P2RY8_HUMAN
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 03-AUG-2022, entry version 151.
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 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; Q86VZ1; -.
DR PeptideAtlas; Q86VZ1; -.
DR PRIDE; Q86VZ1; -.
DR ProteomicsDB; 70092; -.
DR Antibodypedia; 588; 223 antibodies from 29 providers.
DR DNASU; 286530; -.
DR Ensembl; ENST00000381297.10; ENSP00000370697.4; ENSG00000182162.11.
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 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; GNGLSMW; -.
DR OrthoDB; 794310at2759; -.
DR PhylomeDB; Q86VZ1; -.
DR TreeFam; TF330775; -.
DR PathwayCommons; Q86VZ1; -.
DR SignaLink; Q86VZ1; -.
DR BioGRID-ORCS; 286530; 12 hits in 561 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 RNAct; Q86VZ1; protein.
DR Bgee; ENSG00000182162; Expressed in buccal mucosa cell and 118 other tissues.
DR ExpressionAtlas; Q86VZ1; baseline and differential.
DR Genevisible; Q86VZ1; HS.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
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:0051482; P:positive regulation of cytosolic calcium ion concentration involved in phospholipase C-activating G protein-coupled signaling pathway; IBA:GO_Central.
DR GO; GO:0035025; P:positive regulation of Rho protein signal transduction; IBA:GO_Central.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR InterPro; IPR027669; P2Y8_rcpt.
DR PANTHER; PTHR24232:SF25; PTHR24232:SF25; 1.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
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
