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P2RY6_HUMAN
ID   P2RY6_HUMAN             Reviewed;         328 AA.
AC   Q15077; Q15754;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 185.
DE   RecName: Full=P2Y purinoceptor 6;
DE            Short=P2Y6;
GN   Name=P2RY6; ORFNames=PP2891;
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].
RX   PubMed=8670200; DOI=10.1006/bbrc.1996.0739;
RA   Communi D., Parmentier M., Boeynaems J.-M.;
RT   "Cloning, functional expression and tissue distribution of the human P2Y6
RT   receptor.";
RL   Biochem. Biophys. Res. Commun. 222:303-308(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=9286708; DOI=10.1006/geno.1997.4841;
RA   Somers G.R., Hammet F., Woollatt E., Richards R.I., Southey M.C.,
RA   Venter D.J.;
RT   "Chromosomal localization of the human P2y6 purinoceptor gene and
RT   phylogenetic analysis of the P2y purinoceptor family.";
RL   Genomics 44:127-130(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Placenta;
RX   PubMed=9268704; DOI=10.1006/bbrc.1997.7135;
RA   Maier R., Glatz A., Mosbacher J., Bilbe G.;
RT   "Cloning of P2Y6 cDNAs and identification of a pseudogene: comparison of
RT   P2Y receptor subtype expression in bone and brain tissues.";
RL   Biochem. Biophys. Res. Commun. 237:297-302(1997).
RN   [4]
RP   ERRATUM OF PUBMED:9268704.
RX   PubMed=9412455; DOI=10.1006/bbrc.1997.7653;
RA   Maier R., Glatz A., Mosbacher J., Bilbe G.;
RL   Biochem. Biophys. Res. Commun. 240:298-302(1997).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15498874; DOI=10.1073/pnas.0404089101;
RA   Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X.,
RA   Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X.,
RA   Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.;
RT   "Large-scale cDNA transfection screening for genes related to cancer
RT   development and progression.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Puhl H.L. III, Ikeda S.R., Aronstam R.S.;
RT   "cDNA clones of human proteins involved in signal transduction sequenced by
RT   the Guthrie cDNA resource center (www.cdna.org).";
RL   Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA   Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA   Phelan M., Farmer A.;
RT   "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL   Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
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 extracellular UDP > UTP > ATP. The activity of
CC       this receptor is mediated by G proteins which activate a
CC       phosphatidylinositol-calcium second messenger system.
CC   -!- INTERACTION:
CC       Q15077; P55060: CSE1L; NbExp=2; IntAct=EBI-10235794, EBI-286709;
CC       Q15077; P28799: GRN; NbExp=3; IntAct=EBI-10235794, EBI-747754;
CC       Q15077; P49639: HOXA1; NbExp=5; IntAct=EBI-10235794, EBI-740785;
CC       Q15077; Q14974: KPNB1; NbExp=4; IntAct=EBI-10235794, EBI-286758;
CC       Q15077; Q07627: KRTAP1-1; NbExp=3; IntAct=EBI-10235794, EBI-11959885;
CC       Q15077; P60409: KRTAP10-7; NbExp=3; IntAct=EBI-10235794, EBI-10172290;
CC       Q15077; P60410: KRTAP10-8; NbExp=3; IntAct=EBI-10235794, EBI-10171774;
CC       Q15077; P60328: KRTAP12-3; NbExp=3; IntAct=EBI-10235794, EBI-11953334;
CC       Q15077; Q9BYR9: KRTAP2-4; NbExp=3; IntAct=EBI-10235794, EBI-14065470;
CC       Q15077; Q9BYR6: KRTAP3-3; NbExp=3; IntAct=EBI-10235794, EBI-3957694;
CC       Q15077; P26371: KRTAP5-9; NbExp=3; IntAct=EBI-10235794, EBI-3958099;
CC       Q15077; Q9BYQ4: KRTAP9-2; NbExp=5; IntAct=EBI-10235794, EBI-1044640;
CC       Q15077; Q8NI22: MCFD2; NbExp=3; IntAct=EBI-10235794, EBI-2689785;
CC       Q15077; P0DPK4: NOTCH2NLC; NbExp=3; IntAct=EBI-10235794, EBI-22310682;
CC       Q15077; O15162: PLSCR1; NbExp=3; IntAct=EBI-10235794, EBI-740019;
CC       Q15077; O76024: WFS1; NbExp=3; IntAct=EBI-10235794, EBI-720609;
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR   EMBL; X97058; CAA65770.1; -; mRNA.
DR   EMBL; U52464; AAB03572.1; -; mRNA.
DR   EMBL; AF007892; AAB80713.1; -; mRNA.
DR   EMBL; AF007891; AAB80712.1; -; mRNA.
DR   EMBL; AF218005; AAG17247.1; -; mRNA.
DR   EMBL; AF498920; AAM18129.1; -; mRNA.
DR   EMBL; BT006771; AAP35417.1; -; mRNA.
DR   EMBL; BC000571; AAH00571.1; -; mRNA.
DR   EMBL; BC009391; AAH09391.1; -; mRNA.
DR   CCDS; CCDS8220.1; -.
DR   PIR; JC4800; JC4800.
DR   RefSeq; NP_001264133.1; NM_001277204.1.
DR   RefSeq; NP_001264134.1; NM_001277205.1.
DR   RefSeq; NP_001264135.1; NM_001277206.1.
DR   RefSeq; NP_001264136.1; NM_001277207.1.
DR   RefSeq; NP_001264137.1; NM_001277208.1.
DR   RefSeq; NP_789766.1; NM_176796.2.
DR   RefSeq; NP_789767.1; NM_176797.2.
DR   RefSeq; NP_789768.1; NM_176798.2.
DR   RefSeq; XP_005274079.1; XM_005274022.3.
DR   RefSeq; XP_006718634.1; XM_006718571.3.
DR   RefSeq; XP_011543379.1; XM_011545077.2.
DR   RefSeq; XP_011543381.1; XM_011545079.2.
DR   AlphaFoldDB; Q15077; -.
DR   SMR; Q15077; -.
DR   BioGRID; 111070; 383.
DR   IntAct; Q15077; 376.
DR   STRING; 9606.ENSP00000480966; -.
DR   BindingDB; Q15077; -.
DR   ChEMBL; CHEMBL4714; -.
DR   DrugCentral; Q15077; -.
DR   GuidetoPHARMACOLOGY; 326; -.
DR   GlyGen; Q15077; 1 site.
DR   iPTMnet; Q15077; -.
DR   PhosphoSitePlus; Q15077; -.
DR   BioMuta; P2RY6; -.
DR   DMDM; 2495018; -.
DR   jPOST; Q15077; -.
DR   MassIVE; Q15077; -.
DR   MaxQB; Q15077; -.
DR   PaxDb; Q15077; -.
DR   PeptideAtlas; Q15077; -.
DR   PRIDE; Q15077; -.
DR   ProteomicsDB; 60428; -.
DR   Antibodypedia; 17126; 265 antibodies from 34 providers.
DR   DNASU; 5031; -.
DR   Ensembl; ENST00000349767.6; ENSP00000309771.2; ENSG00000171631.16.
DR   Ensembl; ENST00000393590.3; ENSP00000377215.2; ENSG00000171631.16.
DR   Ensembl; ENST00000393591.5; ENSP00000377216.1; ENSG00000171631.16.
DR   Ensembl; ENST00000393592.7; ENSP00000377217.2; ENSG00000171631.16.
DR   Ensembl; ENST00000535931.2; ENSP00000440770.2; ENSG00000171631.16.
DR   Ensembl; ENST00000538328.2; ENSP00000442990.1; ENSG00000171631.16.
DR   Ensembl; ENST00000540124.6; ENSP00000442551.1; ENSG00000171631.16.
DR   Ensembl; ENST00000540342.6; ENSP00000443427.1; ENSG00000171631.16.
DR   Ensembl; ENST00000542092.5; ENSP00000445652.1; ENSG00000171631.16.
DR   Ensembl; ENST00000544437.6; ENSP00000441079.2; ENSG00000171631.16.
DR   Ensembl; ENST00000618468.5; ENSP00000480966.1; ENSG00000171631.16.
DR   Ensembl; ENST00000679753.1; ENSP00000504879.1; ENSG00000171631.16.
DR   Ensembl; ENST00000680955.1; ENSP00000505646.1; ENSG00000171631.16.
DR   GeneID; 5031; -.
DR   KEGG; hsa:5031; -.
DR   MANE-Select; ENST00000540124.6; ENSP00000442551.1; NM_001277204.2; NP_001264133.1.
DR   UCSC; uc001otm.5; human.
DR   CTD; 5031; -.
DR   DisGeNET; 5031; -.
DR   GeneCards; P2RY6; -.
DR   HGNC; HGNC:8543; P2RY6.
DR   HPA; ENSG00000171631; Tissue enhanced (lymphoid).
DR   MIM; 602451; gene.
DR   neXtProt; NX_Q15077; -.
DR   OpenTargets; ENSG00000171631; -.
DR   PharmGKB; PA32872; -.
DR   VEuPathDB; HostDB:ENSG00000171631; -.
DR   eggNOG; ENOG502QRYJ; Eukaryota.
DR   GeneTree; ENSGT01030000234621; -.
DR   InParanoid; Q15077; -.
DR   OMA; KWRHDHC; -.
DR   OrthoDB; 925903at2759; -.
DR   PhylomeDB; Q15077; -.
DR   TreeFam; TF330775; -.
DR   PathwayCommons; Q15077; -.
DR   Reactome; R-HSA-416476; G alpha (q) signalling events.
DR   Reactome; R-HSA-417957; P2Y receptors.
DR   SignaLink; Q15077; -.
DR   SIGNOR; Q15077; -.
DR   BioGRID-ORCS; 5031; 24 hits in 1067 CRISPR screens.
DR   ChiTaRS; P2RY6; human.
DR   GeneWiki; P2RY6; -.
DR   GenomeRNAi; 5031; -.
DR   Pharos; Q15077; Tchem.
DR   PRO; PR:Q15077; -.
DR   Proteomes; UP000005640; Chromosome 11.
DR   RNAct; Q15077; protein.
DR   Bgee; ENSG00000171631; Expressed in spleen and 116 other tissues.
DR   ExpressionAtlas; Q15077; baseline and differential.
DR   Genevisible; Q15077; HS.
DR   GO; GO:0016324; C:apical plasma membrane; IEA:Ensembl.
DR   GO; GO:0016323; C:basolateral plasma membrane; IEA:Ensembl.
DR   GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0001621; F:G protein-coupled ADP receptor activity; IDA:ARUK-UCL.
DR   GO; GO:0004930; F:G protein-coupled receptor activity; TAS:ProtInc.
DR   GO; GO:0045029; F:G protein-coupled UDP receptor activity; IDA:ARUK-UCL.
DR   GO; GO:0045030; F:G protein-coupled UTP receptor activity; IDA:ARUK-UCL.
DR   GO; GO:0038023; F:signaling receptor activity; IBA:GO_Central.
DR   GO; GO:0007202; P:activation of phospholipase C activity; TAS:ARUK-UCL.
DR   GO; GO:0071380; P:cellular response to prostaglandin E stimulus; IEA:Ensembl.
DR   GO; GO:0071415; P:cellular response to purine-containing compound; IDA:ARUK-UCL.
DR   GO; GO:1905835; P:cellular response to pyrimidine ribonucleotide; IDA:ARUK-UCL.
DR   GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR   GO; GO:0006909; P:phagocytosis; ISS:ARUK-UCL.
DR   GO; GO:0007200; P:phospholipase C-activating G protein-coupled receptor signaling pathway; TAS:ProtInc.
DR   GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IDA:BHF-UCL.
DR   GO; GO:0031587; P:positive regulation of inositol 1,4,5-trisphosphate-sensitive calcium-release channel activity; ISS:ARUK-UCL.
DR   GO; GO:0032962; P:positive regulation of inositol trisphosphate biosynthetic process; IDA:ARUK-UCL.
DR   GO; GO:0014911; P:positive regulation of smooth muscle cell migration; IEA:Ensembl.
DR   GO; GO:1904707; P:positive regulation of vascular associated smooth muscle cell proliferation; IMP:BHF-UCL.
DR   GO; GO:0030321; P:transepithelial chloride transport; IEA:Ensembl.
DR   InterPro; IPR000276; GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR   InterPro; IPR001973; P2Y6_rcpt.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PRINTS; PR01068; P2Y6PRNOCPTR.
DR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW   Membrane; Receptor; Reference proteome; Transducer; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..328
FT                   /note="P2Y purinoceptor 6"
FT                   /id="PRO_0000070028"
FT   TOPO_DOM        1..27
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        28..48
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        49..62
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        63..83
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        84..101
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        102..122
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        123..144
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        145..165
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        166..194
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        195..215
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        216..236
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        237..257
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        258..280
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        281..303
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        304..328
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        5
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        99..177
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT   CONFLICT        2..3
FT                   /note="Missing (in Ref. 2)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   328 AA;  36429 MW;  AAD6C55A43818107 CRC64;
     MEWDNGTGQA LGLPPTTCVY RENFKQLLLP PVYSAVLAAG LPLNICVITQ ICTSRRALTR
     TAVYTLNLAL ADLLYACSLP LLIYNYAQGD HWPFGDFACR LVRFLFYANL HGSILFLTCI
     SFQRYLGICH PLAPWHKRGG RRAAWLVCVA VWLAVTTQCL PTAIFAATGI QRNRTVCYDL
     SPPALATHYM PYGMALTVIG FLLPFAALLA CYCLLACRLC RQDGPAEPVA QERRGKAARM
     AVVVAAAFAI SFLPFHITKT AYLAVRSTPG VPCTVLEAFA AAYKGTRPFA SANSVLDPIL
     FYFTQKKFRR RPHELLQKLT AKWQRQGR
 
 
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