P2RX1_MOUSE
ID P2RX1_MOUSE Reviewed; 399 AA.
AC P51576; Q5SRU4;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=P2X purinoceptor 1;
DE Short=P2X1;
DE AltName: Full=ATP receptor;
DE AltName: Full=Purinergic receptor;
GN Name=P2rx1;
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].
RC STRAIN=OF1; TISSUE=Urinary bladder smooth muscle;
RX PubMed=8834001;
RA Valera S., Talabot F., Evans R.J., Gos A., Antonarakis S.E., Morris M.A.,
RA Buell G.N.;
RT "Characterization and chromosomal localization of a human P2X receptor from
RT the urinary bladder.";
RL Recept. Channels 3:283-289(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129/SvJ;
RA Yu X.-M., Connolly A.J.;
RT "Mouse P2X1 purinergic receptor gene structure.";
RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Urinary bladder;
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).
RN [4]
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).
CC -!- FUNCTION: Ligand-gated ion channel with relatively high calcium
CC permeability. Binding to ATP mediates synaptic transmission between
CC neurons and from neurons to smooth muscle. Seems to be linked to
CC apoptosis, by increasing the intracellular concentration of calcium in
CC the presence of ATP, leading to programmed cell death (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Homo- or heteropolymers. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the P2X receptor family. {ECO:0000305}.
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DR EMBL; X84896; CAA59322.1; -; mRNA.
DR EMBL; AF250123; AAF68968.1; -; Genomic_DNA.
DR EMBL; AF250121; AAF68968.1; JOINED; Genomic_DNA.
DR EMBL; AF250122; AAF68968.1; JOINED; Genomic_DNA.
DR EMBL; AK035304; BAC29024.1; -; mRNA.
DR EMBL; AL670399; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS24992.1; -.
DR RefSeq; NP_032797.3; NM_008771.3.
DR AlphaFoldDB; P51576; -.
DR SMR; P51576; -.
DR STRING; 10090.ENSMUSP00000021141; -.
DR BindingDB; P51576; -.
DR ChEMBL; CHEMBL5496; -.
DR GlyGen; P51576; 4 sites.
DR PhosphoSitePlus; P51576; -.
DR MaxQB; P51576; -.
DR PaxDb; P51576; -.
DR PRIDE; P51576; -.
DR ProteomicsDB; 287747; -.
DR Antibodypedia; 3473; 196 antibodies from 28 providers.
DR DNASU; 18436; -.
DR Ensembl; ENSMUST00000021141; ENSMUSP00000021141; ENSMUSG00000020787.
DR GeneID; 18436; -.
DR KEGG; mmu:18436; -.
DR UCSC; uc007jzq.2; mouse.
DR CTD; 5023; -.
DR MGI; MGI:1098235; P2rx1.
DR VEuPathDB; HostDB:ENSMUSG00000020787; -.
DR eggNOG; ENOG502QSUI; Eukaryota.
DR GeneTree; ENSGT01020000230351; -.
DR HOGENOM; CLU_034469_2_0_1; -.
DR InParanoid; P51576; -.
DR OMA; ARHFMEN; -.
DR OrthoDB; 1128763at2759; -.
DR PhylomeDB; P51576; -.
DR TreeFam; TF328633; -.
DR Reactome; R-MMU-139853; Elevation of cytosolic Ca2+ levels.
DR Reactome; R-MMU-418346; Platelet homeostasis.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR BioGRID-ORCS; 18436; 3 hits in 72 CRISPR screens.
DR ChiTaRS; P2rx1; mouse.
DR PRO; PR:P51576; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; P51576; protein.
DR Bgee; ENSMUSG00000020787; Expressed in urinary bladder detrusor smooth muscle and 84 other tissues.
DR ExpressionAtlas; P51576; baseline and differential.
DR Genevisible; P51576; MM.
DR GO; GO:0009897; C:external side of plasma membrane; IDA: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:0099055; C:integral component of postsynaptic membrane; ISO:MGI.
DR GO; GO:0099059; C:integral component of presynaptic active zone membrane; ISO:MGI.
DR GO; GO:0045121; C:membrane raft; ISO:MGI.
DR GO; GO:0043005; C:neuron projection; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0045211; C:postsynaptic membrane; IDA:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; ISO:MGI.
DR GO; GO:0005261; F:cation channel activity; IMP:MGI.
DR GO; GO:0004931; F:extracellularly ATP-gated cation channel activity; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0000166; F:nucleotide binding; ISO:MGI.
DR GO; GO:0097159; F:organic cyclic compound binding; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0001614; F:purinergic nucleotide receptor activity; IMP:MGI.
DR GO; GO:0043924; F:suramin binding; ISO:MGI.
DR GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; IDA:MGI.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0098655; P:cation transmembrane transport; ISO:MGI.
DR GO; GO:0046513; P:ceramide biosynthetic process; IDA:MGI.
DR GO; GO:0051649; P:establishment of localization in cell; IMP:MGI.
DR GO; GO:0007320; P:insemination; IMP:MGI.
DR GO; GO:0034220; P:ion transmembrane transport; ISO:MGI.
DR GO; GO:0006811; P:ion transport; IMP:MGI.
DR GO; GO:0019228; P:neuronal action potential; ISO:MGI.
DR GO; GO:0030168; P:platelet activation; IMP:MGI.
DR GO; GO:1905665; P:positive regulation of calcium ion import across plasma membrane; ISO:MGI.
DR GO; GO:0043270; P:positive regulation of ion transport; IMP:MGI.
DR GO; GO:0008217; P:regulation of blood pressure; ISO:MGI.
DR GO; GO:0051924; P:regulation of calcium ion transport; IMP:MGI.
DR GO; GO:0099509; P:regulation of presynaptic cytosolic calcium ion concentration; ISO:MGI.
DR GO; GO:0006940; P:regulation of smooth muscle contraction; IMP:MGI.
DR GO; GO:2000300; P:regulation of synaptic vesicle exocytosis; ISO:MGI.
DR GO; GO:0003056; P:regulation of vascular associated smooth muscle contraction; IMP:MGI.
DR GO; GO:0019229; P:regulation of vasoconstriction; IMP:MGI.
DR GO; GO:0033198; P:response to ATP; IMP:MGI.
DR GO; GO:0010033; P:response to organic substance; IMP:MGI.
DR GO; GO:0002554; P:serotonin secretion by platelet; IMP:MGI.
DR GO; GO:0035249; P:synaptic transmission, glutamatergic; ISO:MGI.
DR Gene3D; 2.60.490.10; -; 1.
DR InterPro; IPR003044; P2X1_purnocptor.
DR InterPro; IPR027309; P2X_extracellular_dom_sf.
DR InterPro; IPR001429; P2X_purnocptor.
DR PANTHER; PTHR10125:SF9; PTHR10125:SF9; 1.
DR PIRSF; PIRSF005713; P2X_purinoceptor; 1.
DR PRINTS; PR01308; P2X1RECEPTOR.
DR PRINTS; PR01307; P2XRECEPTOR.
DR TIGRFAMs; TIGR00863; P2X; 1.
DR PROSITE; PS01212; P2X_RECEPTOR; 1.
PE 2: Evidence at transcript level;
KW Apoptosis; 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..399
FT /note="P2X purinoceptor 1"
FT /id="PRO_0000161546"
FT TOPO_DOM 1..28
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 29..50
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 51..338
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 339..358
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 359..399
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 331..338
FT /note="Pore-forming motif"
FT /evidence="ECO:0000255"
FT REGION 374..399
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 387
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P51575"
FT MOD_RES 388
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P51575"
FT MOD_RES 389
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P51575"
FT CARBOHYD 153
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 184
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 210
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 300
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 117..165
FT /evidence="ECO:0000250"
FT DISULFID 126..149
FT /evidence="ECO:0000250"
FT DISULFID 132..159
FT /evidence="ECO:0000250"
FT DISULFID 217..227
FT /evidence="ECO:0000250"
FT DISULFID 261..270
FT /evidence="ECO:0000250"
SQ SEQUENCE 399 AA; 44851 MW; 8CBF6B97F569472E CRC64;
MARRLQDELS AFFFEYDTPR MVLVRNKKVG VIFRLIQLVV LVYVIGWVFV YEKGYQTSSG
LISSVSVKLK GLAVTQLQGL GPQVWDVADY VFPAHGDSSF VVMTNFIMTP QQAQGHCAEN
PEGGICQDDS GCTPGKAERK AQGIRTGNCV PFNGTVKTCE IFGWCPVEVD DKIPSPALLH
EAENFTLFIK NSISFPRFKV NRRNLVEEVN GTYMKKCLYH KILHPLCPVF SLGYVVRESG
QDFRSLAEKG GVVGITIDWE CDLDWHVRHC KPIYQFHGLY GEKNLSPGFN FRFARHFVQN
GTNRRHLFKV FGIRFDILVD GKAGKFDIIP TMTTIGSGIG IFGVATVLCD LLLLHILPKR
HYYKQKKFKY AEDMGPGEGE RDPAATSSTL GLQENMRTS
