P2RY6_MOUSE
ID P2RY6_MOUSE Reviewed; 328 AA.
AC Q9ERK9;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=P2Y purinoceptor 6;
DE Short=P2Y6;
GN Name=P2ry6;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=129/SvEv;
RX PubMed=11259526;
RA Lazarowski E.R., Rochelle L.G., O'Neal W.K., Ribeiro C.M.P., Grubb B.R.,
RA Zhang V., Harden T.K., Boucher R.C.;
RT "Cloning and functional characterization of two murine uridine nucleotide
RT receptors reveal a potential target for correcting ion transport deficiency
RT in cystic fibrosis gallbladder.";
RL J. Pharmacol. Exp. Ther. 297:43-49(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Mammary gland;
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 UTP > ADP = 2-methylthio-ATP >
CC ADP-beta-S > ATP = ATP-gamma-S. The activity of this receptor is
CC mediated by G proteins which activate a phosphatidylinositol-calcium
CC second messenger system. Functionally coupled to phospholipase C (By
CC similarity). {ECO:0000250}.
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; AF298899; AAG24619.1; -; Genomic_DNA.
DR EMBL; BC027331; AAH27331.1; -; mRNA.
DR EMBL; BC064095; AAH64095.1; -; mRNA.
DR CCDS; CCDS21507.1; -.
DR RefSeq; NP_898991.1; NM_183168.2.
DR RefSeq; XP_006507703.1; XM_006507640.3.
DR RefSeq; XP_011240041.1; XM_011241739.2.
DR AlphaFoldDB; Q9ERK9; -.
DR SMR; Q9ERK9; -.
DR STRING; 10090.ENSMUSP00000055697; -.
DR GlyGen; Q9ERK9; 2 sites.
DR PhosphoSitePlus; Q9ERK9; -.
DR MaxQB; Q9ERK9; -.
DR PaxDb; Q9ERK9; -.
DR PRIDE; Q9ERK9; -.
DR ProteomicsDB; 294357; -.
DR Antibodypedia; 17126; 265 antibodies from 34 providers.
DR DNASU; 233571; -.
DR Ensembl; ENSMUST00000060174; ENSMUSP00000055697; ENSMUSG00000048779.
DR GeneID; 233571; -.
DR KEGG; mmu:233571; -.
DR UCSC; uc009inw.2; mouse.
DR CTD; 5031; -.
DR MGI; MGI:2673874; P2ry6.
DR VEuPathDB; HostDB:ENSMUSG00000048779; -.
DR eggNOG; ENOG502QRYJ; Eukaryota.
DR GeneTree; ENSGT01030000234621; -.
DR HOGENOM; CLU_009579_8_2_1; -.
DR InParanoid; Q9ERK9; -.
DR OMA; KWRHDHC; -.
DR OrthoDB; 925903at2759; -.
DR PhylomeDB; Q9ERK9; -.
DR TreeFam; TF330775; -.
DR Reactome; R-MMU-416476; G alpha (q) signalling events.
DR Reactome; R-MMU-417957; P2Y receptors.
DR BioGRID-ORCS; 233571; 2 hits in 74 CRISPR screens.
DR PRO; PR:Q9ERK9; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q9ERK9; protein.
DR Bgee; ENSMUSG00000048779; Expressed in stroma of bone marrow and 126 other tissues.
DR ExpressionAtlas; Q9ERK9; baseline and differential.
DR Genevisible; Q9ERK9; MM.
DR GO; GO:0016324; C:apical plasma membrane; ISO:MGI.
DR GO; GO:0016323; C:basolateral plasma membrane; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0001621; F:G protein-coupled ADP receptor activity; ISO:MGI.
DR GO; GO:0045029; F:G protein-coupled UDP receptor activity; IDA:MGI.
DR GO; GO:0045030; F:G protein-coupled UTP receptor activity; ISO:MGI.
DR GO; GO:0019103; F:pyrimidine nucleotide binding; IC:MGI.
DR GO; GO:0038023; F:signaling receptor activity; IBA:GO_Central.
DR GO; GO:0071407; P:cellular response to organic cyclic compound; IDA:MGI.
DR GO; GO:0071380; P:cellular response to prostaglandin E stimulus; IDA:MGI.
DR GO; GO:0071415; P:cellular response to purine-containing compound; ISO:MGI.
DR GO; GO:1905835; P:cellular response to pyrimidine ribonucleotide; ISO:MGI.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0006909; P:phagocytosis; ISO:MGI.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISO:MGI.
DR GO; GO:0031587; P:positive regulation of inositol 1,4,5-trisphosphate-sensitive calcium-release channel activity; ISO:MGI.
DR GO; GO:0032962; P:positive regulation of inositol trisphosphate biosynthetic process; ISO:MGI.
DR GO; GO:0014911; P:positive regulation of smooth muscle cell migration; ISO:MGI.
DR GO; GO:1904707; P:positive regulation of vascular associated smooth muscle cell proliferation; ISO:MGI.
DR GO; GO:0030321; P:transepithelial chloride transport; IDA:MGI.
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 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..328
FT /note="P2Y purinoceptor 6"
FT /id="PRO_0000070029"
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 CARBOHYD 173
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 99..177
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 328 AA; 36721 MW; 00F9DF5ADADF903E CRC64;
MEQDNGTIQA PGLPPTTCVY REDFKRLLLT PVYSVVLVVG LPLNICVIAQ ICASRRTLTR
SAVYTLNLAL ADLMYACSLP LLIYNYARGD HWPFGDLACR FVRFLFYANL HGSILFLTCI
SFQRYLGICH PLASWHKRGG RRAAWVVCGV VWLAVTAQCL PTAVFAATGI QRNRTVCYDL
SPPILSTRYL PYGMALTVIG FLLPFIALLA CYCRMARRLC RQDGPAGPVA QERRSKAARM
AVVVAAVFAI SFLPFHITKT AYLAVRSTPG VSCPVLETFA AAYKGTRPFA SVNSVLDPIL
FYFTQQKFRR QPHDLLQRLT AKWQRQRV
