P2RX5_HUMAN
ID P2RX5_HUMAN Reviewed; 422 AA.
AC Q93086; G5E981; O43450; O75540; Q308M5; Q59F38; Q8IXW4; Q93087; Q9NZV0;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 4.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=P2X purinoceptor 5;
DE Short=P2X5;
DE AltName: Full=ATP receptor;
DE AltName: Full=Purinergic receptor;
GN Name=P2RX5; Synonyms=P2X5;
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] (ISOFORMS 2 AND 3).
RA Tokuyama Y., Mereu L., Chen X., Rouard M., Bell G.I.;
RT "Cloning of human P2X purinoceptor new subtype (P2X5).";
RL Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=9414125; DOI=10.1016/s0014-5793(97)01380-x;
RA Le K.-T., Paquet M., Nouel D., Babinski K., Seguela P.;
RT "Primary structure and expression of a naturally truncated human P2X ATP
RT receptor subunit from brain and immune system.";
RL FEBS Lett. 418:195-199(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10673275; DOI=10.1101/gr.10.2.165;
RA Touchman J.W., Anikster Y., Dietrich N.L., Maduro V.V.B., McDowell G.,
RA Shotelersuk V., Bouffard G.G., Beckstrom-Sternberg S.M., Gahl W.A.,
RA Green E.D.;
RT "The genomic region encompassing the nephropathic cystinosis gene (CTNS):
RT complete sequencing of a 200-kb segment and discovery of a novel gene
RT within the common cystinosis-causing deletion.";
RL Genome Res. 10:165-173(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Brain;
RA Yu W., Gibbs R.A.;
RL Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5).
RA Li H., Nong W., Zhou G., Ke R., Shen C., Zhong G., Zheng Z., Liang M.,
RA Tang Z., Huang B., Lin L., Yang S.;
RL Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Erythroleukemia, and Mesangial cell;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC TISSUE=Spleen;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA Ohara O., Nagase T., Kikuno R.F.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Leukocyte, and Lung;
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).
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q93086-3; Sequence=Displayed;
CC Name=2; Synonyms=A;
CC IsoId=Q93086-1; Sequence=VSP_035587;
CC Name=3; Synonyms=B;
CC IsoId=Q93086-2; Sequence=VSP_004503, VSP_035587;
CC Name=4;
CC IsoId=Q93086-4; Sequence=VSP_035588;
CC Name=5;
CC IsoId=Q93086-5; Sequence=VSP_004503;
CC -!- TISSUE SPECIFICITY: Expressed at high levels in brain and immune
CC system.
CC -!- MISCELLANEOUS: [Isoform 4]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the P2X receptor family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF43106.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AK307959; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAD92860.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BC028084; Type=Frameshift; Evidence={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; U49395; AAB08576.1; -; mRNA.
DR EMBL; U49396; AAB08577.1; -; mRNA.
DR EMBL; AF016709; AAC51931.1; -; mRNA.
DR EMBL; AF168787; AAF43105.1; -; Genomic_DNA.
DR EMBL; AF168787; AAF43106.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AF070573; AAC28645.1; -; mRNA.
DR EMBL; DQ234349; ABB29978.1; -; mRNA.
DR EMBL; AK290889; BAF83578.1; -; mRNA.
DR EMBL; AK307959; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AB209623; BAD92860.1; ALT_FRAME; mRNA.
DR EMBL; AC132942; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471108; EAW90483.1; -; Genomic_DNA.
DR EMBL; BC028084; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC039015; AAH39015.1; -; mRNA.
DR CCDS; CCDS11034.1; -. [Q93086-3]
DR CCDS; CCDS11035.1; -. [Q93086-2]
DR CCDS; CCDS56014.1; -. [Q93086-5]
DR CCDS; CCDS56015.1; -. [Q93086-1]
DR RefSeq; NP_001191448.1; NM_001204519.1. [Q93086-1]
DR RefSeq; NP_001191449.1; NM_001204520.1. [Q93086-5]
DR RefSeq; NP_002552.2; NM_002561.3. [Q93086-3]
DR RefSeq; NP_778255.1; NM_175080.2. [Q93086-2]
DR AlphaFoldDB; Q93086; -.
DR SMR; Q93086; -.
DR BioGRID; 111065; 70.
DR IntAct; Q93086; 25.
DR STRING; 9606.ENSP00000225328; -.
DR BindingDB; Q93086; -.
DR ChEMBL; CHEMBL4942; -.
DR DrugBank; DB01069; Promethazine.
DR TCDB; 1.A.7.1.11; the atp-gated p2x receptor cation channel (p2x receptor) family.
DR GlyGen; Q93086; 3 sites.
DR iPTMnet; Q93086; -.
DR PhosphoSitePlus; Q93086; -.
DR BioMuta; P2RX5; -.
DR DMDM; 209572778; -.
DR jPOST; Q93086; -.
DR MassIVE; Q93086; -.
DR MaxQB; Q93086; -.
DR PaxDb; Q93086; -.
DR PeptideAtlas; Q93086; -.
DR PRIDE; Q93086; -.
DR ProteomicsDB; 33860; -.
DR ProteomicsDB; 75715; -. [Q93086-3]
DR ProteomicsDB; 75716; -. [Q93086-1]
DR ProteomicsDB; 75717; -. [Q93086-2]
DR ProteomicsDB; 75718; -. [Q93086-4]
DR Antibodypedia; 10941; 224 antibodies from 27 providers.
DR DNASU; 5026; -.
DR Ensembl; ENST00000225328.10; ENSP00000225328.5; ENSG00000083454.22. [Q93086-3]
DR Ensembl; ENST00000345901.7; ENSP00000342161.3; ENSG00000083454.22. [Q93086-5]
DR Ensembl; ENST00000547178.5; ENSP00000448355.1; ENSG00000083454.22. [Q93086-1]
DR Ensembl; ENST00000551178.5; ENSP00000447545.1; ENSG00000083454.22. [Q93086-2]
DR GeneID; 5026; -.
DR KEGG; hsa:5026; -.
DR MANE-Select; ENST00000225328.10; ENSP00000225328.5; NM_002561.4; NP_002552.2.
DR UCSC; uc002fwi.4; human. [Q93086-3]
DR CTD; 5026; -.
DR DisGeNET; 5026; -.
DR GeneCards; P2RX5; -.
DR HGNC; HGNC:8536; P2RX5.
DR HPA; ENSG00000083454; Tissue enhanced (intestine, lymphoid tissue).
DR MIM; 602836; gene.
DR neXtProt; NX_Q93086; -.
DR OpenTargets; ENSG00000083454; -.
DR PharmGKB; PA32865; -.
DR VEuPathDB; HostDB:ENSG00000083454; -.
DR eggNOG; ENOG502QSUI; Eukaryota.
DR GeneTree; ENSGT01020000230351; -.
DR InParanoid; Q93086; -.
DR OMA; KVLDGRC; -.
DR OrthoDB; 1128763at2759; -.
DR PhylomeDB; Q93086; -.
DR TreeFam; TF328633; -.
DR PathwayCommons; Q93086; -.
DR Reactome; R-HSA-139853; Elevation of cytosolic Ca2+ levels.
DR Reactome; R-HSA-418346; Platelet homeostasis.
DR SignaLink; Q93086; -.
DR BioGRID-ORCS; 5026; 15 hits in 1066 CRISPR screens.
DR GeneWiki; P2RX5; -.
DR GenomeRNAi; 5026; -.
DR Pharos; Q93086; Tchem.
DR PRO; PR:Q93086; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q93086; protein.
DR Bgee; ENSG00000083454; Expressed in spleen and 141 other tissues.
DR ExpressionAtlas; Q93086; baseline and differential.
DR Genevisible; Q93086; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
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:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0098794; C:postsynapse; IEA:GOC.
DR GO; GO:0005524; F:ATP binding; NAS:BHF-UCL.
DR GO; GO:0004931; F:extracellularly ATP-gated cation channel activity; IBA:GO_Central.
DR GO; GO:0005216; F:ion channel activity; TAS:ProtInc.
DR GO; GO:0001614; F:purinergic nucleotide receptor activity; NAS:BHF-UCL.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; TAS:ProtInc.
DR GO; GO:0007399; P:nervous system development; TAS:ProtInc.
DR GO; GO:0010524; P:positive regulation of calcium ion transport into cytosol; NAS:BHF-UCL.
DR GO; GO:0050850; P:positive regulation of calcium-mediated signaling; NAS:BHF-UCL.
DR GO; GO:0033198; P:response to ATP; IEA:InterPro.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
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 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..422
FT /note="P2X purinoceptor 5"
FT /id="PRO_0000161555"
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..319
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 320..340
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 341..422
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 356..422
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 396..422
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 77
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 VAR_SEQ 97..120
FT /note="Missing (in isoform 3 and isoform 5)"
FT /evidence="ECO:0000303|Ref.1, ECO:0000303|Ref.4,
FT ECO:0000303|Ref.5"
FT /id="VSP_004503"
FT VAR_SEQ 205..206
FT /note="KS -> N (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:9414125, ECO:0000303|Ref.1,
FT ECO:0000303|Ref.4"
FT /id="VSP_035587"
FT VAR_SEQ 421..422
FT /note="ST -> LRTPSASPLHQE (in isoform 4)"
FT /evidence="ECO:0000303|Ref.7"
FT /id="VSP_035588"
FT CONFLICT 96
FT /note="Q -> E (in Ref. 1; AAB08577)"
FT /evidence="ECO:0000305"
FT CONFLICT 97..98
FT /note="GE -> EK (in Ref. 1; AAB08576)"
FT /evidence="ECO:0000305"
FT CONFLICT 156
FT /note="E -> G (in Ref. 2; AAC51931)"
FT /evidence="ECO:0000305"
FT CONFLICT 237..238
FT /note="VI -> IV (in Ref. 2; AAC51931)"
FT /evidence="ECO:0000305"
FT CONFLICT 251
FT /note="E -> R (in Ref. 2; AAC51931)"
FT /evidence="ECO:0000305"
FT CONFLICT 330
FT /note="F -> S (in Ref. 1; AAB08576/AAB08577)"
FT /evidence="ECO:0000305"
FT CONFLICT 350
FT /note="K -> R (in Ref. 5; ABB29978)"
FT /evidence="ECO:0000305"
FT CONFLICT 352
FT /note="E -> Q (in Ref. 1; AAB08576/AAB08577)"
FT /evidence="ECO:0000305"
FT CONFLICT 399..400
FT /note="KR -> NV (in Ref. 1; AAB08576/AAB08577)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 422 AA; 47205 MW; B122027A23B2A240 CRC64;
MGQAGCKGLC LSLFDYKTEK YVIAKNKKVG LLYRLLQASI LAYLVVWVFL IKKGYQDVDT
SLQSAVITKV KGVAFTNTSD LGQRIWDVAD YVIPAQGENV FFVVTNLIVT PNQRQNVCAE
NEGIPDGACS KDSDCHAGEA VTAGNGVKTG RCLRRENLAR GTCEIFAWCP LETSSRPEEP
FLKEAEDFTI FIKNHIRFPK FNFSKSNVMD VKDRSFLKSC HFGPKNHYCP IFRLGSVIRW
AGSDFQDIAL EGGVIGINIE WNCDLDKAAS ECHPHYSFSR LDNKLSKSVS SGYNFRFARY
YRDAAGVEFR TLMKAYGIRF DVMVNGKGAF FCDLVLIYLI KKREFYRDKK YEEVRGLEDS
SQEAEDEASG LGLSEQLTSG PGLLGMPEQQ ELQEPPEAKR GSSSQKGNGS VCPQLLEPHR
ST
