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Q9Z1M0 (P2RX7_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 111. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
P2X purinoceptor 7

Short name=P2X7
Alternative name(s):
ATP receptor
P2Z receptor
Purinergic receptor
Gene names
Name:P2rx7
Synonyms:P2x7
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length595 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subunit structure

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.

Subcellular location

Cell membrane By similarity; Multi-pass membrane protein.

Post-translational modification

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.

Sequence similarities

Belongs to the P2X receptor family.

Ontologies

Keywords
   Biological processIon transport
Transport
   Cellular componentCell membrane
Membrane
   DomainTransmembrane
Transmembrane helix
   Molecular functionIon channel
Ligand-gated ion channel
Receptor
   PTMADP-ribosylation
Disulfide bond
Glycoprotein
Lipoprotein
Palmitate
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processNAD transport

Inferred from mutant phenotype PubMed 17803959. Source: MGI

T cell homeostasis

Inferred from mutant phenotype PubMed 16116196. Source: MGI

T cell proliferation

Inferred from mutant phenotype PubMed 15914561. Source: MGI

activation of MAPK activity

Inferred from mutant phenotype PubMed 17306762. Source: MGI

apoptotic signaling pathway

Inferred from electronic annotation. Source: Ensembl

bleb assembly

Inferred from mutant phenotype PubMed 17135244. Source: MGI

calcium ion transport

Inferred from mutant phenotype PubMed 12370338. Source: MGI

cation transport

Inferred from mutant phenotype PubMed 12677010. Source: MGI

cell death

Inferred from direct assay PubMed 18097031. Source: MGI

cell morphogenesis

Inferred from mutant phenotype PubMed 12055263. Source: MGI

cell volume homeostasis

Inferred from direct assay PubMed 18097031. Source: MGI

cellular response to extracellular stimulus

Inferred from mutant phenotype PubMed 18082965. Source: MGI

ceramide biosynthetic process

Inferred from direct assay PubMed 16325464. Source: MGI

collagen metabolic process

Inferred from mutant phenotype PubMed 16969386. Source: MGI

cytolysis

Inferred from direct assay PubMed 16116196PubMed 18097031. Source: MGI

defense response to Gram-positive bacterium

Inferred from mutant phenotype PubMed 11544318. Source: MGI

gene expression

Inferred from mutant phenotype PubMed 18519738. Source: MGI

homeostasis of number of cells within a tissue

Inferred from mutant phenotype PubMed 16969386. Source: MGI

inflammatory response

Inferred from mutant phenotype PubMed 12055263PubMed 16969386. Source: MGI

membrane budding

Inferred from mutant phenotype PubMed 15905573. Source: MGI

membrane depolarization

Inferred from electronic annotation. Source: Ensembl

membrane protein ectodomain proteolysis

Inferred from mutant phenotype PubMed 17286969. Source: MGI

mitochondrion organization

Inferred from direct assay PubMed 16325464. Source: MGI

multicellular organismal protein catabolic process

Inferred from direct assay PubMed 11489964. Source: MGI

negative regulation of MAPK cascade

Inferred from direct assay PubMed 11489964. Source: MGI

negative regulation of bone resorption

Inferred from mutant phenotype PubMed 12677010. Source: MGI

neuronal action potential

Inferred from electronic annotation. Source: Ensembl

phagolysosome assembly

Inferred from mutant phenotype PubMed 11544318. Source: MGI

phospholipid transfer to membrane

Inferred from mutant phenotype PubMed 12370338. Source: MGI

phospholipid translocation

Inferred from direct assay PubMed 18097031. Source: MGI

plasma membrane organization

Inferred from direct assay PubMed 18097031. Source: MGI

pore complex assembly

Inferred from mutant phenotype PubMed 12370338PubMed 15937334PubMed 16269410. Source: MGI

positive regulation of MAPK cascade

Inferred from mutant phenotype PubMed 15937334. Source: MGI

positive regulation of T cell mediated cytotoxicity

Inferred from mutant phenotype PubMed 14761980. Source: MGI

positive regulation of apoptotic process

Inferred from mutant phenotype PubMed 16325464PubMed 16969386. Source: MGI

positive regulation of bone mineralization

Inferred from mutant phenotype PubMed 12677010PubMed 18519738. Source: MGI

positive regulation of calcium ion transport into cytosol

Inferred from electronic annotation. Source: Ensembl

positive regulation of catalytic activity

Inferred from mutant phenotype PubMed 14761980. Source: MGI

positive regulation of cytokine secretion

Inferred from mutant phenotype PubMed 18490713. Source: MGI

positive regulation of cytolysis

Inferred from electronic annotation. Source: Ensembl

positive regulation of cytoskeleton organization

Inferred from electronic annotation. Source: Ensembl

positive regulation of gamma-aminobutyric acid secretion

Inferred from mutant phenotype PubMed 15640761. Source: MGI

positive regulation of glutamate secretion

Inferred from mutant phenotype PubMed 15640761PubMed 17306762. Source: MGI

positive regulation of interleukin-1 alpha secretion

Inferred from mutant phenotype PubMed 18490713. Source: MGI

positive regulation of interleukin-1 beta production

Inferred from mutant phenotype PubMed 11016935. Source: MGI

positive regulation of interleukin-1 beta secretion

Inferred from mutant phenotype PubMed 11016935PubMed 15905573PubMed 18490713. Source: MGI

positive regulation of interleukin-6 production

Inferred from mutant phenotype PubMed 11016935. Source: MGI

positive regulation of lymphocyte apoptotic process

Inferred from mutant phenotype PubMed 16493071. Source: MGI

positive regulation of mitochondrial depolarization

Inferred from mutant phenotype PubMed 16198349. Source: MGI

positive regulation of ossification

Inferred from mutant phenotype PubMed 16269410PubMed 18519738. Source: MGI

positive regulation of prostaglandin secretion

Inferred from mutant phenotype PubMed 16269410. Source: MGI

positive regulation of protein phosphorylation

Inferred from mutant phenotype PubMed 15937334PubMed 17448897. Source: MGI

positive regulation of protein secretion

Inferred from direct assay PubMed 15240711. Source: MGI

protein oligomerization

Inferred from direct assay PubMed 15713258. Source: MGI

protein phosphorylation

Inferred from mutant phenotype PubMed 17306762. Source: MGI

protein processing

Inferred from mutant phenotype PubMed 11016935. Source: MGI

reactive oxygen species metabolic process

Inferred from mutant phenotype PubMed 17448897. Source: MGI

regulation of sodium ion transport

Inferred from electronic annotation. Source: Ensembl

release of sequestered calcium ion into cytosol

Inferred from mutant phenotype PubMed 18082965. Source: MGI

response to ATP

Inferred from direct assay PubMed 15240711PubMed 15713258. Source: MGI

response to bacterium

Inferred from mutant phenotype PubMed 10395640. Source: MGI

response to calcium ion

Inferred from direct assay PubMed 15240711. Source: MGI

response to drug

Inferred from mutant phenotype PubMed 18082965. Source: MGI

response to electrical stimulus

Inferred from mutant phenotype PubMed 15640761. Source: MGI

response to fluid shear stress

Inferred from mutant phenotype PubMed 16269410. Source: MGI

response to lipopolysaccharide

Inferred from direct assay PubMed 15240711. Source: MGI

response to mechanical stimulus

Inferred from mutant phenotype PubMed 16269410. Source: MGI

response to organic cyclic compound

Inferred from direct assay PubMed 15240711. Source: MGI

response to organic substance

Inferred from mutant phenotype PubMed 16116196PubMed 16455971PubMed 17286969. Source: MGI

response to zinc ion

Inferred from mutant phenotype PubMed 15978588PubMed 18082965. Source: MGI

sensory perception of pain

Inferred from mutant phenotype PubMed 15777864. Source: BHF-UCL

skeletal system morphogenesis

Inferred from mutant phenotype PubMed 18519738. Source: MGI

synaptic vesicle exocytosis

Inferred from mutant phenotype PubMed 15713258. Source: MGI

transmembrane transport

Inferred from mutant phenotype PubMed 18519738. Source: GOC

   Cellular_componentbleb

Inferred from electronic annotation. Source: Ensembl

cell-cell junction

Inferred from direct assay PubMed 15331634. Source: MGI

cytoplasm

Inferred from electronic annotation. Source: Ensembl

external side of plasma membrane

Inferred from direct assay PubMed 17286969. Source: MGI

integral component of nuclear inner membrane

Inferred from electronic annotation. Source: Ensembl

integral component of plasma membrane

Inferred from mutant phenotype PubMed 12677010. Source: MGI

membrane

Inferred from direct assay PubMed 15713258. Source: MGI

membrane raft

Inferred from electronic annotation. Source: Ensembl

neuromuscular junction

Inferred from direct assay PubMed 15713258. Source: MGI

neuronal cell body

Inferred from direct assay PubMed 15964665PubMed 15978588. Source: MGI

plasma membrane

Inferred from direct assay PubMed 15331634. Source: MGI

protein complex

Inferred from electronic annotation. Source: Ensembl

synapse

Inferred from direct assay PubMed 18082965. Source: MGI

terminal bouton

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionATP binding

Inferred from mutant phenotype PubMed 12677010. Source: MGI

channel activity

Inferred from mutant phenotype PubMed 18519738. Source: MGI

copper ion binding

Inferred from electronic annotation. Source: Ensembl

extracellular ATP-gated cation channel activity

Inferred from mutant phenotype PubMed 12677010PubMed 15713258. Source: MGI

lipopolysaccharide binding

Inferred from direct assay PubMed 11489964. Source: MGI

magnesium ion binding

Inferred from electronic annotation. Source: Ensembl

purinergic nucleotide receptor activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

receptor activity

Inferred from mutant phenotype PubMed 12677010. Source: MGI

zinc ion binding

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 595595P2X purinoceptor 7
PRO_0000161561

Regions

Topological domain1 – 2525Cytoplasmic Potential
Transmembrane26 – 4621Helical; Name=1; Potential
Topological domain47 – 334288Extracellular Potential
Transmembrane335 – 35521Helical; Name=2; Potential
Topological domain356 – 595240Cytoplasmic Potential

Amino acid modifications

Modified residue1251ADP-ribosylarginine; by ART2B
Modified residue1331ADP-ribosylarginine; by ART2B
Glycosylation741N-linked (GlcNAc...) Ref.4
Glycosylation1871N-linked (GlcNAc...) Potential
Glycosylation2021N-linked (GlcNAc...) Potential
Glycosylation2131N-linked (GlcNAc...) Potential
Glycosylation2411N-linked (GlcNAc...) Potential
Disulfide bond119 ↔ 168 By similarity
Disulfide bond129 ↔ 152 By similarity
Disulfide bond135 ↔ 162 By similarity
Disulfide bond216 ↔ 226 By similarity
Disulfide bond260 ↔ 269 By similarity

Experimental info

Mutagenesis1251R → K: Abolishes calcium responses to NAD. Ref.3
Mutagenesis1331R → K: No effect on calcium responses to NAD. Ref.3
Sequence conflict111L → F in CAA08853. Ref.1
Sequence conflict2211T → A in CAA08853. Ref.1
Sequence conflict2831T → M in CAA08853. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9Z1M0 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: BE007FE195AF50A4

FASTA59568,388
        10         20         30         40         50         60 
MPACCSWNDV LQYETNKVTR IQSTNYGTVK WVLHMIVFSY ISFALVSDKL YQRKEPVISS 

        70         80         90        100        110        120 
VHTKVKGIAE VTENVTEGGV TKLGHSIFDT ADYTFPLQGN SFFVMTNYVK SEGQVQTLCP 

       130        140        150        160        170        180 
EYPRRGAQCS SDRRCKKGWM DPQSKGIQTG RCVPYDKTRK TCEVSAWCPT EEEKEAPRPA 

       190        200        210        220        230        240 
LLRSAENFTV LIKNNIHFPG HNYTTRNILP TMNGSCTFHK TWDPQCSIFR LGDIFQEAGE 

       250        260        270        280        290        300 
NFTEVAVQGG IMGIEIYWDC NLDSWSHHCR PRYSFRRLDD KNTDESFVPG YNFRYAKYYK 

       310        320        330        340        350        360 
ENNVEKRTLI KAFGIRFDIL VFGTGGKFDI IQLVVYIGST LSYFGLATVC IDLLINTYSS 

       370        380        390        400        410        420 
AFCRSGVYPY CKCCEPCTVN EYYYRKKCES IMEPKPTLKY VSFVDEPHIR MVDQQLLGKS 

       430        440        450        460        470        480 
LQVVKGQEVP RPQMDFSDLS RLSLSLHDSP LTPGQSEEIQ LLHEEVAPKS GDSPSWCQCG 

       490        500        510        520        530        540 
NCLPSRLPEQ RRALEELCCR RKPGRCITTS KLFHKLVLSR DTLQLLLLYQ DPLLVLGEEA 

       550        560        570        580        590 
TNSRLRHRAY RCYATWRFGS QDMADFAILP SCCRWRIRKE FPKTEGQYSG FKYPY 

« Hide

References

« Hide 'large scale' references
[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]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ009823 mRNA. Translation: CAA08853.1.
AC114632 Genomic DNA. No translation available.
RefSeqNP_035157.2. NM_011027.3.
UniGeneMm.42026.

3D structure databases

ProteinModelPortalQ9Z1M0.
SMRQ9Z1M0. Positions 35-355.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid202002. 1 interaction.

Chemistry

BindingDBQ9Z1M0.
ChEMBLCHEMBL5183.

PTM databases

PhosphoSiteQ9Z1M0.

Proteomic databases

PaxDbQ9Z1M0.
PRIDEQ9Z1M0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000100737; ENSMUSP00000098303; ENSMUSG00000029468.
GeneID18439.
KEGGmmu:18439.
UCSCuc008zlq.1. mouse.

Organism-specific databases

CTD5027.
MGIMGI:1339957. P2rx7.

Phylogenomic databases

eggNOGNOG38999.
GeneTreeENSGT00390000016028.
HOVERGENHBG053086.
InParanoidQ9Z1M0.
KOK05220.
OMAFFVMTNF.
OrthoDBEOG78PV92.
TreeFamTF328633.

Gene expression databases

ArrayExpressQ9Z1M0.
BgeeQ9Z1M0.
GenevestigatorQ9Z1M0.

Family and domain databases

Gene3D2.60.490.10. 1 hit.
InterProIPR003050. P2X7_purnocptor.
IPR027309. P2X_extracellular_dom.
IPR001429. P2X_purnocptor.
[Graphical view]
PANTHERPTHR10125. PTHR10125. 1 hit.
PTHR10125:SF13. PTHR10125:SF13. 1 hit.
PfamPF00864. P2X_receptor. 1 hit.
[Graphical view]
PRINTSPR01314. P2X7RECEPTOR.
PR01307. P2XRECEPTOR.
TIGRFAMsTIGR00863. P2X. 1 hit.
PROSITEPS01212. P2X_RECEPTOR. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio294114.
PROQ9Z1M0.
SOURCESearch...

Entry information

Entry nameP2RX7_MOUSE
AccessionPrimary (citable) accession number: Q9Z1M0
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: July 27, 2011
Last modified: April 16, 2014
This is version 111 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot