ID   P2RY8_HUMAN             Reviewed;         359 AA.
AC   Q86VZ1;
DT   07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   27-MAR-2024, entry version 160.
DE   RecName: Full=P2Y purinoceptor 8;
DE            Short=P2Y8;
GN   Name=P2RY8;
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 [LARGE SCALE GENOMIC DNA].
RX   PubMed=15772651; DOI=10.1038/nature03440;
RA   Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA   Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA   Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA   Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA   Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA   Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA   Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA   Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA   Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA   Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA   Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA   Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA   Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA   Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA   Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA   Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA   Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA   Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA   Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA   Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA   Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA   Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA   Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA   Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA   Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA   Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA   Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA   Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA   Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA   Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA   McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA   Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA   Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA   Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA   Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA   Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA   Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA   Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA   Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA   Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA   d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA   Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA   Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA   Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA   Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA   Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA   Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA   Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA   Rogers J., Bentley D.R.;
RT   "The DNA sequence of the human X chromosome.";
RL   Nature 434:325-337(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Lymph;
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   TISSUE SPECIFICITY.
RX   PubMed=11004484; DOI=10.1016/s0167-4781(00)00094-4;
RA   Adrian K., Bernhard M.K., Breitinger H.-G., Ogilvie A.;
RT   "Expression of purinergic receptors (ionotropic P2X1-7 and metabotropic
RT   P2Y1-11) during myeloid differentiation of HL60 cells.";
RL   Biochim. Biophys. Acta 1492:127-138(2000).
RN   [4]
RP   TISSUE SPECIFICITY.
RX   PubMed=15466006; DOI=10.1136/jmg.2004.021626;
RA   Cantagrel V., Lossi A.-M., Boulanger S., Depetris D., Mattei M.-G.,
RA   Gecz J., Schwartz C.E., Van Maldergem L., Villard L.;
RT   "Disruption of a new X linked gene highly expressed in brain in a family
RT   with two mentally retarded males.";
RL   J. Med. Genet. 41:736-742(2004).
RN   [5]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-5 AND ASN-11.
RC   TISSUE=Leukemic T-cell;
RX   PubMed=19349973; DOI=10.1038/nbt.1532;
RA   Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA   Schiess R., Aebersold R., Watts J.D.;
RT   "Mass-spectrometric identification and relative quantification of N-linked
RT   cell surface glycoproteins.";
RL   Nat. Biotechnol. 27:378-386(2009).
CC   -!- FUNCTION: Probable receptor for purines coupled to G-proteins.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- TISSUE SPECIFICITY: Barely detectable in normal blood leukocytes.
CC       Weaker expression was seen in heart, kidney and lung. Not detected in
CC       brain. {ECO:0000269|PubMed:11004484, ECO:0000269|PubMed:15466006}.
CC   -!- INDUCTION: Down-regulated during granulocytic regulation.
CC   -!- MISCELLANEOUS: The gene coding for this protein is located in the
CC       pseudoautosomal region 1 (PAR1) of X and Y chromosomes.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR   EMBL; AL683870; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC043610; AAH43610.1; -; mRNA.
DR   CCDS; CCDS14115.1; -.
DR   RefSeq; NP_835230.1; NM_178129.4.
DR   RefSeq; XP_005274486.1; XM_005274429.3.
DR   RefSeq; XP_005274835.1; XM_005274778.3.
DR   RefSeq; XP_011543933.1; XM_011545631.2.
DR   RefSeq; XP_011543934.1; XM_011545632.2.
DR   RefSeq; XP_011544480.1; XM_011546178.2.
DR   RefSeq; XP_011544481.1; XM_011546179.2.
DR   AlphaFoldDB; Q86VZ1; -.
DR   SMR; Q86VZ1; -.
DR   BioGRID; 130402; 211.
DR   IntAct; Q86VZ1; 18.
DR   STRING; 9606.ENSP00000370697; -.
DR   ChEMBL; CHEMBL4523886; -.
DR   DrugBank; DB01069; Promethazine.
DR   GlyCosmos; Q86VZ1; 2 sites, No reported glycans.
DR   GlyGen; Q86VZ1; 2 sites.
DR   iPTMnet; Q86VZ1; -.
DR   PhosphoSitePlus; Q86VZ1; -.
DR   BioMuta; P2RY8; -.
DR   DMDM; 74762454; -.
DR   EPD; Q86VZ1; -.
DR   jPOST; Q86VZ1; -.
DR   MassIVE; Q86VZ1; -.
DR   MaxQB; Q86VZ1; -.
DR   PaxDb; 9606-ENSP00000370697; -.
DR   PeptideAtlas; Q86VZ1; -.
DR   ProteomicsDB; 70092; -.
DR   Antibodypedia; 588; 260 antibodies from 29 providers.
DR   DNASU; 286530; -.
DR   Ensembl; ENST00000381297.10; ENSP00000370697.4; ENSG00000182162.11.
DR   Ensembl; ENST00000711216.1; ENSP00000518611.1; ENSG00000292333.1.
DR   GeneID; 286530; -.
DR   KEGG; hsa:286530; -.
DR   MANE-Select; ENST00000381297.10; ENSP00000370697.4; NM_178129.5; NP_835230.1.
DR   UCSC; uc004cpz.3; human.
DR   AGR; HGNC:15524; -.
DR   CTD; 286530; -.
DR   DisGeNET; 286530; -.
DR   GeneCards; P2RY8; -.
DR   HGNC; HGNC:15524; P2RY8.
DR   HPA; ENSG00000182162; Group enriched (bone marrow, lymphoid tissue).
DR   MIM; 300525; gene.
DR   neXtProt; NX_Q86VZ1; -.
DR   OpenTargets; ENSG00000182162; -.
DR   PharmGKB; PA32873; -.
DR   VEuPathDB; HostDB:ENSG00000182162; -.
DR   eggNOG; ENOG502QW5Q; Eukaryota.
DR   GeneTree; ENSGT01050000244840; -.
DR   HOGENOM; CLU_009579_8_2_1; -.
DR   InParanoid; Q86VZ1; -.
DR   OMA; YMAYKLS; -.
DR   OrthoDB; 5315465at2759; -.
DR   PhylomeDB; Q86VZ1; -.
DR   TreeFam; TF330775; -.
DR   PathwayCommons; Q86VZ1; -.
DR   SignaLink; Q86VZ1; -.
DR   BioGRID-ORCS; 286530; 12 hits in 604 CRISPR screens.
DR   ChiTaRS; P2RY8; human.
DR   GeneWiki; P2RY8; -.
DR   GenomeRNAi; 286530; -.
DR   Pharos; Q86VZ1; Tbio.
DR   PRO; PR:Q86VZ1; -.
DR   Proteomes; UP000005640; Chromosome X.
DR   Proteomes; UP000005640; Chromosome Y.
DR   RNAct; Q86VZ1; Protein.
DR   Bgee; ENSG00000182162; Expressed in buccal mucosa cell and 118 other cell types or tissues.
DR   ExpressionAtlas; Q86VZ1; baseline and differential.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0045028; F:G protein-coupled purinergic nucleotide receptor activity; IEA:InterPro.
DR   GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central.
DR   GO; GO:0007200; P:phospholipase C-activating G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR   GO; GO:0035025; P:positive regulation of Rho protein signal transduction; IBA:GO_Central.
DR   CDD; cd15368; 7tmA_P2Y8; 1.
DR   Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
DR   InterPro; IPR000276; GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR   InterPro; IPR027669; P2Y8_rcpt.
DR   PANTHER; PTHR24232; G-PROTEIN COUPLED RECEPTOR; 1.
DR   PANTHER; PTHR24232:SF25; P2Y PURINOCEPTOR 8; 1.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PRINTS; PR01157; P2YPURNOCPTR.
DR   SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 1.
DR   PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
DR   Genevisible; Q86VZ1; HS.
PE   1: Evidence at protein level;
KW   Cell membrane; G-protein coupled receptor; Glycoprotein; Membrane;
KW   Receptor; Reference proteome; Transducer; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..359
FT                   /note="P2Y purinoceptor 8"
FT                   /id="PRO_0000070031"
FT   TOPO_DOM        1..19
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        20..40
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        41..57
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        58..78
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        79..88
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        89..109
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        110..138
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        139..159
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        160..187
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        188..208
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        209..237
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        238..258
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        259..275
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        276..296
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        297..359
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          329..359
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        5
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:19349973"
FT   CARBOHYD        11
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:19349973"
SQ   SEQUENCE   359 AA;  40635 MW;  565C43660B3C0CF7 CRC64;
     MQVPNSTGPD NATLQMLRNP AIAVALPVVY SLVAAVSIPG NLFSLWVLCR RMGPRSPSVI
     FMINLSVTDL MLASVLPFQI YYHCNRHHWV FGVLLCNVVT VAFYANMYSS ILTMTCISVE
     RFLGVLYPLS SKRWRRRRYA VAACAGTWLL LLTALSPLAR TDLTYPVHAL GIITCFDVLK
     WTMLPSVAMW AVFLFTIFIL LFLIPFVITV ACYTATILKL LRTEEAHGRE QRRRAVGLAA
     VVLLAFVTCF APNNFVLLAH IVSRLFYGKS YYHVYKLTLC LSCLNNCLDP FVYYFASREF
     QLRLREYLGC RRVPRDTLDT RRESLFSART TSVRSEAGAH PEGMEGATRP GLQRQESVF
//