P2RX6_RAT
ID P2RX6_RAT Reviewed; 389 AA.
AC P51579; R9PXR5;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 31-JAN-2018, sequence version 2.
DT 03-AUG-2022, entry version 153.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RX PubMed=8670303; DOI=10.1006/bbrc.1996.0915;
RA Soto F., Garcia-Guzman M., Karschin C., Stuehmer W.;
RT "Cloning and tissue distribution of a novel P2X receptor from rat brain.";
RL Biochem. Biophys. Res. Commun. 223:456-460(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 7-389.
RC TISSUE=Cervical ganglion;
RX PubMed=8786426; DOI=10.1523/jneurosci.16-08-02495.1996;
RA Collo G., Kawashima E., Pich E., Neidhart S., North R.A., Surprenant A.,
RA Buell G.N.;
RT "Cloning of P2X5 and P2X6 receptors and the distribution and properties of
RT an extended family of ATP-gated ion channels.";
RL J. Neurosci. 16:2495-2507(1996).
CC -!- FUNCTION: Receptor for ATP that acts as a ligand-gated ion channel.
CC -!- SUBUNIT: Unlike most P2XRs, P2RX6 does not seem to form homotrimers or
CC heterotrimers. {ECO:0000250}.
CC -!- INTERACTION:
CC P51579; P49653: P2rx2; NbExp=4; IntAct=EBI-9511515, EBI-9511543;
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- PTM: N-glycosylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the P2X receptor family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA63053.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAA66044.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; X97376; CAA66044.1; ALT_INIT; mRNA.
DR EMBL; AABR07034750; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH473999; EDL77896.1; -; Genomic_DNA.
DR EMBL; X92070; CAA63053.1; ALT_INIT; mRNA.
DR PIR; JC4843; JC4843.
DR RefSeq; NP_036853.2; NM_012721.2.
DR AlphaFoldDB; P51579; -.
DR SMR; P51579; -.
DR IntAct; P51579; 2.
DR MINT; P51579; -.
DR STRING; 10116.ENSRNOP00000002558; -.
DR ChEMBL; CHEMBL2122; -.
DR DrugCentral; P51579; -.
DR GuidetoPHARMACOLOGY; 483; -.
DR GlyGen; P51579; 3 sites.
DR PaxDb; P51579; -.
DR Ensembl; ENSRNOT00000002558; ENSRNOP00000002558; ENSRNOG00000001873.
DR GeneID; 25041; -.
DR KEGG; rno:25041; -.
DR CTD; 9127; -.
DR RGD; 3243; P2rx6.
DR eggNOG; ENOG502R480; Eukaryota.
DR GeneTree; ENSGT01020000230351; -.
DR InParanoid; P51579; -.
DR OMA; WPPQGEN; -.
DR OrthoDB; 1128763at2759; -.
DR PhylomeDB; P51579; -.
DR TreeFam; TF328633; -.
DR Reactome; R-RNO-139853; Elevation of cytosolic Ca2+ levels.
DR Reactome; R-RNO-418346; Platelet homeostasis.
DR PRO; PR:P51579; -.
DR Proteomes; UP000002494; Chromosome 11.
DR Proteomes; UP000234681; Chromosome 11.
DR Bgee; ENSRNOG00000001873; Expressed in quadriceps femoris and 9 other tissues.
DR GO; GO:0030054; C:cell junction; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0043197; C:dendritic spine; IDA:RGD.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0005639; C:integral component of nuclear inner membrane; IBA:GO_Central.
DR GO; GO:0099060; C:integral component of postsynaptic specialization membrane; IDA:SynGO.
DR GO; GO:0016020; C:membrane; IDA:RGD.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0098688; C:parallel fiber to Purkinje cell synapse; IDA:SynGO.
DR GO; GO:0014069; C:postsynaptic density; IDA:RGD.
DR GO; GO:0043235; C:receptor complex; ISO:RGD.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0004931; F:extracellularly ATP-gated cation channel activity; IDA:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:RGD.
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 1: Evidence at protein level;
KW Disulfide bond; Glycoprotein; Ion channel; Ion transport;
KW Ligand-gated ion channel; Membrane; Phosphoprotein; Receptor;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..389
FT /note="P2X purinoceptor 6"
FT /id="PRO_0000161559"
FT TOPO_DOM 1..41
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 42..62
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 63..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 MOD_RES 66
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O15547"
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"
SQ SEQUENCE 389 AA; 43422 MW; 1AE683A0191B6A0B CRC64;
MQLQPAGTGS MASAVAAALV SWGFLDYKTE KYVMTRNCWV GISQRLLQLG VVVYVIGWAL
LAKKGYQEWD MDPQISVITK LKGVSVTQVK ELEKRLWDVA DFVRPSQGEN VFFLVTNFLV
TPAQVQGRCP EHPSVPLANC WADEDCPEGE MGTYSHGIKT GQCVAFNGTH RTCEIWSWCP
VESSAVPRKP LLAQAKNFTL FIKNTVTFNK FNFSRTNALD TWDNTYFKYC LYDSLSSPYC
PVFRIGDLVA MTGGDFEDLA LLGGAVGINI HWDCNLDTKG SDCSPQYSFQ LQERGYNFRT
ANYWWAASGV ESRSLLKLYG IRFDILVTGQ AGKFALIPTA ITVGTGAAWL GMVTFLCDLL
LLYVDREAGF YWRTKYEEAR APKATTNSA
