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P2Y10_HUMAN
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   03-AUG-2022, entry version 174.
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   GlyGen; O00398; 4 sites, 1 O-linked glycan (1 site).
DR   PhosphoSitePlus; O00398; -.
DR   BioMuta; P2RY10; -.
DR   MassIVE; O00398; -.
DR   PaxDb; O00398; -.
DR   PeptideAtlas; O00398; -.
DR   PRIDE; O00398; -.
DR   ProteomicsDB; 47864; -.
DR   Antibodypedia; 14108; 194 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   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; ENSGT01050000244810; -.
DR   HOGENOM; CLU_009579_8_2_1; -.
DR   InParanoid; O00398; -.
DR   OMA; DLGYKKM; -.
DR   OrthoDB; 688340at2759; -.
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; 22 hits in 692 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 107 other tissues.
DR   Genevisible; O00398; HS.
DR   GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
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; IPR027676; P2Y10_rcpt.
DR   PANTHER; PTHR24232:SF47; PTHR24232:SF47; 1.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00237; GPCRRHODOPSN.
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
 
 
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