P2RX2_RAT
ID P2RX2_RAT Reviewed; 472 AA.
AC P49653; O54868;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=P2X purinoceptor 2;
DE Short=P2X2;
DE AltName: Full=ATP receptor;
DE AltName: Full=Purinergic receptor;
GN Name=P2rx2;
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].
RX PubMed=7523952; DOI=10.1038/371519a0;
RA Brake A.J., Wagenbach M.J., Julius D.;
RT "New structural motif for ligand-gated ion channels defined by an
RT ionotropic ATP receptor.";
RL Nature 371:519-523(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Wistar; TISSUE=Liver;
RX PubMed=9119082; DOI=10.1016/s0014-5793(97)00128-2;
RA Braendle U., Spielmanns P., Osteroth R., Sim J., Surprenant A., Buell G.,
RA Ruppersberg J.P., Plinkert P.K., Zenner H.P., Glowatzki E.;
RT "Desensitization of the P2X(2) receptor controlled by alternative
RT splicing.";
RL FEBS Lett. 404:294-298(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 326-340, AND ALTERNATIVE SPLICING.
RC STRAIN=Sprague-Dawley, and Wistar; TISSUE=Vas deferens;
RX PubMed=7542879; DOI=10.1006/bbrc.1995.1998;
RA Housley G.D., Greenwood D., Bennett T., Ryan A.F.;
RT "Identification of a short form of the P2xR1-purinoceptor subunit produced
RT by alternative splicing in the pituitary and cochlea.";
RL Biochem. Biophys. Res. Commun. 212:501-508(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE (ISOFORM P2RX2-3).
RC STRAIN=Sprague-Dawley; TISSUE=Pituitary;
RA Koshimizu T., Tomic M., van Goor F., Stojilkovic S.S.;
RL Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP DISULFIDE BOND.
RX PubMed=12921863; DOI=10.1016/s0014-2999(03)02038-7;
RA Nakazawa K., Ojima H., Ishii-Nozawa R., Takeuchi K., Ohno Y.;
RT "Intracellular disulfide bond that affects ATP responsiveness of P2X(2)
RT receptor/channel.";
RL Eur. J. Pharmacol. 474:205-208(2003).
CC -!- FUNCTION: Ion channel gated by extracellular ATP involved in a variety
CC of cellular responses, such as excitatory postsynaptic responses in
CC sensory neurons, neuromuscular junctions (NMJ) formation, hearing,
CC perception of taste and peristalsis. In the inner ear, regulates sound
CC transduction and auditory neurotransmission, outer hair cell
CC electromotility, inner ear gap junctions, and K(+) recycling. Mediates
CC synaptic transmission between neurons and from neurons to smooth muscle
CC (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homotrimer and heterotrimer; functional P2XRs are organized as
CC homomeric and heteromeric trimers. {ECO:0000250}.
CC -!- INTERACTION:
CC P49653; P51577: P2rx4; NbExp=4; IntAct=EBI-9511543, EBI-9511617;
CC P49653; P51579: P2rx6; NbExp=4; IntAct=EBI-9511543, EBI-9511515;
CC P49653-1; P49653-1: P2rx2; NbExp=3; IntAct=EBI-15757407, EBI-15757407;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Comment=Additional isoforms seem to exist.;
CC Name=P2RX2-1;
CC IsoId=P49653-1; Sequence=Displayed;
CC Name=P2RX2-2;
CC IsoId=P49653-2; Sequence=VSP_004501, VSP_004502;
CC Name=P2RX2-3;
CC IsoId=P49653-3; Sequence=VSP_004500;
CC -!- TISSUE SPECIFICITY: High levels in pituitary and vas deferens. Lower
CC extent in spinal cord, bladder, brain, adrenal, testis, sensory
CC epithelia from the inner ear.
CC -!- SIMILARITY: Belongs to the P2X receptor family. {ECO:0000305}.
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DR EMBL; U14414; AAA50756.1; -; mRNA.
DR EMBL; Y09910; CAA71046.1; -; Genomic_DNA.
DR EMBL; L43511; AAC42067.1; -; mRNA.
DR EMBL; AF020756; AAB94570.1; -; mRNA.
DR PIR; S50859; S50859.
DR RefSeq; NP_446108.2; NM_053656.2. [P49653-1]
DR AlphaFoldDB; P49653; -.
DR SMR; P49653; -.
DR CORUM; P49653; -.
DR DIP; DIP-48329N; -.
DR IntAct; P49653; 2.
DR MINT; P49653; -.
DR STRING; 10116.ENSRNOP00000053533; -.
DR BindingDB; P49653; -.
DR ChEMBL; CHEMBL2135; -.
DR DrugCentral; P49653; -.
DR GuidetoPHARMACOLOGY; 479; -.
DR TCDB; 1.A.7.1.2; the atp-gated p2x receptor cation channel (p2x receptor) family.
DR GlyGen; P49653; 3 sites.
DR iPTMnet; P49653; -.
DR PhosphoSitePlus; P49653; -.
DR PaxDb; P49653; -.
DR PRIDE; P49653; -.
DR Ensembl; ENSRNOT00000056693; ENSRNOP00000053532; ENSRNOG00000037456. [P49653-3]
DR GeneID; 114115; -.
DR KEGG; rno:114115; -.
DR UCSC; RGD:620251; rat. [P49653-1]
DR CTD; 22953; -.
DR RGD; 620251; P2rx2.
DR VEuPathDB; HostDB:ENSRNOG00000037456; -.
DR eggNOG; ENOG502QVP9; Eukaryota.
DR GeneTree; ENSGT01020000230351; -.
DR InParanoid; P49653; -.
DR OrthoDB; 1128763at2759; -.
DR PhylomeDB; P49653; -.
DR Reactome; R-RNO-139853; Elevation of cytosolic Ca2+ levels.
DR Reactome; R-RNO-418346; Platelet homeostasis.
DR PRO; PR:P49653; -.
DR Proteomes; UP000002494; Chromosome 12.
DR Bgee; ENSRNOG00000037456; Expressed in testis and 16 other tissues.
DR ExpressionAtlas; P49653; baseline and differential.
DR Genevisible; P49653; RN.
DR GO; GO:0016324; C:apical plasma membrane; ISO:RGD.
DR GO; GO:0009986; C:cell surface; IDA:RGD.
DR GO; GO:0043197; C:dendritic spine; IDA:RGD.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0016021; C:integral component of membrane; IDA: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; ISO:RGD.
DR GO; GO:0099059; C:integral component of presynaptic active zone membrane; IDA:SynGO.
DR GO; GO:0016020; C:membrane; IDA:RGD.
DR GO; GO:0043025; C:neuronal cell body; IDA:ARUK-UCL.
DR GO; GO:0005886; C:plasma membrane; IDA:BHF-UCL.
DR GO; GO:0014069; C:postsynaptic density; IDA:RGD.
DR GO; GO:0042734; C:presynaptic membrane; IDA:RGD.
DR GO; GO:0043235; C:receptor complex; IDA:ARUK-UCL.
DR GO; GO:0043195; C:terminal bouton; IDA:RGD.
DR GO; GO:0005524; F:ATP binding; IDA:RGD.
DR GO; GO:0046870; F:cadmium ion binding; IDA:RGD.
DR GO; GO:0050897; F:cobalt ion binding; IDA:RGD.
DR GO; GO:0005507; F:copper ion binding; IDA:RGD.
DR GO; GO:0004931; F:extracellularly ATP-gated cation channel activity; IDA:RGD.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0015276; F:ligand-gated ion channel activity; IDA:RGD.
DR GO; GO:0045340; F:mercury ion binding; IDA:RGD.
DR GO; GO:0016151; F:nickel cation binding; IDA:RGD.
DR GO; GO:0035091; F:phosphatidylinositol binding; IMP:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:RGD.
DR GO; GO:0001614; F:purinergic nucleotide receptor activity; IDA:RGD.
DR GO; GO:0043924; F:suramin binding; IDA:RGD.
DR GO; GO:0008270; F:zinc ion binding; IDA:RGD.
DR GO; GO:0048266; P:behavioral response to pain; ISO:RGD.
DR GO; GO:0007268; P:chemical synaptic transmission; ISO:RGD.
DR GO; GO:0003029; P:detection of hypoxic conditions in blood by carotid body chemoreceptor signaling; ISO:RGD.
DR GO; GO:0007528; P:neuromuscular junction development; 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:0099509; P:regulation of presynaptic cytosolic calcium ion concentration; IDA:SynGO.
DR GO; GO:2000300; P:regulation of synaptic vesicle exocytosis; IDA:SynGO.
DR GO; GO:0033198; P:response to ATP; ISO:RGD.
DR GO; GO:0009743; P:response to carbohydrate; ISO:RGD.
DR GO; GO:0001666; P:response to hypoxia; ISO:RGD.
DR GO; GO:0002931; P:response to ischemia; IMP:ARUK-UCL.
DR GO; GO:0014070; P:response to organic cyclic compound; IDA:RGD.
DR GO; GO:0010033; P:response to organic substance; ISO:RGD.
DR GO; GO:0007605; P:sensory perception of sound; ISO:RGD.
DR GO; GO:0050909; P:sensory perception of taste; ISO:RGD.
DR GO; GO:0048741; P:skeletal muscle fiber development; ISO:RGD.
DR GO; GO:0014832; P:urinary bladder smooth muscle contraction; ISO:RGD.
DR Gene3D; 2.60.490.10; -; 1.
DR InterPro; IPR003045; P2X2_purnocptor.
DR InterPro; IPR027309; P2X_extracellular_dom_sf.
DR InterPro; IPR001429; P2X_purnocptor.
DR PIRSF; PIRSF005713; P2X_purinoceptor; 1.
DR PRINTS; PR01309; P2X2RECEPTOR.
DR PRINTS; PR01307; P2XRECEPTOR.
DR TIGRFAMs; TIGR00863; P2X; 1.
DR PROSITE; PS01212; P2X_RECEPTOR; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Disulfide bond; Glycoprotein;
KW Ion channel; Ion transport; Ligand-gated ion channel; Membrane; Receptor;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..472
FT /note="P2X purinoceptor 2"
FT /id="PRO_0000161550"
FT TOPO_DOM 1..34
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 35..52
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 53..326
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 327..347
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 348..472
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 309..322
FT /note="Pore-forming motif"
FT /evidence="ECO:0000255"
FT REGION 393..472
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 396..410
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 429..443
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 452..472
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 182
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 239
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 298
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 9..430
FT /evidence="ECO:0000269|PubMed:12921863"
FT DISULFID 113..164
FT /evidence="ECO:0000250"
FT DISULFID 124..147
FT /evidence="ECO:0000250"
FT DISULFID 130..158
FT /evidence="ECO:0000250"
FT DISULFID 214..224
FT /evidence="ECO:0000250"
FT DISULFID 258..267
FT /evidence="ECO:0000250"
FT VAR_SEQ 173..199
FT /note="Missing (in isoform P2RX2-3)"
FT /evidence="ECO:0000305"
FT /id="VSP_004500"
FT VAR_SEQ 344..360
FT /note="GSFLCDWILLTFMNKNK -> VRNPNSLGDLGQVGSVW (in isoform
FT P2RX2-2)"
FT /evidence="ECO:0000305"
FT /id="VSP_004501"
FT VAR_SEQ 361..472
FT /note="Missing (in isoform P2RX2-2)"
FT /evidence="ECO:0000305"
FT /id="VSP_004502"
SQ SEQUENCE 472 AA; 52617 MW; AB53E09A2CADA6A2 CRC64;
MVRRLARGCW SAFWDYETPK VIVVRNRRLG FVHRMVQLLI LLYFVWYVFI VQKSYQDSET
GPESSIITKV KGITMSEDKV WDVEEYVKPP EGGSVVSIIT RIEVTPSQTL GTCPESMRVH
SSTCHSDDDC IAGQLDMQGN GIRTGHCVPY YHGDSKTCEV SAWCPVEDGT SDNHFLGKMA
PNFTILIKNS IHYPKFKFSK GNIASQKSDY LKHCTFDQDS DPYCPIFRLG FIVEKAGENF
TELAHKGGVI GVIINWNCDL DLSESECNPK YSFRRLDPKY DPASSGYNFR FAKYYKINGT
TTTRTLIKAY GIRIDVIVHG QAGKFSLIPT IINLATALTS IGVGSFLCDW ILLTFMNKNK
LYSHKKFDKV RTPKHPSSRW PVTLALVLGQ IPPPPSHYSQ DQPPSPPSGE GPTLGEGAEL
PLAVQSPRPC SISALTEQVV DTLGQHMGQR PPVPEPSQQD STSTDPKGLA QL
