P2RX7_RAT
ID P2RX7_RAT Reviewed; 595 AA.
AC Q64663;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 160.
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;
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=M33;
RX PubMed=8614837; DOI=10.1126/science.272.5262.735;
RA Surprenant A., Rassendren F., Kawashima E., North R.A., Buell G.N.;
RT "The cytolytic P2Z receptor for extracellular ATP identified as a P2X
RT receptor (P2X7).";
RL Science 272:735-738(1996).
RN [2]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-187 AND ASN-213, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=24090084; DOI=10.1021/pr400783j;
RA Parker B.L., Thaysen-Andersen M., Solis N., Scott N.E., Larsen M.R.,
RA Graham M.E., Packer N.H., Cordwell S.J.;
RT "Site-specific glycan-peptide analysis for determination of N-glycoproteome
RT heterogeneity.";
RL J. Proteome Res. 12:5791-5800(2013).
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.
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.
CC -!- PTM: Phosphorylation results in its inactivation. {ECO:0000250}.
CC -!- PTM: ADP-ribosylation at Arg-125 is necessary and sufficient to
CC activate P2RX7 and gate the channel. {ECO:0000250}.
CC -!- PTM: Palmitoylation of several cysteines in the C-terminal cytoplasmic
CC tail is required for efficient localization to cell surface.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the P2X receptor family. {ECO:0000305}.
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DR EMBL; X95882; CAA65131.1; -; mRNA.
DR RefSeq; NP_062129.1; NM_019256.1.
DR PDB; 6U9V; EM; 2.90 A; A/B/C=1-595.
DR PDB; 6U9W; EM; 3.30 A; A/B/C=1-595.
DR PDBsum; 6U9V; -.
DR PDBsum; 6U9W; -.
DR AlphaFoldDB; Q64663; -.
DR SMR; Q64663; -.
DR BioGRID; 248286; 11.
DR IntAct; Q64663; 2.
DR MINT; Q64663; -.
DR STRING; 10116.ENSRNOP00000001746; -.
DR BindingDB; Q64663; -.
DR ChEMBL; CHEMBL2496; -.
DR GuidetoPHARMACOLOGY; 484; -.
DR TCDB; 1.A.7.1.12; the atp-gated p2x receptor cation channel (p2x receptor) family.
DR GlyGen; Q64663; 6 sites, 8 N-linked glycans (2 sites).
DR iPTMnet; Q64663; -.
DR PhosphoSitePlus; Q64663; -.
DR SwissPalm; Q64663; -.
DR PaxDb; Q64663; -.
DR PRIDE; Q64663; -.
DR GeneID; 29665; -.
DR KEGG; rno:29665; -.
DR UCSC; RGD:3241; rat.
DR CTD; 5027; -.
DR RGD; 3241; P2rx7.
DR VEuPathDB; HostDB:ENSRNOG00000001296; -.
DR eggNOG; ENOG502QSBN; Eukaryota.
DR HOGENOM; CLU_034469_7_0_1; -.
DR InParanoid; Q64663; -.
DR OrthoDB; 1128763at2759; -.
DR PhylomeDB; Q64663; -.
DR TreeFam; TF328633; -.
DR Reactome; R-RNO-139853; Elevation of cytosolic Ca2+ levels.
DR Reactome; R-RNO-418346; Platelet homeostasis.
DR Reactome; R-RNO-844456; The NLRP3 inflammasome.
DR PRO; PR:Q64663; -.
DR Proteomes; UP000002494; Chromosome 12.
DR Bgee; ENSRNOG00000001296; Expressed in liver and 19 other tissues.
DR ExpressionAtlas; Q64663; baseline and differential.
DR Genevisible; Q64663; RN.
DR GO; GO:0032059; C:bleb; IDA:BHF-UCL.
DR GO; GO:0005911; C:cell-cell junction; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
DR GO; GO:0009897; C:external side of plasma membrane; ISO:RGD.
DR GO; GO:0005639; C:integral component of nuclear inner membrane; IDA:RGD.
DR GO; GO:0005887; C:integral component of plasma membrane; ISO:RGD.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0045121; C:membrane raft; IDA:RGD.
DR GO; GO:0031594; C:neuromuscular junction; ISO:RGD.
DR GO; GO:0043005; C:neuron projection; IDA:RGD.
DR GO; GO:0043025; C:neuronal cell body; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA:BHF-UCL.
DR GO; GO:0098794; C:postsynapse; IEA:GOC.
DR GO; GO:0032991; C:protein-containing complex; IDA:RGD.
DR GO; GO:0045202; C:synapse; ISO:RGD.
DR GO; GO:0043195; C:terminal bouton; IDA:RGD.
DR GO; GO:0005524; F:ATP binding; IDA:RGD.
DR GO; GO:0015267; F:channel activity; IDA:MGI.
DR GO; GO:0005507; F:copper ion binding; IDA:RGD.
DR GO; GO:0004931; F:extracellularly ATP-gated cation channel activity; IDA:BHF-UCL.
DR GO; GO:0042802; F:identical protein binding; IPI:BHF-UCL.
DR GO; GO:0001530; F:lipopolysaccharide binding; ISO:RGD.
DR GO; GO:0000287; F:magnesium ion binding; IDA:RGD.
DR GO; GO:0043539; F:protein serine/threonine kinase activator activity; IMP:RGD.
DR GO; GO:0001614; F:purinergic nucleotide receptor activity; IDA:BHF-UCL.
DR GO; GO:0097110; F:scaffold protein binding; IPI:RGD.
DR GO; GO:0038023; F:signaling receptor activity; ISO:RGD.
DR GO; GO:0005102; F:signaling receptor binding; IPI:BHF-UCL.
DR GO; GO:0008270; F:zinc ion binding; IDA:RGD.
DR GO; GO:0097190; P:apoptotic signaling pathway; IDA:BHF-UCL.
DR GO; GO:1904669; P:ATP export; IMP:RGD.
DR GO; GO:0032060; P:bleb assembly; IDA:BHF-UCL.
DR GO; GO:0006816; P:calcium ion transport; ISO:RGD.
DR GO; GO:0006812; P:cation transport; ISO:RGD.
DR GO; GO:0008219; P:cell death; ISO:RGD.
DR GO; GO:0000902; P:cell morphogenesis; ISO:RGD.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IDA:BHF-UCL.
DR GO; GO:0006884; P:cell volume homeostasis; ISO:RGD.
DR GO; GO:0071359; P:cellular response to dsRNA; ISO:RGD.
DR GO; GO:0031668; P:cellular response to extracellular stimulus; ISO:RGD.
DR GO; GO:0071407; P:cellular response to organic cyclic compound; ISO:RGD.
DR GO; GO:0046513; P:ceramide biosynthetic process; ISO:RGD.
DR GO; GO:0032963; P:collagen metabolic process; ISO:RGD.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; ISO:RGD.
DR GO; GO:0097191; P:extrinsic apoptotic signaling pathway; IDA:BHF-UCL.
DR GO; GO:0010467; P:gene expression; ISO:RGD.
DR GO; GO:0048873; P:homeostasis of number of cells within a tissue; ISO:RGD.
DR GO; GO:0006954; P:inflammatory response; ISO:RGD.
DR GO; GO:0051899; P:membrane depolarization; IDA:BHF-UCL.
DR GO; GO:0006509; P:membrane protein ectodomain proteolysis; ISO:RGD.
DR GO; GO:0007005; P:mitochondrion organization; ISO:RGD.
DR GO; GO:0043132; P:NAD transport; ISO:RGD.
DR GO; GO:0045779; P:negative regulation of bone resorption; ISO:RGD.
DR GO; GO:0045794; P:negative regulation of cell volume; ISO:RGD.
DR GO; GO:0043409; P:negative regulation of MAPK cascade; ISO:RGD.
DR GO; GO:0019228; P:neuronal action potential; IDA:RGD.
DR GO; GO:0015695; P:organic cation transport; TAS:RGD.
DR GO; GO:0001845; P:phagolysosome assembly; ISO:RGD.
DR GO; GO:0006649; P:phospholipid transfer to membrane; ISO:RGD.
DR GO; GO:0045332; P:phospholipid translocation; ISO:RGD.
DR GO; GO:0007009; P:plasma membrane organization; ISO:RGD.
DR GO; GO:0017121; P:plasma membrane phospholipid scrambling; ISO:RGD.
DR GO; GO:0046931; P:pore complex assembly; IDA:RGD.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISO:RGD.
DR GO; GO:1904172; P:positive regulation of bleb assembly; ISO:RGD.
DR GO; GO:0030501; P:positive regulation of bone mineralization; ISO:RGD.
DR GO; GO:0010524; P:positive regulation of calcium ion transport into cytosol; ISO:RGD.
DR GO; GO:0043085; P:positive regulation of catalytic activity; ISO:RGD.
DR GO; GO:0001819; P:positive regulation of cytokine production; ISO:RGD.
DR GO; GO:0051495; P:positive regulation of cytoskeleton organization; IDA:BHF-UCL.
DR GO; GO:0014054; P:positive regulation of gamma-aminobutyric acid secretion; ISO:RGD.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:RGD.
DR GO; GO:0014049; P:positive regulation of glutamate secretion; ISO:RGD.
DR GO; GO:0045821; P:positive regulation of glycolytic process; ISO:RGD.
DR GO; GO:0032730; P:positive regulation of interleukin-1 alpha production; ISO:RGD.
DR GO; GO:0032731; P:positive regulation of interleukin-1 beta production; IDA:RGD.
DR GO; GO:0032755; P:positive regulation of interleukin-6 production; ISO:RGD.
DR GO; GO:0034767; P:positive regulation of ion transmembrane transport; ISO:RGD.
DR GO; GO:0070230; P:positive regulation of lymphocyte apoptotic process; ISO:RGD.
DR GO; GO:0043406; P:positive regulation of MAP kinase activity; ISO:RGD.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; ISO:RGD.
DR GO; GO:0051901; P:positive regulation of mitochondrial depolarization; ISO:RGD.
DR GO; GO:0045778; P:positive regulation of ossification; ISO:RGD.
DR GO; GO:0032308; P:positive regulation of prostaglandin secretion; ISO:RGD.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IDA:RGD.
DR GO; GO:0050714; P:positive regulation of protein secretion; ISO:RGD.
DR GO; GO:0001916; P:positive regulation of T cell mediated cytotoxicity; ISO:RGD.
DR GO; GO:0012501; P:programmed cell death; ISO:RGD.
DR GO; GO:0030163; P:protein catabolic process; ISO:RGD.
DR GO; GO:0006468; P:protein phosphorylation; ISO:RGD.
DR GO; GO:0016485; P:protein processing; ISO:RGD.
DR GO; GO:0035590; P:purinergic nucleotide receptor signaling pathway; ISO:RGD.
DR GO; GO:0072593; P:reactive oxygen species metabolic process; ISO:RGD.
DR GO; GO:0099161; P:regulation of presynaptic dense core granule exocytosis; IDA:SynGO.
DR GO; GO:0002028; P:regulation of sodium ion transport; IDA:BHF-UCL.
DR GO; GO:0051209; P:release of sequestered calcium ion into cytosol; ISO:RGD.
DR GO; GO:0033198; P:response to ATP; IDA:BHF-UCL.
DR GO; GO:0009617; P:response to bacterium; ISO:RGD.
DR GO; GO:0051592; P:response to calcium ion; ISO:RGD.
DR GO; GO:0051602; P:response to electrical stimulus; ISO:RGD.
DR GO; GO:0034405; P:response to fluid shear stress; ISO:RGD.
DR GO; GO:0032496; P:response to lipopolysaccharide; ISO:RGD.
DR GO; GO:0009612; P:response to mechanical stimulus; ISO:RGD.
DR GO; GO:0014070; P:response to organic cyclic compound; ISO:RGD.
DR GO; GO:0010033; P:response to organic substance; ISO:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; ISO:RGD.
DR GO; GO:0010043; P:response to zinc ion; ISO:RGD.
DR GO; GO:0019233; P:sensory perception of pain; ISO:RGD.
DR GO; GO:0048705; P:skeletal system morphogenesis; ISO:RGD.
DR GO; GO:0016079; P:synaptic vesicle exocytosis; ISO:RGD.
DR GO; GO:0043029; P:T cell homeostasis; ISO:RGD.
DR GO; GO:0042098; P:T cell proliferation; ISO:RGD.
DR GO; GO:0006900; P:vesicle budding from membrane; ISO:RGD.
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 3D-structure; ADP-ribosylation; Cell membrane; Disulfide bond;
KW Glycoprotein; Ion channel; Ion transport; Ligand-gated ion channel;
KW Lipoprotein; Membrane; Palmitate; Phosphoprotein; Receptor;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..595
FT /note="P2X purinoceptor 7"
FT /id="PRO_0000161562"
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"
FT /evidence="ECO:0000250"
FT CARBOHYD 74
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 187
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0007744|PubMed:24090084"
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:0007744|PubMed:24090084"
FT CARBOHYD 241
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 284
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 HELIX 7..10
FT /evidence="ECO:0007829|PDB:6U9V"
FT STRAND 12..16
FT /evidence="ECO:0007829|PDB:6U9V"
FT STRAND 18..22
FT /evidence="ECO:0007829|PDB:6U9V"
FT HELIX 24..48
FT /evidence="ECO:0007829|PDB:6U9V"
FT TURN 49..51
FT /evidence="ECO:0007829|PDB:6U9W"
FT STRAND 52..55
FT /evidence="ECO:0007829|PDB:6U9V"
FT STRAND 58..66
FT /evidence="ECO:0007829|PDB:6U9V"
FT STRAND 69..72
FT /evidence="ECO:0007829|PDB:6U9V"
FT STRAND 85..88
FT /evidence="ECO:0007829|PDB:6U9V"
FT HELIX 90..93
FT /evidence="ECO:0007829|PDB:6U9V"
FT STRAND 99..118
FT /evidence="ECO:0007829|PDB:6U9V"
FT STRAND 131..133
FT /evidence="ECO:0007829|PDB:6U9V"
FT STRAND 142..146
FT /evidence="ECO:0007829|PDB:6U9V"
FT STRAND 156..158
FT /evidence="ECO:0007829|PDB:6U9V"
FT STRAND 166..170
FT /evidence="ECO:0007829|PDB:6U9V"
FT TURN 183..186
FT /evidence="ECO:0007829|PDB:6U9V"
FT STRAND 189..198
FT /evidence="ECO:0007829|PDB:6U9V"
FT TURN 199..202
FT /evidence="ECO:0007829|PDB:6U9V"
FT STRAND 203..207
FT /evidence="ECO:0007829|PDB:6U9V"
FT STRAND 220..222
FT /evidence="ECO:0007829|PDB:6U9V"
FT STRAND 228..230
FT /evidence="ECO:0007829|PDB:6U9V"
FT HELIX 231..237
FT /evidence="ECO:0007829|PDB:6U9V"
FT HELIX 242..247
FT /evidence="ECO:0007829|PDB:6U9V"
FT STRAND 251..261
FT /evidence="ECO:0007829|PDB:6U9V"
FT HELIX 264..266
FT /evidence="ECO:0007829|PDB:6U9V"
FT STRAND 271..277
FT /evidence="ECO:0007829|PDB:6U9V"
FT STRAND 285..287
FT /evidence="ECO:0007829|PDB:6U9V"
FT STRAND 292..301
FT /evidence="ECO:0007829|PDB:6U9V"
FT STRAND 304..328
FT /evidence="ECO:0007829|PDB:6U9V"
FT HELIX 330..340
FT /evidence="ECO:0007829|PDB:6U9V"
FT HELIX 341..345
FT /evidence="ECO:0007829|PDB:6U9V"
FT HELIX 346..358
FT /evidence="ECO:0007829|PDB:6U9V"
FT HELIX 361..365
FT /evidence="ECO:0007829|PDB:6U9V"
FT HELIX 367..371
FT /evidence="ECO:0007829|PDB:6U9V"
FT STRAND 372..374
FT /evidence="ECO:0007829|PDB:6U9V"
FT HELIX 375..378
FT /evidence="ECO:0007829|PDB:6U9V"
FT HELIX 379..387
FT /evidence="ECO:0007829|PDB:6U9V"
FT STRAND 388..392
FT /evidence="ECO:0007829|PDB:6U9W"
FT STRAND 399..402
FT /evidence="ECO:0007829|PDB:6U9V"
FT STRAND 404..412
FT /evidence="ECO:0007829|PDB:6U9V"
FT STRAND 417..419
FT /evidence="ECO:0007829|PDB:6U9V"
FT TURN 421..423
FT /evidence="ECO:0007829|PDB:6U9V"
FT STRAND 427..429
FT /evidence="ECO:0007829|PDB:6U9V"
FT HELIX 436..439
FT /evidence="ECO:0007829|PDB:6U9V"
FT STRAND 478..481
FT /evidence="ECO:0007829|PDB:6U9V"
FT HELIX 489..491
FT /evidence="ECO:0007829|PDB:6U9V"
FT HELIX 493..495
FT /evidence="ECO:0007829|PDB:6U9W"
FT STRAND 501..504
FT /evidence="ECO:0007829|PDB:6U9V"
FT HELIX 507..509
FT /evidence="ECO:0007829|PDB:6U9V"
FT HELIX 511..516
FT /evidence="ECO:0007829|PDB:6U9V"
FT HELIX 520..530
FT /evidence="ECO:0007829|PDB:6U9V"
FT HELIX 542..557
FT /evidence="ECO:0007829|PDB:6U9V"
FT HELIX 561..564
FT /evidence="ECO:0007829|PDB:6U9V"
FT HELIX 571..580
FT /evidence="ECO:0007829|PDB:6U9V"
FT STRAND 584..586
FT /evidence="ECO:0007829|PDB:6U9V"
SQ SEQUENCE 595 AA; 68392 MW; 4A6DD6058E5988D3 CRC64;
MPACCSWNDV FQYETNKVTR IQSVNYGTIK WILHMTVFSY VSFALMSDKL YQRKEPLISS
VHTKVKGVAE VTENVTEGGV TKLVHGIFDT ADYTLPLQGN SFFVMTNYLK SEGQEQKLCP
EYPSRGKQCH SDQGCIKGWM DPQSKGIQTG RCIPYDQKRK TCEIFAWCPA EEGKEAPRPA
LLRSAENFTV LIKNNIDFPG HNYTTRNILP GMNISCTFHK TWNPQCPIFR LGDIFQEIGE
NFTEVAVQGG IMGIEIYWDC NLDSWSHRCQ PKYSFRRLDD KYTNESLFPG YNFRYAKYYK
ENGMEKRTLI KAFGVRFDIL VFGTGGKFDI IQLVVYIGST LSYFGLATVC IDLIINTYAS
TCCRSRVYPS CKCCEPCAVN EYYYRKKCEP IVEPKPTLKY VSFVDEPHIW MVDQQLLGKS
LQDVKGQEVP RPQTDFLELS RLSLSLHHSP PIPGQPEEMQ LLQIEAVPRS RDSPDWCQCG
NCLPSQLPEN RRALEELCCR RKPGQCITTS ELFSKIVLSR EALQLLLLYQ EPLLALEGEA
INSKLRHCAY RSYATWRFVS QDMADFAILP SCCRWKIRKE FPKTQGQYSG FKYPY
