P2RX1_HUMAN
ID P2RX1_HUMAN Reviewed; 399 AA.
AC P51575; Q9UK84;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=P2X purinoceptor 1;
DE Short=P2X1;
DE AltName: Full=ATP receptor;
DE AltName: Full=Purinergic receptor;
GN Name=P2RX1; Synonyms=P2X1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Urinary bladder smooth muscle;
RX PubMed=8834001;
RA Valera S., Talabot F., Evans R.J., Gos A., Antonarakis S.E., Morris M.A.,
RA Buell G.N.;
RT "Characterization and chromosomal localization of a human P2X receptor from
RT the urinary bladder.";
RL Recept. Channels 3:283-289(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Urinary bladder;
RX PubMed=8809107; DOI=10.1016/0167-4781(96)00112-1;
RA Longhurst P.A., Schwegel T., Folander K., Swanson R.;
RT "The human P2x1 receptor: molecular cloning, tissue distribution, and
RT localization to chromosome 17.";
RL Biochim. Biophys. Acta 1308:185-188(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Platelet;
RX PubMed=9565569; DOI=10.1074/jbc.273.19.11544;
RA Sun B., Li J., Okahara K., Kambayashi J.;
RT "P2X1 purinoceptor in human platelets. Molecular cloning and functional
RT characterization after heterologous expression.";
RL J. Biol. Chem. 273:11544-11547(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Blood;
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 [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-8.
RC TISSUE=Placenta;
RA Dhulipala P.D., Kotlikoff M.I.;
RT "Regulation of human P2X1 promoter by bHLH factors in smooth muscle
RT cells.";
RL Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP DISULFIDE BONDS.
RX PubMed=11809854; DOI=10.1124/mol.61.2.303;
RA Ennion S.J., Evans R.J.;
RT "Conserved cysteine residues in the extracellular loop of the human P2X(1)
RT receptor form disulfide bonds and are involved in receptor trafficking to
RT the cell surface.";
RL Mol. Pharmacol. 61:303-311(2002).
RN [7]
RP PHOSPHORYLATION AT SER-387; SER-388 AND THR-389.
RX PubMed=22971236; DOI=10.1111/jnc.12012;
RA Roberts J.A., Bottrill A.R., Mistry S., Evans R.J.;
RT "Mass spectrometry analysis of human P2X1 receptors; insight into
RT phosphorylation, modelling and conformational changes.";
RL J. Neurochem. 123:725-735(2012).
RN [8]
RP VARIANT LEU-351 DEL, AND CHARACTERIZATION OF VARIANT LEU-351 DEL.
RX PubMed=10816552; DOI=10.1074/jbc.c000305200;
RA Oury C., Toth-Zsamboki E., Van Geet C., Thys C., Wei L., Nilius B.,
RA Vermylen J., Hoylaerts M.F.;
RT "A natural dominant negative P2X1 receptor due to deletion of a single
RT amino acid residue.";
RL J. Biol. Chem. 275:22611-22614(2000).
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 (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Homo- or heteropolymers. {ECO:0000250}.
CC -!- INTERACTION:
CC P51575; Q9BQA9: CYBC1; NbExp=5; IntAct=EBI-11599725, EBI-2680384;
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the P2X receptor family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Wikipedia; Note=P2X receptor entry;
CC URL="https://en.wikipedia.org/wiki/P2X_receptor";
CC -!- WEB RESOURCE: Name=Wikipedia; Note=P2RX1 entry;
CC URL="https://en.wikipedia.org/wiki/P2RX1";
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DR EMBL; X83688; CAA58657.1; -; mRNA.
DR EMBL; U45448; AAC50698.1; -; mRNA.
DR EMBL; AF020498; AAC24494.1; -; mRNA.
DR EMBL; BC044657; AAH44657.1; -; mRNA.
DR EMBL; AF177472; AAD55395.1; -; Genomic_DNA.
DR CCDS; CCDS11040.1; -.
DR PIR; S71927; S71927.
DR RefSeq; NP_002549.1; NM_002558.3.
DR AlphaFoldDB; P51575; -.
DR SMR; P51575; -.
DR BioGRID; 111062; 36.
DR IntAct; P51575; 17.
DR STRING; 9606.ENSP00000225538; -.
DR BindingDB; P51575; -.
DR ChEMBL; CHEMBL2094; -.
DR DrugBank; DB01069; Promethazine.
DR DrugCentral; P51575; -.
DR GuidetoPHARMACOLOGY; 478; -.
DR GlyGen; P51575; 4 sites.
DR iPTMnet; P51575; -.
DR PhosphoSitePlus; P51575; -.
DR BioMuta; P2RX1; -.
DR DMDM; 1709519; -.
DR EPD; P51575; -.
DR MassIVE; P51575; -.
DR PaxDb; P51575; -.
DR PeptideAtlas; P51575; -.
DR PRIDE; P51575; -.
DR ProteomicsDB; 56337; -.
DR Antibodypedia; 3473; 196 antibodies from 28 providers.
DR DNASU; 5023; -.
DR Ensembl; ENST00000225538.4; ENSP00000225538.3; ENSG00000108405.4.
DR GeneID; 5023; -.
DR KEGG; hsa:5023; -.
DR MANE-Select; ENST00000225538.4; ENSP00000225538.3; NM_002558.4; NP_002549.1.
DR UCSC; uc002fww.4; human.
DR CTD; 5023; -.
DR DisGeNET; 5023; -.
DR GeneCards; P2RX1; -.
DR HGNC; HGNC:8533; P2RX1.
DR HPA; ENSG00000108405; Tissue enhanced (bone marrow, pancreas, urinary bladder).
DR MIM; 600845; gene+phenotype.
DR neXtProt; NX_P51575; -.
DR OpenTargets; ENSG00000108405; -.
DR PharmGKB; PA32861; -.
DR VEuPathDB; HostDB:ENSG00000108405; -.
DR eggNOG; ENOG502QSUI; Eukaryota.
DR GeneTree; ENSGT01020000230351; -.
DR HOGENOM; CLU_034469_2_0_1; -.
DR InParanoid; P51575; -.
DR OMA; ARHFMEN; -.
DR OrthoDB; 1128763at2759; -.
DR PhylomeDB; P51575; -.
DR TreeFam; TF328633; -.
DR PathwayCommons; P51575; -.
DR Reactome; R-HSA-139853; Elevation of cytosolic Ca2+ levels.
DR Reactome; R-HSA-418346; Platelet homeostasis.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR SignaLink; P51575; -.
DR BioGRID-ORCS; 5023; 9 hits in 1078 CRISPR screens.
DR ChiTaRS; P2RX1; human.
DR GeneWiki; P2RX1; -.
DR GenomeRNAi; 5023; -.
DR Pharos; P51575; Tchem.
DR PRO; PR:P51575; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; P51575; protein.
DR Bgee; ENSG00000108405; Expressed in popliteal artery and 109 other tissues.
DR ExpressionAtlas; P51575; baseline and differential.
DR Genevisible; P51575; HS.
DR GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl.
DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR GO; GO:0005639; C:integral component of nuclear inner membrane; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR GO; GO:0099055; C:integral component of postsynaptic membrane; IEA:Ensembl.
DR GO; GO:0099059; C:integral component of presynaptic active zone membrane; IEA:Ensembl.
DR GO; GO:0045121; C:membrane raft; IEA:Ensembl.
DR GO; GO:0043005; C:neuron projection; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0032991; C:protein-containing complex; IEA:Ensembl.
DR GO; GO:0030667; C:secretory granule membrane; TAS:Reactome.
DR GO; GO:0035579; C:specific granule membrane; TAS:Reactome.
DR GO; GO:0005524; F:ATP binding; IEA:Ensembl.
DR GO; GO:0005261; F:cation channel activity; IDA:MGI.
DR GO; GO:0004931; F:extracellularly ATP-gated cation channel activity; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl.
DR GO; GO:0001614; F:purinergic nucleotide receptor activity; IDA:MGI.
DR GO; GO:0043924; F:suramin binding; IEA:Ensembl.
DR GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; IEA:Ensembl.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0046513; P:ceramide biosynthetic process; IEA:Ensembl.
DR GO; GO:0007320; P:insemination; IEA:Ensembl.
DR GO; GO:0006811; P:ion transport; IDA:MGI.
DR GO; GO:0019228; P:neuronal action potential; IEA:Ensembl.
DR GO; GO:0030168; P:platelet activation; IEA:Ensembl.
DR GO; GO:1905665; P:positive regulation of calcium ion import across plasma membrane; IEA:Ensembl.
DR GO; GO:0008217; P:regulation of blood pressure; IEA:Ensembl.
DR GO; GO:0099509; P:regulation of presynaptic cytosolic calcium ion concentration; IEA:Ensembl.
DR GO; GO:2000300; P:regulation of synaptic vesicle exocytosis; IEA:Ensembl.
DR GO; GO:0003056; P:regulation of vascular associated smooth muscle contraction; IEA:Ensembl.
DR GO; GO:0033198; P:response to ATP; IEA:Ensembl.
DR GO; GO:0002554; P:serotonin secretion by platelet; IEA:Ensembl.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR GO; GO:0035249; P:synaptic transmission, glutamatergic; IEA:Ensembl.
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 1: Evidence at protein level;
KW Apoptosis; Disease variant; Disulfide bond; Glycoprotein; Ion channel;
KW Ion transport; Ligand-gated ion channel; Membrane; Phosphoprotein;
KW Receptor; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..399
FT /note="P2X purinoceptor 1"
FT /id="PRO_0000161545"
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 MOD_RES 387
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:22971236"
FT MOD_RES 388
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:22971236"
FT MOD_RES 389
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:22971236"
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 242
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:0000269|PubMed:11809854"
FT DISULFID 126..149
FT /evidence="ECO:0000269|PubMed:11809854"
FT DISULFID 132..159
FT /evidence="ECO:0000269|PubMed:11809854"
FT DISULFID 217..227
FT /evidence="ECO:0000269|PubMed:11809854"
FT DISULFID 261..270
FT /evidence="ECO:0000269|PubMed:11809854"
FT VARIANT 351
FT /note="Missing (in one patient presenting with severe
FT bleeding; somatic mutation; results in a non-functional
FT channel; dbSNP:rs587776702)"
FT /evidence="ECO:0000269|PubMed:10816552"
FT /id="VAR_025382"
FT VARIANT 396
FT /note="M -> V (in dbSNP:rs34617528)"
FT /id="VAR_053552"
SQ SEQUENCE 399 AA; 44980 MW; 8365466665522BF8 CRC64;
MARRFQEELA AFLFEYDTPR MVLVRNKKVG VIFRLIQLVV LVYVIGWVFL YEKGYQTSSG
LISSVSVKLK GLAVTQLPGL GPQVWDVADY VFPAQGDNSF VVMTNFIVTP KQTQGYCAEH
PEGGICKEDS GCTPGKAKRK AQGIRTGKCV AFNDTVKTCE IFGWCPVEVD DDIPRPALLR
EAENFTLFIK NSISFPRFKV NRRNLVEEVN AAHMKTCLFH KTLHPLCPVF QLGYVVQESG
QNFSTLAEKG GVVGITIDWH CDLDWHVRHC RPIYEFHGLY EEKNLSPGFN FRFARHFVEN
GTNYRHLFKV FGIRFDILVD GKAGKFDIIP TMTTIGSGIG IFGVATVLCD LLLLHILPKR
HYYKQKKFKY AEDMGPGAAE RDLAATSSTL GLQENMRTS
