P2RX4_HUMAN
ID P2RX4_HUMAN Reviewed; 388 AA.
AC Q99571; E7EPF7; F6RU17; O00450; O14722; Q5U089; Q5U090; Q8N4N1; Q9UBG9;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 196.
DE RecName: Full=P2X purinoceptor 4;
DE Short=P2X4;
DE AltName: Full=ATP receptor;
DE AltName: Full=Purinergic receptor;
GN Name=P2RX4;
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] (ISOFORM 1), AND VARIANT SER-6.
RC TISSUE=Brain;
RX PubMed=9016352; DOI=10.1124/mol.51.1.109;
RA Garcia-Guzman M., Soto F., Gomez-Hernandez J.M., Lund P.E., Stuhmer W.;
RT "Characterization of recombinant human P2X4 receptor reveals
RT pharmacological differences to the rat homologue.";
RL Mol. Pharmacol. 51:109-118(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
RA Yamagata K., Oda N., Furuta H., Vaxillaire M., Southam L., Boriraj V.,
RA Chen X., Oda Y., Takeda J., Yamada S., Nishigori H., Lebeau M.M.,
RA Lathrop M., Cox R.D., Bell G.I.;
RT "Transcription map of the 5cM region surrounding the hepatocyte nuclear
RT factor-1a/MODY3 gene on chromosome 12.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), AND VARIANT SER-6.
RA Korenaga R., Yamamoto K., Kamiya A., Ando J.;
RT "Shear stress downregulates the expression of P2X4 receptor by human
RT endothelial cells.";
RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3), AND VARIANT
RP SER-6.
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT GLY-242.
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 [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 35-388 (ISOFORM 1), AND VARIANT CYS-315.
RA Takahashi K., Korenaga R., Kamiya A., Ando J.;
RT "Human P2X purinoceptor.";
RL Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 73-326 (ISOFORM 1).
RC TISSUE=Kidney;
RA Chang A.S., Chang S.M.;
RT "Cloning of P2X4 cDNA from human embryonic kidney (HEK) 293 cells.";
RL Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP ALTERNATIVE SPLICING (ISOFORMS 1 AND 2), FUNCTION, AND SUBCELLULAR
RP LOCATION.
RX PubMed=10515189; DOI=10.1016/s0304-3940(99)00653-9;
RA Carpenter D., Meadows H.J., Brough S., Chapman G., Clarke C., Coldwell M.,
RA Davis R., Harrison D., Meakin J., McHale M., Rice S.Q., Tomlinson W.J.,
RA Wood M., Sanger G.J.;
RT "Site-specific splice variation of the human P2X4 receptor.";
RL Neurosci. Lett. 273:183-186(1999).
RN [10]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-184.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [11]
RP INTERACTION WITH P2X7.
RX PubMed=26456657; DOI=10.1016/j.bbrc.2015.10.025;
RA Perez-Flores G., Levesque S.A., Pacheco J., Vaca L., Lacroix S.,
RA Perez-Cornejo P., Arreola J.;
RT "The P2X7/P2X4 interaction shapes the purinergic response in murine
RT macrophages.";
RL Biochem. Biophys. Res. Commun. 467:484-490(2015).
RN [12]
RP FUNCTION.
RX PubMed=35165166; DOI=10.4049/jimmunol.2100550;
RA Hamoudi C., Zhao C., Abderrazak A., Salem M., Fortin P.R., Sevigny J.,
RA Aoudjit F.;
RT "The Purinergic Receptor P2X4 Promotes Th17 Activation and the Development
RT of Arthritis.";
RL J. Immunol. 208:1115-1127(2022).
RN [13]
RP VARIANTS GLY-242 AND CYS-315, CHARACTERIZATION OF VARIANTS SER-6; GLY-242
RP AND CYS-315, MUTAGENESIS OF ILE-119, AND FUNCTION.
RX PubMed=22068874; DOI=10.1161/hypertensionaha.111.176180;
RA Stokes L., Scurrah K., Ellis J.A., Cromer B.A., Skarratt K.K., Gu B.J.,
RA Harrap S.B., Wiley J.S.;
RT "A loss-of-function polymorphism in the human P2X4 receptor is associated
RT with increased pulse pressure.";
RL Hypertension 58:1086-1092(2011).
RN [14]
RP VARIANT CYS-315, CHARACTERIZATION OF VARIANT CYS-315, AND SUBCELLULAR
RP LOCATION.
RX PubMed=23303206; DOI=10.1096/fj.12-215368;
RA Gu B.J., Baird P.N., Vessey K.A., Skarratt K.K., Fletcher E.L.,
RA Fuller S.J., Richardson A.J., Guymer R.H., Wiley J.S.;
RT "A rare functional haplotype of the P2RX4 and P2RX7 genes leads to loss of
RT innate phagocytosis and confers increased risk of age-related macular
RT degeneration.";
RL FASEB J. 27:1479-1487(2013).
RN [15]
RP VARIANTS CYS-3; SER-135; GLY-242 AND CYS-315, CHARACTERIZATION OF VARIANT
RP SER-135, SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=28326637; DOI=10.1002/humu.23218;
RA Sadovnick A.D., Gu B.J., Traboulsee A.L., Bernales C.Q., Encarnacion M.,
RA Yee I.M., Criscuoli M.G., Huang X., Ou A., Milligan C.J., Petrou S.,
RA Wiley J.S., Vilarino-Gueell C.;
RT "Purinergic receptors P2RX4 and P2RX7 in familial multiple sclerosis.";
RL Hum. Mutat. 38:736-744(2017).
CC -!- FUNCTION: Receptor for extracellularly released ATP acting as a ligand-
CC gated ion channel that plays multiple role in immunity and central
CC nervous system physiology (PubMed:35165166). Plays a key role in
CC initial steps of T-cell activation and Ca(2+) microdomain formation (By
CC similarity). Participates also in basal T-cell activity without TCR/CD3
CC stimulation (By similarity). Promotes the differentiation and
CC activation of Th17 cells via expression of retinoic acid-related orphan
CC receptor C/RORC (PubMed:35165166). Upon activation, drives microglia
CC motility via the PI3K/Akt pathway (By similarity).
CC {ECO:0000250|UniProtKB:P51577, ECO:0000250|UniProtKB:Q9JJX6,
CC ECO:0000269|PubMed:35165166}.
CC -!- SUBUNIT: Functional P2XRs are organized as homomeric and heteromeric
CC trimers. Interacts with P2X7 (via C-terminus); this interaction is
CC functional only in the presence of ATP (PubMed:26456657). Interacts
CC with AP1M2 (By similarity). {ECO:0000250|UniProtKB:P51577,
CC ECO:0000269|PubMed:26456657}.
CC -!- INTERACTION:
CC Q99571; Q9NQM4: DNAAF6; NbExp=3; IntAct=EBI-2828248, EBI-10239299;
CC Q99571; Q07627: KRTAP1-1; NbExp=3; IntAct=EBI-2828248, EBI-11959885;
CC Q99571; P60328: KRTAP12-3; NbExp=3; IntAct=EBI-2828248, EBI-11953334;
CC Q99571; P26371: KRTAP5-9; NbExp=3; IntAct=EBI-2828248, EBI-3958099;
CC Q99571; Q7Z3S9: NOTCH2NLA; NbExp=3; IntAct=EBI-2828248, EBI-945833;
CC Q99571; P0DPK4: NOTCH2NLC; NbExp=3; IntAct=EBI-2828248, EBI-22310682;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:10515189,
CC ECO:0000269|PubMed:23303206, ECO:0000269|PubMed:28326637}; Multi-pass
CC membrane protein {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q99571-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q99571-2; Sequence=VSP_053812;
CC Name=3;
CC IsoId=Q99571-3; Sequence=VSP_053813;
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";
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DR EMBL; Y07684; CAA68948.1; -; mRNA.
DR EMBL; U87270; AAD00556.1; -; Genomic_DNA.
DR EMBL; U85971; AAD00556.1; JOINED; Genomic_DNA.
DR EMBL; U85972; AAD00556.1; JOINED; Genomic_DNA.
DR EMBL; U85973; AAD00556.1; JOINED; Genomic_DNA.
DR EMBL; U85974; AAD00556.1; JOINED; Genomic_DNA.
DR EMBL; U85975; AAD00556.1; JOINED; Genomic_DNA.
DR EMBL; U83993; AAD00553.1; -; mRNA.
DR EMBL; AF191093; AAF06661.1; -; Genomic_DNA.
DR EMBL; BT019738; AAV38543.1; -; mRNA.
DR EMBL; BT019739; AAV38544.1; -; mRNA.
DR EMBL; AC069209; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC033826; AAH33826.1; -; mRNA.
DR EMBL; AF000234; AAB58405.1; -; mRNA.
DR EMBL; AF012903; AAB66834.1; -; mRNA.
DR CCDS; CCDS58282.1; -. [Q99571-2]
DR CCDS; CCDS9214.1; -. [Q99571-1]
DR RefSeq; NP_001243725.1; NM_001256796.1. [Q99571-2]
DR RefSeq; NP_001248326.1; NM_001261397.1. [Q99571-3]
DR RefSeq; NP_002551.2; NM_002560.2. [Q99571-1]
DR AlphaFoldDB; Q99571; -.
DR SMR; Q99571; -.
DR BioGRID; 111064; 47.
DR IntAct; Q99571; 26.
DR STRING; 9606.ENSP00000353032; -.
DR BindingDB; Q99571; -.
DR ChEMBL; CHEMBL2104; -.
DR DrugBank; DB14575; Eslicarbazepine.
DR DrugBank; DB09119; Eslicarbazepine acetate.
DR DrugBank; DB01069; Promethazine.
DR DrugCentral; Q99571; -.
DR GuidetoPHARMACOLOGY; 481; -.
DR TCDB; 1.A.7.1.5; the atp-gated p2x receptor cation channel (p2x receptor) family.
DR GlyConnect; 1590; 12 N-Linked glycans (4 sites).
DR GlyGen; Q99571; 6 sites, 11 N-linked glycans (4 sites).
DR iPTMnet; Q99571; -.
DR PhosphoSitePlus; Q99571; -.
DR BioMuta; P2RX4; -.
DR DMDM; 116242696; -.
DR EPD; Q99571; -.
DR jPOST; Q99571; -.
DR MassIVE; Q99571; -.
DR MaxQB; Q99571; -.
DR PaxDb; Q99571; -.
DR PeptideAtlas; Q99571; -.
DR PRIDE; Q99571; -.
DR ProteomicsDB; 17348; -.
DR ProteomicsDB; 27898; -.
DR ProteomicsDB; 78331; -. [Q99571-1]
DR Antibodypedia; 31537; 270 antibodies from 35 providers.
DR DNASU; 5025; -.
DR Ensembl; ENST00000337233.9; ENSP00000336607.4; ENSG00000135124.16. [Q99571-1]
DR Ensembl; ENST00000359949.11; ENSP00000353032.7; ENSG00000135124.16. [Q99571-2]
DR Ensembl; ENST00000542067.5; ENSP00000438329.1; ENSG00000135124.16. [Q99571-3]
DR GeneID; 5025; -.
DR KEGG; hsa:5025; -.
DR MANE-Select; ENST00000337233.9; ENSP00000336607.4; NM_002560.3; NP_002551.2.
DR UCSC; uc001tzr.4; human. [Q99571-1]
DR CTD; 5025; -.
DR DisGeNET; 5025; -.
DR GeneCards; P2RX4; -.
DR HGNC; HGNC:8535; P2RX4.
DR HPA; ENSG00000135124; Low tissue specificity.
DR MIM; 600846; gene.
DR neXtProt; NX_Q99571; -.
DR OpenTargets; ENSG00000135124; -.
DR PharmGKB; PA32864; -.
DR VEuPathDB; HostDB:ENSG00000135124; -.
DR eggNOG; ENOG502QSUI; Eukaryota.
DR GeneTree; ENSGT01020000230351; -.
DR InParanoid; Q99571; -.
DR OMA; QGYCPEL; -.
DR OrthoDB; 1128763at2759; -.
DR PhylomeDB; Q99571; -.
DR TreeFam; TF328633; -.
DR PathwayCommons; Q99571; -.
DR Reactome; R-HSA-139853; Elevation of cytosolic Ca2+ levels.
DR Reactome; R-HSA-418346; Platelet homeostasis.
DR Reactome; R-HSA-9660826; Purinergic signaling in leishmaniasis infection.
DR SignaLink; Q99571; -.
DR BioGRID-ORCS; 5025; 10 hits in 1078 CRISPR screens.
DR ChiTaRS; P2RX4; human.
DR GeneWiki; P2RX4; -.
DR GenomeRNAi; 5025; -.
DR Pharos; Q99571; Tchem.
DR PRO; PR:Q99571; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q99571; protein.
DR Bgee; ENSG00000135124; Expressed in mucosa of transverse colon and 158 other tissues.
DR ExpressionAtlas; Q99571; baseline and differential.
DR Genevisible; Q99571; HS.
DR GO; GO:0044297; C:cell body; ISS:ARUK-UCL.
DR GO; GO:0030054; C:cell junction; IDA:BHF-UCL.
DR GO; GO:0043197; C:dendritic spine; IEA:Ensembl.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
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:0005765; C:lysosomal membrane; HDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IDA:BHF-UCL.
DR GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:BHF-UCL.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0014069; C:postsynaptic density; IEA:Ensembl.
DR GO; GO:0043195; C:terminal bouton; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IC:BHF-UCL.
DR GO; GO:0045296; F:cadherin binding; IPI:BHF-UCL.
DR GO; GO:0005507; F:copper ion binding; ISS:BHF-UCL.
DR GO; GO:0004931; F:extracellularly ATP-gated cation channel activity; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:BHF-UCL.
DR GO; GO:0099604; F:ligand-gated calcium channel activity; IDA:BHF-UCL.
DR GO; GO:0001614; F:purinergic nucleotide receptor activity; IDA:BHF-UCL.
DR GO; GO:0005102; F:signaling receptor binding; ISS:BHF-UCL.
DR GO; GO:0008270; F:zinc ion binding; ISS:BHF-UCL.
DR GO; GO:0097190; P:apoptotic signaling pathway; IDA:BHF-UCL.
DR GO; GO:0048266; P:behavioral response to pain; ISS:ARUK-UCL.
DR GO; GO:0070588; P:calcium ion transmembrane transport; IDA:BHF-UCL.
DR GO; GO:0019722; P:calcium-mediated signaling; TAS:ARUK-UCL.
DR GO; GO:0071318; P:cellular response to ATP; IDA:UniProtKB.
DR GO; GO:0071294; P:cellular response to zinc ion; ISS:UniProtKB.
DR GO; GO:0042118; P:endothelial cell activation; TAS:BHF-UCL.
DR GO; GO:0034220; P:ion transmembrane transport; IDA:UniProtKB.
DR GO; GO:0051899; P:membrane depolarization; IDA:BHF-UCL.
DR GO; GO:0010614; P:negative regulation of cardiac muscle hypertrophy; IMP:BHF-UCL.
DR GO; GO:0019228; P:neuronal action potential; IEA:Ensembl.
DR GO; GO:0043536; P:positive regulation of blood vessel endothelial cell migration; IMP:CAFA.
DR GO; GO:0051928; P:positive regulation of calcium ion transport; NAS:BHF-UCL.
DR GO; GO:0010524; P:positive regulation of calcium ion transport into cytosol; IDA:BHF-UCL.
DR GO; GO:0050850; P:positive regulation of calcium-mediated signaling; IDA:BHF-UCL.
DR GO; GO:2001028; P:positive regulation of endothelial cell chemotaxis; IMP:CAFA.
DR GO; GO:1904141; P:positive regulation of microglial cell migration; ISS:ARUK-UCL.
DR GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; NAS:BHF-UCL.
DR GO; GO:0032308; P:positive regulation of prostaglandin secretion; NAS:BHF-UCL.
DR GO; GO:0051897; P:positive regulation of protein kinase B signaling; ISS:ARUK-UCL.
DR GO; GO:0035590; P:purinergic nucleotide receptor signaling pathway; IMP:BHF-UCL.
DR GO; GO:0008217; P:regulation of blood pressure; IMP:BHF-UCL.
DR GO; GO:0055117; P:regulation of cardiac muscle contraction; IMP:BHF-UCL.
DR GO; GO:0050920; P:regulation of chemotaxis; ISS:ARUK-UCL.
DR GO; GO:0002028; P:regulation of sodium ion transport; ISS:BHF-UCL.
DR GO; GO:0055119; P:relaxation of cardiac muscle; IMP:BHF-UCL.
DR GO; GO:0033198; P:response to ATP; IDA:BHF-UCL.
DR GO; GO:0048678; P:response to axon injury; ISS:ARUK-UCL.
DR GO; GO:0034405; P:response to fluid shear stress; IDA:BHF-UCL.
DR GO; GO:0002931; P:response to ischemia; ISS:ARUK-UCL.
DR GO; GO:0019233; P:sensory perception of pain; ISS:ARUK-UCL.
DR GO; GO:0050975; P:sensory perception of touch; ISS:ARUK-UCL.
DR GO; GO:0007165; P:signal transduction; IDA:BHF-UCL.
DR GO; GO:0001894; P:tissue homeostasis; NAS:BHF-UCL.
DR Gene3D; 2.60.490.10; -; 1.
DR InterPro; IPR003047; P2X4_purnocptor.
DR InterPro; IPR027309; P2X_extracellular_dom_sf.
DR InterPro; IPR001429; P2X_purnocptor.
DR PIRSF; PIRSF005713; P2X_purinoceptor; 1.
DR PRINTS; PR01311; P2X4RECEPTOR.
DR PRINTS; PR01307; P2XRECEPTOR.
DR TIGRFAMs; TIGR00863; P2X; 1.
DR PROSITE; PS01212; P2X_RECEPTOR; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Disulfide bond; Glycoprotein; Ion channel;
KW Ion transport; Ligand-gated ion channel; Membrane; Receptor;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..388
FT /note="P2X purinoceptor 4"
FT /id="PRO_0000161553"
FT TOPO_DOM 1..33
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 34..54
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 55..338
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 339..359
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 360..388
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 75
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 110
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
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:0000269|PubMed:19159218"
FT CARBOHYD 199
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 208
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 116..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 VAR_SEQ 45
FT /note="G -> GCYHPHLAEVEMESPRR (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_053812"
FT VAR_SEQ 149..175
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_053813"
FT VARIANT 3
FT /note="G -> C (in dbSNP:rs200492184)"
FT /evidence="ECO:0000269|PubMed:28326637"
FT /id="VAR_079856"
FT VARIANT 6
FT /note="A -> S (does not change ATP-induced inward current;
FT does not change affinity for ATP; dbSNP:rs1044249)"
FT /evidence="ECO:0000269|PubMed:22068874,
FT ECO:0000269|PubMed:9016352, ECO:0000269|Ref.3,
FT ECO:0000269|Ref.4"
FT /id="VAR_028307"
FT VARIANT 135
FT /note="G -> S (does not change protein expression; does not
FT affect membrane subcellular location; increases ATP-induced
FT inward current; dbSNP:rs765866317)"
FT /evidence="ECO:0000269|PubMed:28326637"
FT /id="VAR_079857"
FT VARIANT 242
FT /note="S -> G (does not change ATP-induced inward current;
FT does not change affinity for ATP; dbSNP:rs25644)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:22068874, ECO:0000269|PubMed:28326637"
FT /id="VAR_014942"
FT VARIANT 315
FT /note="Y -> C (may influence susceptibility to multiple
FT sclerosis in the presence of variants M-205 and S-361 in
FT P2RX7; does not affect membrane subcellular location;
FT reduces ATP-induced inward current; decreases affinity for
FT ATP; dbSNP:rs28360472)"
FT /evidence="ECO:0000269|PubMed:22068874,
FT ECO:0000269|PubMed:23303206, ECO:0000269|PubMed:28326637,
FT ECO:0000269|Ref.7"
FT /id="VAR_079858"
FT MUTAGEN 119
FT /note="I->V: Does not change ATP-induced inward current.
FT Does not change affinity for ATP."
FT /evidence="ECO:0000269|PubMed:22068874"
FT CONFLICT 121
FT /note="D -> S (in Ref. 8; AAB66834)"
FT /evidence="ECO:0000305"
FT CONFLICT 148
FT /note="R -> W (in Ref. 8; AAB66834)"
FT /evidence="ECO:0000305"
FT CONFLICT 179
FT /note="L -> F (in Ref. 8; AAB66834)"
FT /evidence="ECO:0000305"
FT CONFLICT 238
FT /note="N -> I (in Ref. 8; AAB66834)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 388 AA; 43369 MW; BA3BE7F30114C2A5 CRC64;
MAGCCAALAA FLFEYDTPRI VLIRSRKVGL MNRAVQLLIL AYVIGWVFVW EKGYQETDSV
VSSVTTKVKG VAVTNTSKLG FRIWDVADYV IPAQEENSLF VMTNVILTMN QTQGLCPEIP
DATTVCKSDA SCTAGSAGTH SNGVSTGRCV AFNGSVKTCE VAAWCPVEDD THVPQPAFLK
AAENFTLLVK NNIWYPKFNF SKRNILPNIT TTYLKSCIYD AKTDPFCPIF RLGKIVENAG
HSFQDMAVEG GIMGIQVNWD CNLDRAASLC LPRYSFRRLD TRDVEHNVSP GYNFRFAKYY
RDLAGNEQRT LIKAYGIRFD IIVFGKAGKF DIIPTMINIG SGLALLGMAT VLCDIIVLYC
MKKRLYYREK KYKYVEDYEQ GLASELDQ
