P2RX6_MOUSE
ID P2RX6_MOUSE Reviewed; 389 AA.
AC O54803; G3X8W3; Q3UUD0;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 31-JAN-2018, sequence version 3.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=P2X purinoceptor 6;
DE Short=P2X6;
DE AltName: Full=ATP receptor;
DE AltName: Full=P2XM;
DE AltName: Full=Purinergic receptor;
DE AltName: Full=Purinergic receptor P2X-like 1;
GN Name=P2rx6; Synonyms=P2rxl1;
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 [MRNA].
RX PubMed=9852680; DOI=10.1007/s100380050086;
RA Nawa G., Urano T., Tokino T., Ochi T., Miyoshi Y.;
RT "Cloning and characterization of the murine P2XM receptor gene.";
RL J. Hum. Genet. 43:262-267(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 8-389.
RC STRAIN=C57BL/6J; TISSUE=Spinal cord;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
CC -!- FUNCTION: Receptor for ATP that acts as a ligand-gated ion channel.
CC {ECO:0000250}.
CC -!- SUBUNIT: Unlike most P2XRs, P2RX6 does not seem to form homotrimers or
CC heterotrimers. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Predominantly expressed in skeletal muscle. Also
CC expressed in lung.
CC -!- PTM: N-glycosylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the P2X receptor family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA24693.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAE23697.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB010883; BAA24693.1; ALT_INIT; mRNA.
DR EMBL; AC115733; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466521; EDK97466.1; -; Genomic_DNA.
DR EMBL; AK138541; BAE23697.1; ALT_INIT; mRNA.
DR CCDS; CCDS28007.2; -.
DR RefSeq; NP_001153033.1; NM_001159561.1.
DR RefSeq; NP_035158.2; NM_011028.2.
DR AlphaFoldDB; O54803; -.
DR SMR; O54803; -.
DR STRING; 10090.ENSMUSP00000023441; -.
DR GlyGen; O54803; 3 sites.
DR iPTMnet; O54803; -.
DR PhosphoSitePlus; O54803; -.
DR PaxDb; O54803; -.
DR PRIDE; O54803; -.
DR ProteomicsDB; 287748; -.
DR Antibodypedia; 8429; 159 antibodies from 25 providers.
DR DNASU; 18440; -.
DR Ensembl; ENSMUST00000023441; ENSMUSP00000023441; ENSMUSG00000022758.
DR GeneID; 18440; -.
DR KEGG; mmu:18440; -.
DR UCSC; uc007yli.2; mouse.
DR CTD; 9127; -.
DR MGI; MGI:1337113; P2rx6.
DR VEuPathDB; HostDB:ENSMUSG00000022758; -.
DR eggNOG; ENOG502R480; Eukaryota.
DR GeneTree; ENSGT01020000230351; -.
DR InParanoid; O54803; -.
DR OMA; WPPQGEN; -.
DR OrthoDB; 1128763at2759; -.
DR TreeFam; TF328633; -.
DR Reactome; R-MMU-139853; Elevation of cytosolic Ca2+ levels.
DR Reactome; R-MMU-418346; Platelet homeostasis.
DR BioGRID-ORCS; 18440; 2 hits in 74 CRISPR screens.
DR PRO; PR:O54803; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; O54803; protein.
DR Bgee; ENSMUSG00000022758; Expressed in facial nucleus and 91 other tissues.
DR ExpressionAtlas; O54803; baseline and differential.
DR GO; GO:0030054; C:cell junction; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0043197; C:dendritic spine; ISO:MGI.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:MGI.
DR GO; GO:0005639; C:integral component of nuclear inner membrane; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:MGI.
DR GO; GO:0099060; C:integral component of postsynaptic specialization membrane; ISO:MGI.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0098688; C:parallel fiber to Purkinje cell synapse; ISO:MGI.
DR GO; GO:0014069; C:postsynaptic density; ISO:MGI.
DR GO; GO:0043235; C:receptor complex; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0004931; F:extracellularly ATP-gated cation channel activity; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0001614; F:purinergic nucleotide receptor activity; IEA:InterPro.
DR GO; GO:0033198; P:response to ATP; IEA:InterPro.
DR Gene3D; 2.60.490.10; -; 1.
DR InterPro; IPR003049; P2X6_purnocptor.
DR InterPro; IPR027309; P2X_extracellular_dom_sf.
DR InterPro; IPR001429; P2X_purnocptor.
DR PANTHER; PTHR10125:SF21; PTHR10125:SF21; 1.
DR PIRSF; PIRSF005713; P2X_purinoceptor; 1.
DR PRINTS; PR01313; P2X6RECEPTOR.
DR PRINTS; PR01307; P2XRECEPTOR.
DR TIGRFAMs; TIGR00863; P2X; 1.
DR PROSITE; PS01212; P2X_RECEPTOR; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond; Glycoprotein; Ion channel; Ion transport;
KW Ligand-gated ion channel; Membrane; Receptor; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..389
FT /note="P2X purinoceptor 6"
FT /id="PRO_0000161558"
FT TOPO_DOM 1..45
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 46..66
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 67..335
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 336..356
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 357..389
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 167
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 197
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 212
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 129..179
FT /evidence="ECO:0000250"
FT DISULFID 140..163
FT /evidence="ECO:0000250"
FT DISULFID 146..173
FT /evidence="ECO:0000250"
FT DISULFID 230..240
FT /evidence="ECO:0000250"
FT DISULFID 274..283
FT /evidence="ECO:0000250"
FT CONFLICT 269
FT /note="S -> T (in Ref. 1; BAA24693)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 389 AA; 43099 MW; 55852B6BECA1B7F4 CRC64;
MQLQPAGTGN MASAAAAALV SWGFLDYKTE KYVLTRNCRV GVSQRLLQLA VVVYVIGWAL
LAKKGYQERD LAPQTSVITK LKGVSVTQVK ELENRLWDVA DFVKPSQGEN VFFLVTNFLV
TPAQVQGRCP EHPSVPLANC WADEDCPEGE TGTYSHGIKT GQCVVFNGTH RTCEIWSWCP
VESGAVPRKP LLAQAKNFTL FIKNTVTFSK FNFSRSNALL TWDNTYFKHC LYDPLSSPYC
PVFRIGDLVA MAGGDFEDLA LLGGAVGISI HWDCNLDTKG SDCCPQYSFQ LQQKGYNFRT
ANHWWAASGV ETRSLLKLYG IRFDILVTGQ AGKFALIPTA ITVGTGAAWL GMVTFLCDLL
LLYVDREAGF YWRTKYEEAR APKTTTNSS
