerves.";
RL Science 310:1495-1499(2005).
CC -!- FUNCTION: Receptor for ATP that acts as a ligand-gated cation channel
CC (By similarity). Plays a role in sensory perception (PubMed:15961431,
CC PubMed:16322458). Required for normal perception of pain
CC (PubMed:15961431). Required for normal taste perception
CC (PubMed:16322458). {ECO:0000250|UniProtKB:P56373,
CC ECO:0000269|PubMed:15961431, ECO:0000269|PubMed:16322458}.
CC -!- SUBUNIT: Homotrimer (By similarity). Functional P2XRs are organized as
CC homomeric and heteromeric trimers (By similarity).
CC {ECO:0000250|UniProtKB:P49654, ECO:0000250|UniProtKB:P56373}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P56373};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:P56373}.
CC -!- DISRUPTION PHENOTYPE: Simultaneous knockout of P2rx2 and P2rx3 results
CC in reduced pain-related behaviors in response to intraplantar injection
CC of formalin and reduced urinary bladder reflexes and decreased pelvic
CC afferent nerve activity in response to bladder distension. Neurons have
CC minimal to no response to ATP (PubMed:15961431). Simultaneous knockout
CC of P2rx2 and P2rx3 results in defects in taste responses in the taste
CC nerves and reduced behavioral responses to sweeteners, glutamate and
CC bitter substances (PubMed:16322458). {ECO:0000269|PubMed:15961431,
CC ECO:0000269|PubMed:16322458}.
CC -!- SIMILARITY: Belongs to the P2X receptor family. {ECO:0000305}.
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DR EMBL; AK140283; BAE24316.1; -; mRNA.
DR EMBL; AK141847; BAE24856.1; -; mRNA.
DR EMBL; AL935159; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC023089; AAH23089.1; -; mRNA.
DR CCDS; CCDS16200.1; -.
DR RefSeq; NP_663501.2; NM_145526.2.
DR AlphaFoldDB; Q3UR32; -.
DR SMR; Q3UR32; -.
DR STRING; 10090.ENSMUSP00000028465; -.
DR BindingDB; Q3UR32; -.
DR ChEMBL; CHEMBL2401608; -.
DR GlyGen; Q3UR32; 4 sites.
DR iPTMnet; Q3UR32; -.
DR PhosphoSitePlus; Q3UR32; -.
DR MaxQB; Q3UR32; -.
DR PaxDb; Q3UR32; -.
DR PRIDE; Q3UR32; -.
DR Antibodypedia; 14096; 253 antibodies from 31 providers.
DR DNASU; 228139; -.
DR Ensembl; ENSMUST00000028465; ENSMUSP00000028465; ENSMUSG00000027071.
DR GeneID; 228139; -.
DR KEGG; mmu:228139; -.
DR UCSC; uc008kjr.1; mouse.
DR CTD; 5024; -.
DR MGI; MGI:1097160; P2rx3.
DR VEuPathDB; HostDB:ENSMUSG00000027071; -.
DR eggNOG; ENOG502QUDE; Eukaryota.
DR GeneTree; ENSGT01020000230351; -.
DR InParanoid; Q3UR32; -.
DR OMA; CPAEIDD; -.
DR OrthoDB; 1128763at2759; -.
DR PhylomeDB; Q3UR32; -.
DR TreeFam; TF328633; -.
DR Reactome; R-MMU-139853; Elevation of cytosolic Ca2+ levels.
DR Reactome; R-MMU-418346; Platelet homeostasis.
DR BioGRID-ORCS; 228139; 0 hits in 71 CRISPR screens.
DR ChiTaRS; P2rx3; mouse.
DR PRO; PR:Q3UR32; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q3UR32; protein.
DR Bgee; ENSMUSG00000027071; Expressed in lumbar dorsal root ganglion and 59 other tissues.
DR ExpressionAtlas; Q3UR32; baseline and differential.
DR Genevisible; Q3UR32; MM.
DR GO; GO:0030424; C:axon; IDA:MGI.
DR GO; GO:0043197; C:dendritic spine; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0098686; C:hippocampal mossy fiber to CA3 synapse; IMP:SynGO.
DR GO; GO:0005639; C:integral component of nuclear inner membrane; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0099056; C:integral component of presynaptic membrane; ISO:MGI.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0045121; C:membrane raft; ISO:MGI.
DR GO; GO:0043005; C:neuron projection; IDA:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0043235; C:receptor complex; ISO:MGI.
DR GO; GO:0005791; C:rough endoplasmic reticulum; ISO:MGI.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IMP:SynGO.
DR GO; GO:0043195; C:terminal bouton; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
DR GO; GO:0004931; F:extracellularly ATP-gated cation channel activity; IGI:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0001614; F:purinergic nucleotide receptor activity; ISS:UniProtKB.
DR GO; GO:0061368; P:behavioral response to formalin induced pain; ISO:MGI.
DR GO; GO:0048266; P:behavioral response to pain; IMP:MGI.
DR GO; GO:0006812; P:cation transport; IMP:MGI.
DR GO; GO:0071318; P:cellular response to ATP; ISS:UniProtKB.
DR GO; GO:0007268; P:chemical synaptic transmission; IMP:MGI.
DR GO; GO:0051649; P:establishment of localization in cell; IMP:MGI.
DR GO; GO:0098662; P:inorganic cation transmembrane transport; ISS:UniProtKB.
DR GO; GO:0006811; P:ion transport; IMP:MGI.
DR GO; GO:0050804; P:modulation of chemical synaptic transmission; IMP:SynGO.
DR GO; GO:0007274; P:neuromuscular synaptic transmission; IMP:MGI.
DR GO; GO:0019228; P:neuronal action potential; ISO:MGI.
DR GO; GO:0030432; P:peristalsis; IMP:MGI.
DR GO; GO:1904058; P:positive regulation of sensory perception of pain; ISO:MGI.
DR GO; GO:0070207; P:protein homotrimerization; ISS:UniProtKB.
DR GO; GO:0048167; P:regulation of synaptic plasticity; IMP:MGI.
DR GO; GO:0033198; P:response to ATP; IMP:MGI.
DR GO; GO:0009743; P:response to carbohydrate; IMP:MGI.
DR GO; GO:0009409; P:response to cold; IMP:MGI.
DR GO; GO:0009408; P:response to heat; IMP:MGI.
DR GO; GO:0001666; P:response to hypoxia; IMP:MGI.
DR GO; GO:0009612; P:response to mechanical stimulus; IMP:MGI.
DR GO; GO:0010033; P:response to organic substance; IMP:MGI.
DR GO; GO:0009266; P:response to temperature stimulus; IMP:MGI.
DR GO; GO:0050909; P:sensory perception of taste; IGI:MGI.
DR GO; GO:0014832; P:urinary bladder smooth muscle contraction; IMP:MGI.
DR Gene3D; 2.60.490.10; -; 1.
DR InterPro; IPR003046; P2X3_purnocptor.
DR InterPro; IPR027309; P2X_extracellular_dom_sf.
DR InterPro; IPR001429; P2X_purnocptor.
DR PANTHER; PTHR10125:SF8; PTHR10125:SF8; 1.
DR PIRSF; PIRSF005713; P2X_purinoceptor; 1.
DR PRINTS; PR01310; P2X3RECEPTOR.
DR PRINTS; PR01307; P2XRECEPTOR.
DR TIGRFAMs; TIGR00863; P2X; 1.
DR PROSITE; PS01212; P2X_RECEPTOR; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Cell membrane; Disulfide bond; Glycoprotein; Ion channel;
KW Ion transport; Ligand-gated ion channel; Membrane; Nucleotide-binding;
KW Receptor; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..397
FT /note="P2X purinoceptor 3"
FT /id="PRO_0000269195"
FT TOPO_DOM 1..20
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 21..43
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250|UniProtKB:P56373"
FT TOPO_DOM 44..322
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 323..341
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250|UniProtKB:P56373"
FT TOPO_DOM 342..397
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT BINDING 63..65
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P56373"
FT BINDING 172
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P56373"
FT BINDING 275
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P56373"
FT BINDING 279..281
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P56373"
FT BINDING 299
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P56373"
FT CARBOHYD 139
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 170
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 194
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 290
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 107..153
FT /evidence="ECO:0000250|UniProtKB:P56373"
FT DISULFID 116..137
FT /evidence="ECO:0000250|UniProtKB:P56373"
FT DISULFID 122..147
FT /evidence="ECO:0000250|UniProtKB:P56373"
FT DISULFID 203..213
FT /evidence="ECO:0000250|UniProtKB:P56373"
FT DISULFID 247..256
FT /evidence="ECO:0000250|UniProtKB:P56373"
FT CONFLICT 295
FT /note="R -> P (in Ref. 3; AAH23089)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 397 AA; 44437 MW; BFB90C740E5DD910 CRC64;
MNCISDFFTY ETTKSVVVKS WTIGIINRAV QLLIISYFVG WVFLHEKAYQ VRDTAIESSV
VTKVKGFGRY ANRVMDVSDY VTPPQGTSVF VIITKMIVTE NQMQGFCPEN EEKYRCVSDS
QCGPERFPGG GILTGRCVNY SSVRRTCEIQ GWCPTEVDTV EMPIMMEAEN FTIFIKNSIR
FPLFNFEKGN LLPNLTDKDI KKCRFHPEKA PFCPILRVGD VVKFAGQDFA KLARTGGVLG
IKIGWVCDLD KAWDQCIPKY SFTRLDGVSE KSSVSPGYNF RFAKYYKMEN GSEYRTLLKA
FGIRFDVLVY GNAGKFNIIP TIISSVAAFT SVGVGTVLCD IILLNFLKGA DHYKARKFEE
VTETTLKGTA STNPVFTSDQ ATVEKQSTDS GAYSIGH
