P2RX5_RAT
ID P2RX5_RAT Reviewed; 455 AA.
AC P51578; Q64613;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 25-MAY-2022, entry version 134.
DE RecName: Full=P2X purinoceptor 5;
DE Short=P2X5;
DE AltName: Full=ATP receptor;
DE AltName: Full=Purinergic receptor;
GN Name=P2rx5;
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].
RC TISSUE=Coeliac ganglion;
RX PubMed=8786426; DOI=10.1523/jneurosci.16-08-02495.1996;
RA Collo G., Kawashima E., Pich E., Neidhart S., North R.A., Surprenant A.,
RA Buell G.N.;
RT "Cloning of P2X5 and P2X6 receptors and the distribution and properties of
RT an extended family of ATP-gated ion channels.";
RL J. Neurosci. 16:2495-2507(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Heart;
RX PubMed=8690069; DOI=10.1016/0014-5793(96)00499-1;
RA Garcia-Guzman M., Soto F., Laube B., Stuehmer W.;
RT "Molecular cloning and functional expression of a novel rat heart P2X
RT purinoceptor.";
RL FEBS Lett. 388:123-127(1996).
CC -!- FUNCTION: Receptor for ATP that acts as a ligand-gated ion channel.
CC -!- SUBUNIT: Functional P2XRs are organized as homomeric and heteromeric
CC trimers. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Predominantly expressed in heart but are also
CC present in brain, spinal cord and adrenal gland.
CC -!- SIMILARITY: Belongs to the P2X receptor family. {ECO:0000305}.
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DR EMBL; X92069; CAA63052.1; -; mRNA.
DR EMBL; X97328; CAA65993.1; -; mRNA.
DR PIR; S71344; S71344.
DR RefSeq; NP_542958.2; NM_080780.2.
DR AlphaFoldDB; P51578; -.
DR SMR; P51578; -.
DR STRING; 10116.ENSRNOP00000026156; -.
DR BindingDB; P51578; -.
DR ChEMBL; CHEMBL2495; -.
DR DrugCentral; P51578; -.
DR GuidetoPHARMACOLOGY; 482; -.
DR GlyGen; P51578; 3 sites.
DR PaxDb; P51578; -.
DR GeneID; 113995; -.
DR KEGG; rno:113995; -.
DR CTD; 5026; -.
DR RGD; 620256; P2rx5.
DR eggNOG; ENOG502QSUI; Eukaryota.
DR InParanoid; P51578; -.
DR OrthoDB; 1128763at2759; -.
DR PhylomeDB; P51578; -.
DR Reactome; R-RNO-139853; Elevation of cytosolic Ca2+ levels.
DR Reactome; R-RNO-418346; Platelet homeostasis.
DR PRO; PR:P51578; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005639; C:integral component of nuclear inner membrane; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:InterPro.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0098794; C:postsynapse; IEA:GOC.
DR GO; GO:0005524; F:ATP 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:RGD.
DR GO; GO:0001614; F:purinergic nucleotide receptor activity; IEA:InterPro.
DR GO; GO:0005244; F:voltage-gated ion channel activity; IDA:RGD.
DR GO; GO:0098655; P:cation transmembrane transport; IDA:RGD.
DR GO; GO:0006812; P:cation transport; TAS:RGD.
DR GO; GO:1905665; P:positive regulation of calcium ion import across plasma membrane; IDA:RGD.
DR GO; GO:0043416; P:regulation of skeletal muscle tissue regeneration; IMP:RGD.
DR GO; GO:0033198; P:response to ATP; IDA:RGD.
DR GO; GO:0051592; P:response to calcium ion; IDA:RGD.
DR GO; GO:0009268; P:response to pH; IDA:RGD.
DR GO; GO:0010043; P:response to zinc ion; IDA:RGD.
DR GO; GO:0048630; P:skeletal muscle tissue growth; TAS:RGD.
DR Gene3D; 2.60.490.10; -; 1.
DR InterPro; IPR003048; P2X5_purnocptor.
DR InterPro; IPR027309; P2X_extracellular_dom_sf.
DR InterPro; IPR001429; P2X_purnocptor.
DR PANTHER; PTHR10125:SF12; PTHR10125:SF12; 1.
DR PIRSF; PIRSF005713; P2X_purinoceptor; 1.
DR PRINTS; PR01312; P2X5RECEPTOR.
DR PRINTS; PR01307; P2XRECEPTOR.
DR TIGRFAMs; TIGR00863; P2X; 1.
DR PROSITE; PS01212; P2X_RECEPTOR; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond; Glycoprotein; Ion channel; Ion transport;
KW Ligand-gated ion channel; Membrane; Receptor; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..455
FT /note="P2X purinoceptor 5"
FT /id="PRO_0000161556"
FT TOPO_DOM 1..30
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 31..51
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 52..341
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 342..362
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 363..455
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 384..422
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 384..410
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 77
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 157
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 202
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 118..169
FT /evidence="ECO:0000250"
FT DISULFID 129..152
FT /evidence="ECO:0000250"
FT DISULFID 135..163
FT /evidence="ECO:0000250"
FT DISULFID 220..229
FT /evidence="ECO:0000250"
FT DISULFID 263..272
FT /evidence="ECO:0000250"
FT CONFLICT 191
FT /note="S -> F (in Ref. 2; CAA65993)"
FT /evidence="ECO:0000305"
FT CONFLICT 396
FT /note="R -> Q (in Ref. 2; CAA65993)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 455 AA; 51479 MW; D4405BE440490F70 CRC64;
MGQAAWKGFV LSLFDYKTAK FVVAKSKKVG LLYRVLQLII LLYLLIWVFL IKKSYQDIDT
SLQSAVVTKV KGVAYTNTTM LGERLWDVAD FVIPSQGENV FFVVTNLIVT PNQRQGICAE
REGIPDGECS EDDDCHAGES VVAGHGLKTG RCLRVGNSTR GTCEIFAWCP VETKSMPTDP
LLKDAESFTI SIKNFIRFPK FNFSKANVLE TDNKHFLKTC HFSSTNLYCP IFRLGSIVRW
AGADFQDIAL KGGVIGIYIE WDCDLDKAAS KCNPHYYFNR LDNKHTHSIS SGYNFRFARY
YRDPNGVEFR DLMKAYGIRF DVIVNGKAGK FSIIPTVINI GSGLALMGAG AFFCDLVLIY
LIRKSEFYRD KKFEKVRGQK EDANVEVEAN EMEQERPEDE PLERVRQDEQ SQELAQSGRK
QNSNCQVLLE PARFGLRENA IVNVKQSQIL HPVKT
