P2RX3_RAT
ID P2RX3_RAT Reviewed; 397 AA.
AC P49654;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=P2X purinoceptor 3;
DE Short=P2X3;
DE AltName: Full=ATP receptor;
DE AltName: Full=Purinergic receptor;
GN Name=P2rx3;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND SUBUNIT.
RC TISSUE=Spinal ganglion;
RX PubMed=7566120; DOI=10.1038/377432a0;
RA Lewis C., Neidhart S., Holy C., North R.A., Buell G.N., Surprenant A.;
RT "Coexpression of P2X2 and P2X3 receptor subunits can account for ATP-gated
RT currents in sensory neurons.";
RL Nature 377:432-435(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC STRAIN=Sprague-Dawley; TISSUE=Spinal ganglion;
RX PubMed=7566119; DOI=10.1038/377428a0;
RA Chen C.-C., Akopian A.N., Sivilotti L., Colquhoun D., Burnstock G.,
RA Wood J.N.;
RT "A P2X purinoceptor expressed by a subset of sensory neurons.";
RL Nature 377:428-432(1995).
CC -!- FUNCTION: Receptor for ATP that acts as a ligand-gated cation channel
CC (PubMed:7566120, PubMed:7566119). Plays a role in sensory perception.
CC Required for normal perception of pain. Required for normal taste
CC perception (By similarity). {ECO:0000250|UniProtKB:Q3UR32,
CC ECO:0000269|PubMed:7566119, ECO:0000269|PubMed:7566120}.
CC -!- SUBUNIT: Homotrimer (By similarity). Functional P2XRs are organized as
CC homomeric and heteromeric trimers (PubMed:7566120).
CC {ECO:0000250|UniProtKB:P56373, ECO:0000269|PubMed:7566120}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:7566119,
CC ECO:0000269|PubMed:7566120}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P56373}.
CC -!- TISSUE SPECIFICITY: Selectively expressed in sensory ganglia.
CC {ECO:0000269|PubMed:7566119}.
CC -!- SIMILARITY: Belongs to the P2X receptor family. {ECO:0000305}.
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DR EMBL; X91167; CAA62594.1; -; mRNA.
DR EMBL; X90651; CAA62223.1; -; mRNA.
DR PIR; I58099; I58099.
DR PIR; S60334; S60334.
DR RefSeq; NP_001257550.1; NM_001270621.1.
DR RefSeq; NP_112337.2; NM_031075.2.
DR AlphaFoldDB; P49654; -.
DR SMR; P49654; -.
DR STRING; 10116.ENSRNOP00000031629; -.
DR BindingDB; P49654; -.
DR ChEMBL; CHEMBL4824; -.
DR DrugCentral; P49654; -.
DR GuidetoPHARMACOLOGY; 480; -.
DR GlyGen; P49654; 4 sites.
DR iPTMnet; P49654; -.
DR PhosphoSitePlus; P49654; -.
DR PaxDb; P49654; -.
DR GeneID; 81739; -.
DR KEGG; rno:81739; -.
DR UCSC; RGD:620253; rat.
DR CTD; 5024; -.
DR RGD; 620253; P2rx3.
DR VEuPathDB; HostDB:ENSRNOG00000008552; -.
DR eggNOG; ENOG502QUDE; Eukaryota.
DR InParanoid; P49654; -.
DR OMA; CPAEIDD; -.
DR OrthoDB; 1128763at2759; -.
DR PhylomeDB; P49654; -.
DR Reactome; R-RNO-139853; Elevation of cytosolic Ca2+ levels.
DR Reactome; R-RNO-418346; Platelet homeostasis.
DR PRO; PR:P49654; -.
DR Proteomes; UP000002494; Chromosome 3.
DR Bgee; ENSRNOG00000008552; Expressed in pancreas and 13 other tissues.
DR ExpressionAtlas; P49654; baseline and differential.
DR Genevisible; P49654; RN.
DR GO; GO:0030424; C:axon; ISO:RGD.
DR GO; GO:0043197; C:dendritic spine; IDA:RGD.
DR GO; GO:0005794; C:Golgi apparatus; IDA:RGD.
DR GO; GO:0098686; C:hippocampal mossy fiber to CA3 synapse; ISO:RGD.
DR GO; GO:0005639; C:integral component of nuclear inner membrane; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; IMP:UniProtKB.
DR GO; GO:0099056; C:integral component of presynaptic membrane; IDA:SynGO.
DR GO; GO:0016020; C:membrane; IDA:RGD.
DR GO; GO:0045121; C:membrane raft; IDA:RGD.
DR GO; GO:0043005; C:neuron projection; IDA:RGD.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0043235; C:receptor complex; ISO:RGD.
DR GO; GO:0005791; C:rough endoplasmic reticulum; IDA:RGD.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; ISO:RGD.
DR GO; GO:0043195; C:terminal bouton; IDA:RGD.
DR GO; GO:0005524; F:ATP binding; IDA:RGD.
DR GO; GO:0004931; F:extracellularly ATP-gated cation channel activity; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:RGD.
DR GO; GO:0001614; F:purinergic nucleotide receptor activity; IDA:UniProtKB.
DR GO; GO:0061368; P:behavioral response to formalin induced pain; IMP:RGD.
DR GO; GO:0048266; P:behavioral response to pain; ISO:RGD.
DR GO; GO:0006812; P:cation transport; ISO:RGD.
DR GO; GO:0071318; P:cellular response to ATP; IDA:UniProtKB.
DR GO; GO:0007268; P:chemical synaptic transmission; ISO:RGD.
DR GO; GO:0051649; P:establishment of localization in cell; IEA:Ensembl.
DR GO; GO:0098662; P:inorganic cation transmembrane transport; ISS:UniProtKB.
DR GO; GO:0006811; P:ion transport; ISO:RGD.
DR GO; GO:0050804; P:modulation of chemical synaptic transmission; ISO:RGD.
DR GO; GO:0007274; P:neuromuscular synaptic transmission; ISO:RGD.
DR GO; GO:0019228; P:neuronal action potential; IDA:RGD.
DR GO; GO:0030432; P:peristalsis; ISO:RGD.
DR GO; GO:1904058; P:positive regulation of sensory perception of pain; IMP:RGD.
DR GO; GO:0070207; P:protein homotrimerization; ISS:UniProtKB.
DR GO; GO:0048167; P:regulation of synaptic plasticity; ISO:RGD.
DR GO; GO:0033198; P:response to ATP; ISO:RGD.
DR GO; GO:0009743; P:response to carbohydrate; ISO:RGD.
DR GO; GO:0009409; P:response to cold; ISO:RGD.
DR GO; GO:0009408; P:response to heat; ISO:RGD.
DR GO; GO:0001666; P:response to hypoxia; ISO:RGD.
DR GO; GO:0009612; P:response to mechanical stimulus; ISO:RGD.
DR GO; GO:0010033; P:response to organic substance; ISO:RGD.
DR GO; GO:0009266; P:response to temperature stimulus; ISO:RGD.
DR GO; GO:0050909; P:sensory perception of taste; ISO:RGD.
DR GO; GO:0014832; P:urinary bladder smooth muscle contraction; ISO:RGD.
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 1: Evidence at protein 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_0000161552"
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 96
FT /note="M -> I (in Ref. 2; CAA62223)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 397 AA; 44392 MW; AA7ED5410F639D25 CRC64;
MNCISDFFTY ETTKSVVVKS WTIGIINRAV QLLIISYFVG WVFLHEKAYQ VRDTAIESSV
VTKVKGFGRY ANRVMDVSDY VTPPQGTSVF VIITKMIVTE NQMQGFCPEN EEKYRCVSDS
QCGPERFPGG GILTGRCVNY SSVLRTCEIQ GWCPTEVDTV EMPIMMEAEN FTIFIKNSIR
FPLFNFEKGN LLPNLTDKDI KRCRFHPEKA PFCPILRVGD VVKFAGQDFA KLARTGGVLG
IKIGWVCDLD KAWDQCIPKY SFTRLDGVSE KSSVSPGYNF RFAKYYKMEN GSEYRTLLKA
FGIRFDVLVY GNAGKFNIIP TIISSVAAFT SVGVGTVLCD IILLNFLKGA DHYKARKFEE
VTETTLKGTA STNPVFASDQ ATVEKQSTDS GAYSIGH
