P2RX1_RAT
ID P2RX1_RAT Reviewed; 399 AA.
AC P47824;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=P2X purinoceptor 1;
DE Short=P2X1;
DE AltName: Full=ATP receptor;
DE AltName: Full=Purinergic receptor;
DE AltName: Full=RP-2 protein;
GN Name=P2rx1;
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=Vas deferens;
RX PubMed=7523951; DOI=10.1038/371516a0;
RA Valera S., Hussy N., Evans R.J., Adami N., North R.A., Surprenant A.,
RA Buell G.N.;
RT "A new class of ligand-gated ion channel defined by P2x receptor for
RT extracellular ATP.";
RL Nature 371:516-519(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate;
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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 189-399.
RC STRAIN=Sprague-Dawley; TISSUE=Thymus;
RX PubMed=2072913; DOI=10.1128/mcb.11.8.4177-4188.1991;
RA Owens G.P., Hahn W.E., Cohen J.J.;
RT "Identification of mRNAs associated with programmed cell death in immature
RT thymocytes.";
RL Mol. Cell. Biol. 11:4177-4188(1991).
CC -!- FUNCTION: Ligand-gated ion channel with relatively high calcium
CC permeability. Binding to ATP mediates synaptic transmission between
CC neurons and from neurons to smooth muscle. Seems to be linked to
CC apoptosis, by increasing the intracellular concentration of calcium in
CC the presence of ATP, leading to programmed cell death.
CC -!- SUBUNIT: Homo- or heteropolymers.
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: High levels in vas deferens and urinary bladder.
CC Lower extent in spinal cord, coeliac ganglion, lung and spleen
CC (probably in the smooth muscle part of both organs).
CC -!- DEVELOPMENTAL STAGE: Expressed during apoptosis in thymocytes.
CC -!- INDUCTION: By irradiation and dexamethasone (in thymocytes).
CC -!- SIMILARITY: Belongs to the P2X receptor family. {ECO:0000305}.
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DR EMBL; X80477; CAA56647.1; -; mRNA.
DR EMBL; BC061742; AAH61742.1; -; mRNA.
DR EMBL; M80602; AAA42065.1; -; mRNA.
DR PIR; S50860; S50860.
DR RefSeq; NP_001135839.1; NM_001142367.2.
DR RefSeq; NP_001272344.1; NM_001285415.1.
DR RefSeq; NP_037129.1; NM_012997.3.
DR AlphaFoldDB; P47824; -.
DR SMR; P47824; -.
DR STRING; 10116.ENSRNOP00000024068; -.
DR BindingDB; P47824; -.
DR ChEMBL; CHEMBL2530; -.
DR DrugCentral; P47824; -.
DR GuidetoPHARMACOLOGY; 478; -.
DR TCDB; 1.A.7.1.1; the atp-gated p2x receptor cation channel (p2x receptor) family.
DR GlyGen; P47824; 4 sites.
DR iPTMnet; P47824; -.
DR PhosphoSitePlus; P47824; -.
DR PaxDb; P47824; -.
DR PRIDE; P47824; -.
DR DNASU; 25505; -.
DR Ensembl; ENSRNOT00000024068; ENSRNOP00000024068; ENSRNOG00000017606.
DR GeneID; 25505; -.
DR KEGG; rno:25505; -.
DR CTD; 5023; -.
DR RGD; 3240; P2rx1.
DR eggNOG; ENOG502QSUI; Eukaryota.
DR GeneTree; ENSGT01020000230351; -.
DR HOGENOM; CLU_034469_2_0_1; -.
DR InParanoid; P47824; -.
DR OMA; ARHFMEN; -.
DR OrthoDB; 1128763at2759; -.
DR PhylomeDB; P47824; -.
DR Reactome; R-RNO-139853; Elevation of cytosolic Ca2+ levels.
DR Reactome; R-RNO-418346; Platelet homeostasis.
DR Reactome; R-RNO-6798695; Neutrophil degranulation.
DR PRO; PR:P47824; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000017606; Expressed in pancreas and 16 other tissues.
DR ExpressionAtlas; P47824; baseline and differential.
DR Genevisible; P47824; RN.
DR GO; GO:0009897; C:external side of plasma membrane; ISO:RGD.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0005639; C:integral component of nuclear inner membrane; IBA:GO_Central.
DR GO; GO:0099055; C:integral component of postsynaptic membrane; IDA:SynGO.
DR GO; GO:0099059; C:integral component of presynaptic active zone membrane; IDA:SynGO.
DR GO; GO:0045121; C:membrane raft; IDA:RGD.
DR GO; GO:0043005; C:neuron projection; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0045211; C:postsynaptic membrane; ISO:RGD.
DR GO; GO:0032991; C:protein-containing complex; IDA:RGD.
DR GO; GO:0005524; F:ATP binding; IDA:RGD.
DR GO; GO:0005261; F:cation channel activity; ISO: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:0000166; F:nucleotide binding; IDA:RGD.
DR GO; GO:0097159; F:organic cyclic compound binding; IPI:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:RGD.
DR GO; GO:0001614; F:purinergic nucleotide receptor activity; ISO:RGD.
DR GO; GO:0043924; F:suramin binding; IDA:RGD.
DR GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; ISO:RGD.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0098655; P:cation transmembrane transport; IDA:RGD.
DR GO; GO:0046513; P:ceramide biosynthetic process; ISO:RGD.
DR GO; GO:0007320; P:insemination; ISO:RGD.
DR GO; GO:0034220; P:ion transmembrane transport; IMP:RGD.
DR GO; GO:0006811; P:ion transport; ISO:RGD.
DR GO; GO:0019228; P:neuronal action potential; IDA:RGD.
DR GO; GO:0030168; P:platelet activation; ISO:RGD.
DR GO; GO:1905665; P:positive regulation of calcium ion import across plasma membrane; IDA:RGD.
DR GO; GO:0043270; P:positive regulation of ion transport; ISO:RGD.
DR GO; GO:0008217; P:regulation of blood pressure; IMP:RGD.
DR GO; GO:0051924; P:regulation of calcium ion transport; ISO:RGD.
DR GO; GO:0099509; P:regulation of presynaptic cytosolic calcium ion concentration; IDA:SynGO.
DR GO; GO:0006940; P:regulation of smooth muscle contraction; ISO:RGD.
DR GO; GO:2000300; P:regulation of synaptic vesicle exocytosis; IDA:SynGO.
DR GO; GO:0003056; P:regulation of vascular associated smooth muscle contraction; ISO:RGD.
DR GO; GO:0019229; P:regulation of vasoconstriction; ISO:RGD.
DR GO; GO:0033198; P:response to ATP; ISO:RGD.
DR GO; GO:0010033; P:response to organic substance; ISO:RGD.
DR GO; GO:0002554; P:serotonin secretion by platelet; ISO:RGD.
DR GO; GO:0035249; P:synaptic transmission, glutamatergic; IMP:RGD.
DR Gene3D; 2.60.490.10; -; 1.
DR InterPro; IPR003044; P2X1_purnocptor.
DR InterPro; IPR027309; P2X_extracellular_dom_sf.
DR InterPro; IPR001429; P2X_purnocptor.
DR PANTHER; PTHR10125:SF9; PTHR10125:SF9; 1.
DR PIRSF; PIRSF005713; P2X_purinoceptor; 1.
DR PRINTS; PR01308; P2X1RECEPTOR.
DR PRINTS; PR01307; P2XRECEPTOR.
DR TIGRFAMs; TIGR00863; P2X; 1.
DR PROSITE; PS01212; P2X_RECEPTOR; 1.
PE 2: Evidence at transcript level;
KW Apoptosis; Disulfide bond; Glycoprotein; Ion channel; Ion transport;
KW Ligand-gated ion channel; Membrane; Phosphoprotein; Receptor;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..399
FT /note="P2X purinoceptor 1"
FT /id="PRO_0000161547"
FT TOPO_DOM 1..28
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 29..50
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 51..338
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 339..358
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 359..399
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 331..338
FT /note="Pore-forming motif"
FT /evidence="ECO:0000255"
FT REGION 374..399
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 387
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P51575"
FT MOD_RES 388
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P51575"
FT MOD_RES 389
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P51575"
FT CARBOHYD 153
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 184
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 210
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 300
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 117..165
FT /evidence="ECO:0000250"
FT DISULFID 126..149
FT /evidence="ECO:0000250"
FT DISULFID 132..159
FT /evidence="ECO:0000250"
FT DISULFID 217..227
FT /evidence="ECO:0000250"
FT DISULFID 261..270
FT /evidence="ECO:0000250"
FT CONFLICT 189..201
FT /note="IKNSISFPRFKVN -> PQLAHGCYPCPPH (in Ref. 3)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 399 AA; 44957 MW; 04B79E171D78AEC2 CRC64;
MARRLQDELS AFFFEYDTPR MVLVRNKKVG VIFRLIQLVV LVYVIGWVFV YEKGYQTSSD
LISSVSVKLK GLAVTQLQGL GPQVWDVADY VFPAHGDSSF VVMTNFIVTP QQTQGHCAEN
PEGGICQDDS GCTPGKAERK AQGIRTGNCV PFNGTVKTCE IFGWCPVEVD DKIPSPALLR
EAENFTLFIK NSISFPRFKV NRRNLVEEVN GTYMKKCLYH KIQHPLCPVF NLGYVVRESG
QDFRSLAEKG GVVGITIDWK CDLDWHVRHC KPIYQFHGLY GEKNLSPGFN FRFARHFVQN
GTNRRHLFKV FGIHFDILVD GKAGKFDIIP TMTTIGSGIG IFGVATVLCD LLLLHILPKR
HYYKQKKFKY AEDMGPGEGE HDPVATSSTL GLQENMRTS
