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Protein

P2X purinoceptor 7

Gene

P2rx7

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Receptor for ATP that acts as a ligand-gated ion channel. Responsible for ATP-dependent lysis of macrophages through the formation of membrane pores permeable to large molecules. Could function in both fast synaptic transmission and the ATP-mediated lysis of antigen-presenting cells.

GO - Molecular functioni

  1. ATP binding Source: MGI
  2. channel activity Source: MGI
  3. copper ion binding Source: Ensembl
  4. extracellular ATP-gated cation channel activity Source: MGI
  5. lipopolysaccharide binding Source: MGI
  6. magnesium ion binding Source: Ensembl
  7. purinergic nucleotide receptor activity Source: MGI
  8. receptor activity Source: MGI
  9. zinc ion binding Source: Ensembl

GO - Biological processi

  1. activation of MAPK activity Source: MGI
  2. bleb assembly Source: MGI
  3. calcium ion transport Source: MGI
  4. cation transmembrane transport Source: MGI
  5. cation transport Source: MGI
  6. cell morphogenesis Source: MGI
  7. cellular response to extracellular stimulus Source: MGI
  8. cellular response to organic cyclic compound Source: MGI
  9. cell volume homeostasis Source: MGI
  10. ceramide biosynthetic process Source: MGI
  11. collagen metabolic process Source: MGI
  12. cytolysis Source: MGI
  13. defense response to Gram-positive bacterium Source: MGI
  14. extrinsic apoptotic signaling pathway Source: MGI
  15. gene expression Source: MGI
  16. homeostasis of number of cells within a tissue Source: MGI
  17. inflammatory response Source: MGI
  18. membrane budding Source: MGI
  19. membrane depolarization Source: MGI
  20. membrane protein ectodomain proteolysis Source: MGI
  21. mitochondrion organization Source: MGI
  22. multicellular organismal protein catabolic process Source: MGI
  23. NAD transport Source: MGI
  24. negative regulation of bone resorption Source: MGI
  25. negative regulation of MAPK cascade Source: MGI
  26. neuronal action potential Source: Ensembl
  27. phagolysosome assembly Source: MGI
  28. phospholipid transfer to membrane Source: MGI
  29. phospholipid translocation Source: MGI
  30. plasma membrane organization Source: MGI
  31. pore complex assembly Source: MGI
  32. positive regulation of apoptotic process Source: MGI
  33. positive regulation of bone mineralization Source: MGI
  34. positive regulation of calcium ion transport into cytosol Source: MGI
  35. positive regulation of catalytic activity Source: MGI
  36. positive regulation of cytokine secretion Source: MGI
  37. positive regulation of cytolysis Source: Ensembl
  38. positive regulation of cytoskeleton organization Source: Ensembl
  39. positive regulation of gamma-aminobutyric acid secretion Source: MGI
  40. positive regulation of glutamate secretion Source: MGI
  41. positive regulation of interleukin-1 alpha secretion Source: MGI
  42. positive regulation of interleukin-1 beta production Source: MGI
  43. positive regulation of interleukin-1 beta secretion Source: MGI
  44. positive regulation of interleukin-6 production Source: MGI
  45. positive regulation of lymphocyte apoptotic process Source: MGI
  46. positive regulation of MAPK cascade Source: MGI
  47. positive regulation of mitochondrial depolarization Source: MGI
  48. positive regulation of ossification Source: MGI
  49. positive regulation of prostaglandin secretion Source: MGI
  50. positive regulation of protein phosphorylation Source: MGI
  51. positive regulation of protein secretion Source: MGI
  52. positive regulation of T cell mediated cytotoxicity Source: MGI
  53. programmed cell death Source: MGI
  54. protein oligomerization Source: MGI
  55. protein phosphorylation Source: MGI
  56. protein processing Source: MGI
  57. purinergic nucleotide receptor signaling pathway Source: MGI
  58. reactive oxygen species metabolic process Source: MGI
  59. regulation of sodium ion transport Source: Ensembl
  60. release of sequestered calcium ion into cytosol Source: MGI
  61. response to ATP Source: MGI
  62. response to bacterium Source: MGI
  63. response to calcium ion Source: MGI
  64. response to drug Source: MGI
  65. response to electrical stimulus Source: MGI
  66. response to fluid shear stress Source: MGI
  67. response to lipopolysaccharide Source: MGI
  68. response to mechanical stimulus Source: MGI
  69. response to organic cyclic compound Source: MGI
  70. response to organic substance Source: MGI
  71. response to zinc ion Source: MGI
  72. sensory perception of pain Source: BHF-UCL
  73. skeletal system morphogenesis Source: MGI
  74. synaptic vesicle exocytosis Source: MGI
  75. T cell homeostasis Source: MGI
  76. T cell proliferation Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Ion channel, Ligand-gated ion channel, Receptor

Keywords - Biological processi

Ion transport, Transport

Enzyme and pathway databases

ReactomeiREACT_198644. The NLRP3 inflammasome.

Names & Taxonomyi

Protein namesi
Recommended name:
P2X purinoceptor 7
Short name:
P2X7
Alternative name(s):
ATP receptor
P2Z receptor
Purinergic receptor
Gene namesi
Name:P2rx7
Synonyms:P2x7
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 5

Organism-specific databases

MGIiMGI:1339957. P2rx7.

Subcellular locationi

Cell membrane By similarity; Multi-pass membrane protein

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 2525CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei26 – 4621Helical; Name=1Sequence AnalysisAdd
BLAST
Topological domaini47 – 334288ExtracellularSequence AnalysisAdd
BLAST
Transmembranei335 – 35521Helical; Name=2Sequence AnalysisAdd
BLAST
Topological domaini356 – 595240CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. bleb Source: Ensembl
  2. cell-cell junction Source: MGI
  3. cytoplasm Source: Ensembl
  4. external side of plasma membrane Source: MGI
  5. integral component of nuclear inner membrane Source: GO_Central
  6. integral component of plasma membrane Source: MGI
  7. membrane Source: MGI
  8. membrane raft Source: Ensembl
  9. neuromuscular junction Source: MGI
  10. neuronal cell body Source: MGI
  11. plasma membrane Source: MGI
  12. protein complex Source: Ensembl
  13. synapse Source: MGI
  14. terminal bouton Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi125 – 1251R → K: Abolishes calcium responses to NAD. 1 Publication
Mutagenesisi133 – 1331R → K: No effect on calcium responses to NAD. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 595595P2X purinoceptor 7PRO_0000161561Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi74 – 741N-linked (GlcNAc...)1 Publication
Disulfide bondi119 ↔ 168By similarity
Modified residuei125 – 1251ADP-ribosylarginine; by ART2B1 Publication
Disulfide bondi129 ↔ 152By similarity
Modified residuei133 – 1331ADP-ribosylarginine; by ART2B1 Publication
Disulfide bondi135 ↔ 162By similarity
Glycosylationi187 – 1871N-linked (GlcNAc...)Sequence Analysis
Glycosylationi202 – 2021N-linked (GlcNAc...)Sequence Analysis
Glycosylationi213 – 2131N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi216 ↔ 226By similarity
Glycosylationi241 – 2411N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi260 ↔ 269By similarity
Modified residuei390 – 3901PhosphoserineBy similarity

Post-translational modificationi

Phosphorylation results in its inactivation.By similarity
ADP-ribosylation at Arg-125 is necessary and sufficient to activate P2RX7 and gate the channel.
Palmitoylation of several cysteines in the C-terminal cytoplasmic tail is required for efficient localization to cell surface.By similarity

Keywords - PTMi

ADP-ribosylation, Disulfide bond, Glycoprotein, Lipoprotein, Palmitate, Phosphoprotein

Proteomic databases

MaxQBiQ9Z1M0.
PaxDbiQ9Z1M0.
PRIDEiQ9Z1M0.

PTM databases

PhosphoSiteiQ9Z1M0.

Expressioni

Gene expression databases

BgeeiQ9Z1M0.
ExpressionAtlasiQ9Z1M0. baseline and differential.
GenevestigatoriQ9Z1M0.

Interactioni

Subunit structurei

Functional P2XRs are organized as homomeric and heteromeric trimers. Interacts with LAMA3, ITGB2, ACTB, ACTN4, SVIL, MPP3, HSPA1, HSPCB, HSPA8, PIK230 and PTPRB (By similarity). Interacts (via C-terminus) with EMP2 (By similarity).By similarity

Protein-protein interaction databases

BioGridi202002. 1 interaction.

Structurei

3D structure databases

ProteinModelPortaliQ9Z1M0.
SMRiQ9Z1M0. Positions 35-355.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the P2X receptor family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG38999.
GeneTreeiENSGT00390000016028.
HOVERGENiHBG053086.
InParanoidiQ9Z1M0.
KOiK05220.
OMAiLCPEYPT.
OrthoDBiEOG78PV92.
TreeFamiTF328633.

Family and domain databases

Gene3Di2.60.490.10. 1 hit.
InterProiIPR003050. P2X7_purnocptor.
IPR027309. P2X_extracellular_dom.
IPR001429. P2X_purnocptor.
[Graphical view]
PANTHERiPTHR10125. PTHR10125. 1 hit.
PTHR10125:SF13. PTHR10125:SF13. 1 hit.
PfamiPF00864. P2X_receptor. 1 hit.
[Graphical view]
PRINTSiPR01314. P2X7RECEPTOR.
PR01307. P2XRECEPTOR.
TIGRFAMsiTIGR00863. P2X. 1 hit.
PROSITEiPS01212. P2X_RECEPTOR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9Z1M0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPACCSWNDV LQYETNKVTR IQSTNYGTVK WVLHMIVFSY ISFALVSDKL
60 70 80 90 100
YQRKEPVISS VHTKVKGIAE VTENVTEGGV TKLGHSIFDT ADYTFPLQGN
110 120 130 140 150
SFFVMTNYVK SEGQVQTLCP EYPRRGAQCS SDRRCKKGWM DPQSKGIQTG
160 170 180 190 200
RCVPYDKTRK TCEVSAWCPT EEEKEAPRPA LLRSAENFTV LIKNNIHFPG
210 220 230 240 250
HNYTTRNILP TMNGSCTFHK TWDPQCSIFR LGDIFQEAGE NFTEVAVQGG
260 270 280 290 300
IMGIEIYWDC NLDSWSHHCR PRYSFRRLDD KNTDESFVPG YNFRYAKYYK
310 320 330 340 350
ENNVEKRTLI KAFGIRFDIL VFGTGGKFDI IQLVVYIGST LSYFGLATVC
360 370 380 390 400
IDLLINTYSS AFCRSGVYPY CKCCEPCTVN EYYYRKKCES IMEPKPTLKY
410 420 430 440 450
VSFVDEPHIR MVDQQLLGKS LQVVKGQEVP RPQMDFSDLS RLSLSLHDSP
460 470 480 490 500
LTPGQSEEIQ LLHEEVAPKS GDSPSWCQCG NCLPSRLPEQ RRALEELCCR
510 520 530 540 550
RKPGRCITTS KLFHKLVLSR DTLQLLLLYQ DPLLVLGEEA TNSRLRHRAY
560 570 580 590
RCYATWRFGS QDMADFAILP SCCRWRIRKE FPKTEGQYSG FKYPY
Length:595
Mass (Da):68,388
Last modified:July 27, 2011 - v2
Checksum:iBE007FE195AF50A4
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti11 – 111L → F in CAA08853 (PubMed:9849870).Curated
Sequence conflicti221 – 2211T → A in CAA08853 (PubMed:9849870).Curated
Sequence conflicti283 – 2831T → M in CAA08853 (PubMed:9849870).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ009823 mRNA. Translation: CAA08853.1.
AC114632 Genomic DNA. No translation available.
CCDSiCCDS19652.1.
RefSeqiNP_035157.2. NM_011027.3.
UniGeneiMm.42026.

Genome annotation databases

EnsembliENSMUST00000100737; ENSMUSP00000098303; ENSMUSG00000029468.
GeneIDi18439.
KEGGimmu:18439.
UCSCiuc008zlq.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ009823 mRNA. Translation: CAA08853.1.
AC114632 Genomic DNA. No translation available.
CCDSiCCDS19652.1.
RefSeqiNP_035157.2. NM_011027.3.
UniGeneiMm.42026.

3D structure databases

ProteinModelPortaliQ9Z1M0.
SMRiQ9Z1M0. Positions 35-355.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi202002. 1 interaction.

Chemistry

ChEMBLiCHEMBL5183.
GuidetoPHARMACOLOGYi484.

PTM databases

PhosphoSiteiQ9Z1M0.

Proteomic databases

MaxQBiQ9Z1M0.
PaxDbiQ9Z1M0.
PRIDEiQ9Z1M0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000100737; ENSMUSP00000098303; ENSMUSG00000029468.
GeneIDi18439.
KEGGimmu:18439.
UCSCiuc008zlq.1. mouse.

Organism-specific databases

CTDi5027.
MGIiMGI:1339957. P2rx7.

Phylogenomic databases

eggNOGiNOG38999.
GeneTreeiENSGT00390000016028.
HOVERGENiHBG053086.
InParanoidiQ9Z1M0.
KOiK05220.
OMAiLCPEYPT.
OrthoDBiEOG78PV92.
TreeFamiTF328633.

Enzyme and pathway databases

ReactomeiREACT_198644. The NLRP3 inflammasome.

Miscellaneous databases

NextBioi294114.
PROiQ9Z1M0.
SOURCEiSearch...

Gene expression databases

BgeeiQ9Z1M0.
ExpressionAtlasiQ9Z1M0. baseline and differential.
GenevestigatoriQ9Z1M0.

Family and domain databases

Gene3Di2.60.490.10. 1 hit.
InterProiIPR003050. P2X7_purnocptor.
IPR027309. P2X_extracellular_dom.
IPR001429. P2X_purnocptor.
[Graphical view]
PANTHERiPTHR10125. PTHR10125. 1 hit.
PTHR10125:SF13. PTHR10125:SF13. 1 hit.
PfamiPF00864. P2X_receptor. 1 hit.
[Graphical view]
PRINTSiPR01314. P2X7RECEPTOR.
PR01307. P2XRECEPTOR.
TIGRFAMsiTIGR00863. P2X. 1 hit.
PROSITEiPS01212. P2X_RECEPTOR. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and functional characterisation of the mouse P2X7 receptor."
    Chessell I.P., Simon J., Hibell A.D., Michel A.D., Barnard E.A., Humphrey P.P.
    FEBS Lett. 439:26-30(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. "ADP-ribosylation at R125 gates the P2X7 ion channel by presenting a covalent ligand to its nucleotide binding site."
    Adriouch S., Bannas P., Schwarz N., Fliegert R., Guse A.H., Seman M., Haag F., Koch-Nolte F.
    FASEB J. 22:861-869(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: ADP-RIBOSYLATION AT ARG-125 AND ARG-133 BY ART2B, MUTAGENESIS OF ARG-125 AND ARG-133.
  4. "Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."
    Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D.
    Nat. Biotechnol. 27:378-386(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-74.

Entry informationi

Entry nameiP2RX7_MOUSE
AccessioniPrimary (citable) accession number: Q9Z1M0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: July 27, 2011
Last modified: March 4, 2015
This is version 121 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.