ID P2Y10_HUMAN Reviewed; 339 AA.
AC O00398; D3DTE5; Q4VBN7; Q86V16;
DT 27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 24-JAN-2024, entry version 182.
DE RecName: Full=Putative P2Y purinoceptor 10;
DE Short=P2Y10;
DE AltName: Full=P2Y-like receptor;
GN Name=P2RY10;
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 [GENOMIC DNA].
RA Bohm S.K.;
RT "Putative purinergic receptor related to P2Y5 and P2Y9 is localized on the
RT X chromosome.";
RL Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Warren C.N., Aronstam R.S., Sharma S.V.;
RT "cDNA clones of human proteins involved in signal transduction sequenced by
RT the Guthrie cDNA resource center (www.cdna.org).";
RL Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.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 [5]
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 [6]
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).
CC -!- FUNCTION: Putative receptor for purines coupled to G-proteins.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Weakly expressed in blood leukocytes.
CC {ECO:0000269|PubMed:11004484}.
CC -!- DEVELOPMENTAL STAGE: Up-regulated during promyelocytic cell
CC differentiation along the monocytic pathway, but not during
CC granulocytic differentiation.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; AF000545; AAB57836.1; -; Genomic_DNA.
DR EMBL; AY275461; AAP32293.1; -; Genomic_DNA.
DR EMBL; Z82200; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471104; EAW98594.1; -; Genomic_DNA.
DR EMBL; CH471104; EAW98595.1; -; Genomic_DNA.
DR EMBL; BC051875; AAH51875.2; -; mRNA.
DR EMBL; BC095498; AAH95498.1; -; mRNA.
DR CCDS; CCDS14442.1; -.
DR RefSeq; NP_001311147.1; NM_001324218.1.
DR RefSeq; NP_055314.1; NM_014499.3.
DR RefSeq; NP_938147.1; NM_198333.2.
DR AlphaFoldDB; O00398; -.
DR SMR; O00398; -.
DR BioGRID; 118147; 105.
DR STRING; 9606.ENSP00000171757; -.
DR BindingDB; O00398; -.
DR ChEMBL; CHEMBL3562166; -.
DR DrugBank; DB01069; Promethazine.
DR GuidetoPHARMACOLOGY; 165; -.
DR GlyCosmos; O00398; 3 sites, No reported glycans.
DR GlyGen; O00398; 4 sites, 1 O-linked glycan (1 site).
DR PhosphoSitePlus; O00398; -.
DR BioMuta; P2RY10; -.
DR MassIVE; O00398; -.
DR PaxDb; 9606-ENSP00000171757; -.
DR PeptideAtlas; O00398; -.
DR ProteomicsDB; 47864; -.
DR Antibodypedia; 14108; 230 antibodies from 29 providers.
DR DNASU; 27334; -.
DR Ensembl; ENST00000171757.3; ENSP00000171757.2; ENSG00000078589.13.
DR Ensembl; ENST00000544091.1; ENSP00000443138.1; ENSG00000078589.13.
DR GeneID; 27334; -.
DR KEGG; hsa:27334; -.
DR MANE-Select; ENST00000171757.3; ENSP00000171757.2; NM_014499.4; NP_055314.1.
DR UCSC; uc004ede.4; human.
DR AGR; HGNC:19906; -.
DR CTD; 27334; -.
DR DisGeNET; 27334; -.
DR GeneCards; P2RY10; -.
DR HGNC; HGNC:19906; P2RY10.
DR HPA; ENSG00000078589; Tissue enhanced (lymphoid).
DR MIM; 300529; gene.
DR neXtProt; NX_O00398; -.
DR OpenTargets; ENSG00000078589; -.
DR PharmGKB; PA134873055; -.
DR VEuPathDB; HostDB:ENSG00000078589; -.
DR eggNOG; ENOG502QTX2; Eukaryota.
DR GeneTree; ENSGT01100000263536; -.
DR HOGENOM; CLU_009579_8_2_1; -.
DR InParanoid; O00398; -.
DR OMA; YMMVKEN; -.
DR OrthoDB; 3076997at2759; -.
DR PhylomeDB; O00398; -.
DR TreeFam; TF350009; -.
DR PathwayCommons; O00398; -.
DR Reactome; R-HSA-416476; G alpha (q) signalling events.
DR Reactome; R-HSA-417957; P2Y receptors.
DR SignaLink; O00398; -.
DR SIGNOR; O00398; -.
DR BioGRID-ORCS; 27334; 23 hits in 766 CRISPR screens.
DR GeneWiki; P2RY10; -.
DR GenomeRNAi; 27334; -.
DR Pharos; O00398; Tchem.
DR PRO; PR:O00398; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; O00398; Protein.
DR Bgee; ENSG00000078589; Expressed in lymph node and 108 other cell types or tissues.
DR Genevisible; O00398; HS.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
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; cd15153; 7tmA_P2Y10; 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 PANTHER; PTHR24232; G-PROTEIN COUPLED RECEPTOR; 1.
DR PANTHER; PTHR24232:SF47; P2Y PURINOCEPTOR 10-RELATED; 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; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW Membrane; Receptor; Reference proteome; Transducer; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..339
FT /note="Putative P2Y purinoceptor 10"
FT /id="PRO_0000070034"
FT TOPO_DOM 1..39
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 40..60
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 61..68
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 69..89
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 90..103
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 104..124
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 125..149
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 150..170
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 171..193
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 194..214
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 215..244
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 245..265
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 266..288
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 289..309
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 310..339
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 16
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 26
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 178
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 106..181
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT VARIANT 3
FT /note="N -> H (in dbSNP:rs6618868)"
FT /id="VAR_033481"
SQ SEQUENCE 339 AA; 38774 MW; 2C043E4DC342FA0D CRC64;
MANLDKYTET FKMGSNSTST AEIYCNVTNV KFQYSLYATT YILIFIPGLL ANSAALWVLC
RFISKKNKAI IFMINLSVAD LAHVLSLPLR IYYYISHHWP FQRALCLLCF YLKYLNMYAS
ICFLTCISLQ RCFFLLKPFR ARDWKRRYDV GISAAIWIVV GTACLPFPIL RSTDLNNNKS
CFADLGYKQM NAVALVGMIT VAELAGFVIP VIIIAWCTWK TTISLRQPPM AFQGISERQK
ALRMVFMCAA VFFICFTPYH INFIFYTMVK ETIISSCPVV RIALYFHPFC LCLASLCCLL
DPILYYFMAS EFRDQLSRHG SSVTRSRLMS KESGSSMIG
//
