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   24-JAN-2024, entry version 156.
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   GlyCosmos; O54803; 3 sites, No reported glycans.
DR   GlyGen; O54803; 3 sites.
DR   iPTMnet; O54803; -.
DR   PhosphoSitePlus; O54803; -.
DR   PaxDb; 10090-ENSMUSP00000023441; -.
DR   ProteomicsDB; 287748; -.
DR   Antibodypedia; 8429; 177 antibodies from 25 providers.
DR   DNASU; 18440; -.
DR   Ensembl; ENSMUST00000023441.11; ENSMUSP00000023441.5; ENSMUSG00000022758.15.
DR   GeneID; 18440; -.
DR   KEGG; mmu:18440; -.
DR   UCSC; uc007yli.2; mouse.
DR   AGR; MGI:1337113; -.
DR   CTD; 9127; -.
DR   MGI; MGI:1337113; P2rx6.
DR   VEuPathDB; HostDB:ENSMUSG00000022758; -.
DR   eggNOG; ENOG502R480; Eukaryota.
DR   GeneTree; ENSGT01020000230351; -.
DR   InParanoid; O54803; -.
DR   OMA; ATMVCDL; -.
DR   OrthoDB; 5312692at2759; -.
DR   TreeFam; TF328633; -.
DR   Reactome; R-MMU-139853; Elevation of cytosolic Ca2+ levels.
DR   Reactome; R-MMU-418346; Platelet homeostasis.
DR   BioGRID-ORCS; 18440; 3 hits in 79 CRISPR screens.
DR   PRO; PR:O54803; -.
DR   Proteomes; UP000000589; Chromosome 16.
DR   RNAct; O54803; Protein.
DR   Bgee; ENSMUSG00000022758; Expressed in facial nucleus and 93 other cell types or 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:0043025; C:neuronal cell body; ISO:MGI.
DR   GO; GO:0098688; C:parallel fiber to Purkinje cell synapse; ISO:MGI.
DR   GO; GO:0005886; C:plasma membrane; ISS:MGI.
DR   GO; GO:0099634; C:postsynaptic specialization membrane; 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 monoatomic 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:0070588; P:calcium ion transmembrane transport; IBA:GO_Central.
DR   GO; GO:0033198; P:response to ATP; IEA:InterPro.
DR   Gene3D; 1.10.287.940; atp-gated p2x4 ion channel; 1.
DR   Gene3D; 2.60.490.10; atp-gated p2x4 ion channel domain; 1.
DR   InterPro; IPR003049; P2X6_purnocptor.
DR   InterPro; IPR027309; P2X_extracellular_dom_sf.
DR   InterPro; IPR001429; P2X_purnocptor.
DR   NCBIfam; TIGR00863; P2X; 1.
DR   PANTHER; PTHR10125; P2X PURINOCEPTOR; 1.
DR   PANTHER; PTHR10125:SF21; P2X PURINOCEPTOR 6; 1.
DR   Pfam; PF00864; P2X_receptor; 1.
DR   PIRSF; PIRSF005713; P2X_purinoceptor; 1.
DR   PRINTS; PR01313; P2X6RECEPTOR.
DR   PRINTS; PR01307; P2XRECEPTOR.
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
//