P2RX7_MOUSE
ID P2RX7_MOUSE Reviewed; 595 AA.
AC Q9Z1M0;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=P2X purinoceptor 7;
DE Short=P2X7;
DE AltName: Full=ATP receptor;
DE AltName: Full=P2Z receptor;
DE AltName: Full=Purinergic receptor;
GN Name=P2rx7; Synonyms=P2x7;
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=9849870; DOI=10.1016/s0014-5793(98)01332-5;
RA Chessell I.P., Simon J., Hibell A.D., Michel A.D., Barnard E.A.,
RA Humphrey P.P.;
RT "Cloning and functional characterisation of the mouse P2X7 receptor.";
RL FEBS Lett. 439:26-30(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 ADP-RIBOSYLATION AT ARG-125 AND ARG-133 BY ART2B, AND MUTAGENESIS OF
RP ARG-125 AND ARG-133.
RX PubMed=17928361; DOI=10.1096/fj.07-9294com;
RA Adriouch S., Bannas P., Schwarz N., Fliegert R., Guse A.H., Seman M.,
RA Haag F., Koch-Nolte F.;
RT "ADP-ribosylation at R125 gates the P2X7 ion channel by presenting a
RT covalent ligand to its nucleotide binding site.";
RL FASEB J. 22:861-869(2008).
RN [4]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-74.
RX PubMed=19349973; DOI=10.1038/nbt.1532;
RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA Schiess R., Aebersold R., Watts J.D.;
RT "Mass-spectrometric identification and relative quantification of N-linked
RT cell surface glycoproteins.";
RL Nat. Biotechnol. 27:378-386(2009).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Receptor for ATP that acts as a ligand-gated ion channel.
CC Responsible for ATP-dependent lysis of macrophages through the
CC formation of membrane pores permeable to large molecules. Could
CC function in both fast synaptic transmission and the ATP-mediated lysis
CC of antigen-presenting cells. In the absence of its natural ligand, ATP,
CC functions as a scavenger receptor in the recognition and engulfment of
CC apoptotic cells. {ECO:0000250|UniProtKB:Q99572}.
CC -!- SUBUNIT: Functional P2XRs are organized as homomeric and heteromeric
CC trimers. Interacts with LAMA3, ITGB2, ACTB, ACTN4, SVIL, MPP3, HSPA1,
CC HSPCB, HSPA8, PIK230 and PTPRB (By similarity). Interacts (via C-
CC terminus) with EMP2 (By similarity). {ECO:0000250|UniProtKB:Q99572}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q99572};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- PTM: Phosphorylation results in its inactivation.
CC {ECO:0000250|UniProtKB:Q99572}.
CC -!- PTM: ADP-ribosylation at Arg-125 is necessary and sufficient to
CC activate P2RX7 and gate the channel.
CC -!- PTM: Palmitoylation of several cysteines in the C-terminal cytoplasmic
CC tail is required for efficient localization to cell surface.
CC {ECO:0000250|UniProtKB:Q99572}.
CC -!- SIMILARITY: Belongs to the P2X receptor family. {ECO:0000305}.
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DR EMBL; AJ009823; CAA08853.1; -; mRNA.
DR EMBL; AC114632; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS19652.1; -.
DR RefSeq; NP_035157.2; NM_011027.3.
DR AlphaFoldDB; Q9Z1M0; -.
DR SMR; Q9Z1M0; -.
DR BioGRID; 202002; 5.
DR IntAct; Q9Z1M0; 1.
DR STRING; 10090.ENSMUSP00000098303; -.
DR BindingDB; Q9Z1M0; -.
DR ChEMBL; CHEMBL5183; -.
DR GuidetoPHARMACOLOGY; 484; -.
DR GlyConnect; 2573; 6 N-Linked glycans (3 sites).
DR GlyGen; Q9Z1M0; 5 sites, 5 N-linked glycans (3 sites).
DR iPTMnet; Q9Z1M0; -.
DR PhosphoSitePlus; Q9Z1M0; -.
DR SwissPalm; Q9Z1M0; -.
DR MaxQB; Q9Z1M0; -.
DR PaxDb; Q9Z1M0; -.
DR PRIDE; Q9Z1M0; -.
DR ProteomicsDB; 294303; -.
DR Antibodypedia; 19042; 453 antibodies from 43 providers.
DR DNASU; 18439; -.
DR Ensembl; ENSMUST00000100737; ENSMUSP00000098303; ENSMUSG00000029468.
DR GeneID; 18439; -.
DR KEGG; mmu:18439; -.
DR UCSC; uc008zlq.2; mouse.
DR CTD; 5027; -.
DR MGI; MGI:1339957; P2rx7.
DR VEuPathDB; HostDB:ENSMUSG00000029468; -.
DR eggNOG; ENOG502QSBN; Eukaryota.
DR GeneTree; ENSGT01020000230351; -.
DR InParanoid; Q9Z1M0; -.
DR OMA; YRKKCET; -.
DR OrthoDB; 1128763at2759; -.
DR PhylomeDB; Q9Z1M0; -.
DR TreeFam; TF328633; -.
DR Reactome; R-MMU-139853; Elevation of cytosolic Ca2+ levels.
DR Reactome; R-MMU-418346; Platelet homeostasis.
DR Reactome; R-MMU-844456; The NLRP3 inflammasome.
DR BioGRID-ORCS; 18439; 2 hits in 72 CRISPR screens.
DR ChiTaRS; P2rx7; mouse.
DR PRO; PR:Q9Z1M0; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q9Z1M0; protein.
DR Bgee; ENSMUSG00000029468; Expressed in heart right ventricle and 84 other tissues.
DR ExpressionAtlas; Q9Z1M0; baseline and differential.
DR Genevisible; Q9Z1M0; MM.
DR GO; GO:0032059; C:bleb; ISO:MGI.
DR GO; GO:0005911; C:cell-cell junction; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR GO; GO:0005639; C:integral component of nuclear inner membrane; ISO:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; IMP:MGI.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0045121; C:membrane raft; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; IEA:GOC.
DR GO; GO:0031594; C:neuromuscular junction; IDA:MGI.
DR GO; GO:0043005; C:neuron projection; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0098794; C:postsynapse; IEA:GOC.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0045202; C:synapse; IDA:MGI.
DR GO; GO:0043195; C:terminal bouton; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; IMP:MGI.
DR GO; GO:0015267; F:channel activity; IMP:MGI.
DR GO; GO:0005507; F:copper ion binding; ISO:MGI.
DR GO; GO:0004931; F:extracellularly ATP-gated cation channel activity; IMP:MGI.
DR GO; GO:0042802; F:identical protein binding; IPI:MGI.
DR GO; GO:0001530; F:lipopolysaccharide binding; IDA:MGI.
DR GO; GO:0000287; F:magnesium ion binding; ISO:MGI.
DR GO; GO:0043539; F:protein serine/threonine kinase activator activity; ISO:MGI.
DR GO; GO:0001614; F:purinergic nucleotide receptor activity; ISO:MGI.
DR GO; GO:0097110; F:scaffold protein binding; ISO:MGI.
DR GO; GO:0038023; F:signaling receptor activity; IMP:MGI.
DR GO; GO:0005102; F:signaling receptor binding; ISO:MGI.
DR GO; GO:0008270; F:zinc ion binding; ISO:MGI.
DR GO; GO:0097190; P:apoptotic signaling pathway; ISO:MGI.
DR GO; GO:1904669; P:ATP export; ISO:MGI.
DR GO; GO:0032060; P:bleb assembly; IMP:UniProtKB.
DR GO; GO:0006816; P:calcium ion transport; IMP:MGI.
DR GO; GO:0006812; P:cation transport; IMP:MGI.
DR GO; GO:0008219; P:cell death; IDA:MGI.
DR GO; GO:0000902; P:cell morphogenesis; IMP:MGI.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; ISO:MGI.
DR GO; GO:0006884; P:cell volume homeostasis; IDA:MGI.
DR GO; GO:0071359; P:cellular response to dsRNA; IMP:MGI.
DR GO; GO:0031668; P:cellular response to extracellular stimulus; IMP:MGI.
DR GO; GO:0071407; P:cellular response to organic cyclic compound; IDA:MGI.
DR GO; GO:0046513; P:ceramide biosynthetic process; IDA:MGI.
DR GO; GO:0032963; P:collagen metabolic process; IMP:MGI.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IMP:MGI.
DR GO; GO:0051649; P:establishment of localization in cell; IDA:MGI.
DR GO; GO:0097191; P:extrinsic apoptotic signaling pathway; IMP:MGI.
DR GO; GO:0014051; P:gamma-aminobutyric acid secretion; IMP:MGI.
DR GO; GO:0010467; P:gene expression; IMP:MGI.
DR GO; GO:0014047; P:glutamate secretion; IMP:MGI.
DR GO; GO:0048873; P:homeostasis of number of cells within a tissue; IMP:MGI.
DR GO; GO:0006954; P:inflammatory response; IMP:MGI.
DR GO; GO:0070227; P:lymphocyte apoptotic process; IMP:MGI.
DR GO; GO:0000165; P:MAPK cascade; IMP:MGI.
DR GO; GO:0051899; P:membrane depolarization; ISO:MGI.
DR GO; GO:0006509; P:membrane protein ectodomain proteolysis; IMP:MGI.
DR GO; GO:0051882; P:mitochondrial depolarization; IMP:MGI.
DR GO; GO:0007005; P:mitochondrion organization; IDA:MGI.
DR GO; GO:0043132; P:NAD transport; IMP:MGI.
DR GO; GO:0045779; P:negative regulation of bone resorption; IMP:MGI.
DR GO; GO:0045794; P:negative regulation of cell volume; IMP:UniProtKB.
DR GO; GO:0043409; P:negative regulation of MAPK cascade; IDA:MGI.
DR GO; GO:0019228; P:neuronal action potential; ISO:MGI.
DR GO; GO:0001845; P:phagolysosome assembly; IMP:MGI.
DR GO; GO:0006649; P:phospholipid transfer to membrane; IMP:MGI.
DR GO; GO:0045332; P:phospholipid translocation; IDA:MGI.
DR GO; GO:0007009; P:plasma membrane organization; IDA:MGI.
DR GO; GO:0017121; P:plasma membrane phospholipid scrambling; ISO:MGI.
DR GO; GO:0046931; P:pore complex assembly; IMP:MGI.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IMP:MGI.
DR GO; GO:1904172; P:positive regulation of bleb assembly; ISO:MGI.
DR GO; GO:0030501; P:positive regulation of bone mineralization; IMP:MGI.
DR GO; GO:0010524; P:positive regulation of calcium ion transport into cytosol; ISO:MGI.
DR GO; GO:0043085; P:positive regulation of catalytic activity; IMP:MGI.
DR GO; GO:0051495; P:positive regulation of cytoskeleton organization; ISO:MGI.
DR GO; GO:0014054; P:positive regulation of gamma-aminobutyric acid secretion; IMP:MGI.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI.
DR GO; GO:0014049; P:positive regulation of glutamate secretion; IMP:MGI.
DR GO; GO:0045821; P:positive regulation of glycolytic process; ISO:MGI.
DR GO; GO:0032730; P:positive regulation of interleukin-1 alpha production; IMP:MGI.
DR GO; GO:0032731; P:positive regulation of interleukin-1 beta production; IMP:MGI.
DR GO; GO:0032755; P:positive regulation of interleukin-6 production; IMP:MGI.
DR GO; GO:0034767; P:positive regulation of ion transmembrane transport; ISO:MGI.
DR GO; GO:0070230; P:positive regulation of lymphocyte apoptotic process; IMP:MGI.
DR GO; GO:0060907; P:positive regulation of macrophage cytokine production; IMP:MGI.
DR GO; GO:0043406; P:positive regulation of MAP kinase activity; IMP:MGI.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; IMP:MGI.
DR GO; GO:0051901; P:positive regulation of mitochondrial depolarization; IMP:MGI.
DR GO; GO:0045778; P:positive regulation of ossification; IMP:MGI.
DR GO; GO:0032308; P:positive regulation of prostaglandin secretion; IMP:MGI.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IMP:MGI.
DR GO; GO:0050714; P:positive regulation of protein secretion; IDA:MGI.
DR GO; GO:0070234; P:positive regulation of T cell apoptotic process; IMP:MGI.
DR GO; GO:0001916; P:positive regulation of T cell mediated cytotoxicity; IMP:MGI.
DR GO; GO:0012501; P:programmed cell death; IDA:MGI.
DR GO; GO:0032310; P:prostaglandin secretion; IMP:MGI.
DR GO; GO:0030163; P:protein catabolic process; IDA:MGI.
DR GO; GO:0006468; P:protein phosphorylation; IMP:MGI.
DR GO; GO:0016485; P:protein processing; IMP:MGI.
DR GO; GO:0009306; P:protein secretion; IDA:MGI.
DR GO; GO:0035590; P:purinergic nucleotide receptor signaling pathway; ISO:MGI.
DR GO; GO:0072593; P:reactive oxygen species metabolic process; IMP:MGI.
DR GO; GO:0099161; P:regulation of presynaptic dense core granule exocytosis; ISO:MGI.
DR GO; GO:0002028; P:regulation of sodium ion transport; ISO:MGI.
DR GO; GO:0051209; P:release of sequestered calcium ion into cytosol; IMP:MGI.
DR GO; GO:0033198; P:response to ATP; IDA:MGI.
DR GO; GO:0009617; P:response to bacterium; IMP:MGI.
DR GO; GO:0051592; P:response to calcium ion; IDA:MGI.
DR GO; GO:0051602; P:response to electrical stimulus; IMP:MGI.
DR GO; GO:0034405; P:response to fluid shear stress; IMP:MGI.
DR GO; GO:0032496; P:response to lipopolysaccharide; IDA:MGI.
DR GO; GO:0009612; P:response to mechanical stimulus; IMP:MGI.
DR GO; GO:0014070; P:response to organic cyclic compound; IDA:MGI.
DR GO; GO:0010033; P:response to organic substance; IMP:MGI.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IMP:MGI.
DR GO; GO:0010043; P:response to zinc ion; IMP:MGI.
DR GO; GO:0019233; P:sensory perception of pain; IMP:BHF-UCL.
DR GO; GO:0048705; P:skeletal system morphogenesis; IMP:MGI.
DR GO; GO:0016079; P:synaptic vesicle exocytosis; IMP:MGI.
DR GO; GO:0070231; P:T cell apoptotic process; IMP:MGI.
DR GO; GO:0043029; P:T cell homeostasis; IMP:MGI.
DR GO; GO:0001913; P:T cell mediated cytotoxicity; IMP:MGI.
DR GO; GO:0042098; P:T cell proliferation; IMP:MGI.
DR GO; GO:0006900; P:vesicle budding from membrane; IMP:MGI.
DR Gene3D; 2.60.490.10; -; 1.
DR InterPro; IPR003050; P2X7_purinoceptor.
DR InterPro; IPR027309; P2X_extracellular_dom_sf.
DR InterPro; IPR001429; P2X_purnocptor.
DR PANTHER; PTHR10125:SF13; PTHR10125:SF13; 1.
DR PRINTS; PR01314; P2X7RECEPTOR.
DR PRINTS; PR01307; P2XRECEPTOR.
DR TIGRFAMs; TIGR00863; P2X; 1.
DR PROSITE; PS01212; P2X_RECEPTOR; 1.
PE 1: Evidence at protein level;
KW ADP-ribosylation; Cell membrane; Disulfide bond; Glycoprotein; Ion channel;
KW Ion transport; Ligand-gated ion channel; Lipoprotein; Membrane; Palmitate;
KW Phosphoprotein; Receptor; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..595
FT /note="P2X purinoceptor 7"
FT /id="PRO_0000161561"
FT TOPO_DOM 1..25
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 26..46
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 47..334
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 335..355
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 356..595
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOD_RES 125
FT /note="ADP-ribosylarginine; by ART2B"
FT /evidence="ECO:0000269|PubMed:17928361"
FT MOD_RES 133
FT /note="ADP-ribosylarginine; by ART2B"
FT /evidence="ECO:0000269|PubMed:17928361"
FT MOD_RES 390
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99572"
FT CARBOHYD 74
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT CARBOHYD 187
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 202
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 213
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 241
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 119..168
FT /evidence="ECO:0000250"
FT DISULFID 129..152
FT /evidence="ECO:0000250"
FT DISULFID 135..162
FT /evidence="ECO:0000250"
FT DISULFID 216..226
FT /evidence="ECO:0000250"
FT DISULFID 260..269
FT /evidence="ECO:0000250"
FT MUTAGEN 125
FT /note="R->K: Abolishes calcium responses to NAD."
FT /evidence="ECO:0000269|PubMed:17928361"
FT MUTAGEN 133
FT /note="R->K: No effect on calcium responses to NAD."
FT /evidence="ECO:0000269|PubMed:17928361"
FT CONFLICT 11
FT /note="L -> F (in Ref. 1; CAA08853)"
FT /evidence="ECO:0000305"
FT CONFLICT 221
FT /note="T -> A (in Ref. 1; CAA08853)"
FT /evidence="ECO:0000305"
FT CONFLICT 283
FT /note="T -> M (in Ref. 1; CAA08853)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 595 AA; 68388 MW; BE007FE195AF50A4 CRC64;
MPACCSWNDV LQYETNKVTR IQSTNYGTVK WVLHMIVFSY ISFALVSDKL YQRKEPVISS
VHTKVKGIAE VTENVTEGGV TKLGHSIFDT ADYTFPLQGN SFFVMTNYVK SEGQVQTLCP
EYPRRGAQCS SDRRCKKGWM DPQSKGIQTG RCVPYDKTRK TCEVSAWCPT EEEKEAPRPA
LLRSAENFTV LIKNNIHFPG HNYTTRNILP TMNGSCTFHK TWDPQCSIFR LGDIFQEAGE
NFTEVAVQGG IMGIEIYWDC NLDSWSHHCR PRYSFRRLDD KNTDESFVPG YNFRYAKYYK
ENNVEKRTLI KAFGIRFDIL VFGTGGKFDI IQLVVYIGST LSYFGLATVC IDLLINTYSS
AFCRSGVYPY CKCCEPCTVN EYYYRKKCES IMEPKPTLKY VSFVDEPHIR MVDQQLLGKS
LQVVKGQEVP RPQMDFSDLS RLSLSLHDSP LTPGQSEEIQ LLHEEVAPKS GDSPSWCQCG
NCLPSRLPEQ RRALEELCCR RKPGRCITTS KLFHKLVLSR DTLQLLLLYQ DPLLVLGEEA
TNSRLRHRAY RCYATWRFGS QDMADFAILP SCCRWRIRKE FPKTEGQYSG FKYPY
