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Q64663 (P2RX7_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 111. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length595 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript 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 By similarity.

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 electronic annotation. Source: Ensembl

T cell homeostasis

Inferred from electronic annotation. Source: Ensembl

T cell proliferation

Inferred from electronic annotation. Source: Ensembl

activation of MAPK activity

Inferred from electronic annotation. Source: Ensembl

apoptotic signaling pathway

Inferred from direct assay PubMed 12857854. Source: BHF-UCL

bleb assembly

Inferred from direct assay PubMed 12857854. Source: BHF-UCL

cell morphogenesis

Inferred from electronic annotation. Source: Ensembl

cell surface receptor signaling pathway

Inferred from direct assay PubMed 12857854. Source: BHF-UCL

cell volume homeostasis

Inferred from electronic annotation. Source: Ensembl

cellular response to extracellular stimulus

Inferred from electronic annotation. Source: Ensembl

ceramide biosynthetic process

Inferred from electronic annotation. Source: Ensembl

collagen metabolic process

Inferred from electronic annotation. Source: Ensembl

cytolysis

Inferred from electronic annotation. Source: Ensembl

defense response to Gram-positive bacterium

Inferred from electronic annotation. Source: Ensembl

homeostasis of number of cells within a tissue

Inferred from electronic annotation. Source: Ensembl

inflammatory response

Inferred from electronic annotation. Source: Ensembl

membrane budding

Inferred from electronic annotation. Source: Ensembl

membrane depolarization

Inferred from direct assay Ref.1. Source: BHF-UCL

membrane protein ectodomain proteolysis

Inferred from electronic annotation. Source: Ensembl

mitochondrion organization

Inferred from electronic annotation. Source: Ensembl

multicellular organismal protein catabolic process

Inferred from electronic annotation. Source: Ensembl

negative regulation of MAPK cascade

Inferred from electronic annotation. Source: Ensembl

negative regulation of bone resorption

Inferred from electronic annotation. Source: Ensembl

neuronal action potential

Inferred from direct assay PubMed 17394459. Source: RGD

organic cation transport

Traceable author statement PubMed 12422208. Source: RGD

phagolysosome assembly

Inferred from electronic annotation. Source: Ensembl

phospholipid transfer to membrane

Inferred from electronic annotation. Source: Ensembl

phospholipid translocation

Inferred from electronic annotation. Source: Ensembl

plasma membrane organization

Inferred from electronic annotation. Source: Ensembl

pore complex assembly

Inferred from direct assay PubMed 15883745. Source: RGD

positive regulation of T cell mediated cytotoxicity

Inferred from electronic annotation. Source: Ensembl

positive regulation of bone mineralization

Inferred from electronic annotation. Source: Ensembl

positive regulation of cytolysis

Inferred from direct assay PubMed 12857854Ref.1. Source: BHF-UCL

positive regulation of cytoskeleton organization

Inferred from direct assay PubMed 12857854. Source: BHF-UCL

positive regulation of gamma-aminobutyric acid secretion

Inferred from electronic annotation. Source: Ensembl

positive regulation of glutamate secretion

Inferred from electronic annotation. Source: Ensembl

positive regulation of interleukin-1 alpha secretion

Inferred from electronic annotation. Source: Ensembl

positive regulation of interleukin-1 beta secretion

Inferred from direct assay PubMed 15883745. Source: RGD

positive regulation of interleukin-6 production

Inferred from electronic annotation. Source: Ensembl

positive regulation of lymphocyte apoptotic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of mitochondrial depolarization

Inferred from electronic annotation. Source: Ensembl

positive regulation of prostaglandin secretion

Inferred from electronic annotation. Source: Ensembl

positive regulation of protein phosphorylation

Inferred from direct assay PubMed 15023862. Source: RGD

protein oligomerization

Inferred from electronic annotation. Source: Ensembl

protein phosphorylation

Inferred from electronic annotation. Source: Ensembl

protein processing

Inferred from electronic annotation. Source: Ensembl

purinergic nucleotide receptor signaling pathway

Inferred from direct assay Ref.1. Source: GOC

reactive oxygen species metabolic process

Inferred from electronic annotation. Source: Ensembl

regulation of sodium ion transport

Inferred from direct assay PubMed 17785580. Source: BHF-UCL

release of sequestered calcium ion into cytosol

Inferred from electronic annotation. Source: Ensembl

response to ATP

Inferred from direct assay Ref.1. Source: BHF-UCL

response to calcium ion

Inferred from electronic annotation. Source: Ensembl

response to drug

Inferred from electronic annotation. Source: Ensembl

response to electrical stimulus

Inferred from electronic annotation. Source: Ensembl

response to fluid shear stress

Inferred from electronic annotation. Source: Ensembl

response to lipopolysaccharide

Inferred from electronic annotation. Source: Ensembl

response to mechanical stimulus

Inferred from electronic annotation. Source: Ensembl

response to zinc ion

Inferred from electronic annotation. Source: Ensembl

sensory perception of pain

Inferred from electronic annotation. Source: Ensembl

skeletal system morphogenesis

Inferred from electronic annotation. Source: Ensembl

synaptic vesicle exocytosis

Inferred from electronic annotation. Source: Ensembl

transmembrane transport

Inferred from direct assay PubMed 18519738. Source: GOC

   Cellular_componentbleb

Inferred from direct assay PubMed 12857854. Source: BHF-UCL

cell-cell junction

Inferred from electronic annotation. Source: Ensembl

cytoplasm

Inferred from direct assay PubMed 12857854. Source: BHF-UCL

external side of plasma membrane

Inferred from electronic annotation. Source: Ensembl

integral component of nuclear inner membrane

Inferred from direct assay PubMed 12422208. Source: RGD

integral component of plasma membrane

Inferred from electronic annotation. Source: Ensembl

membrane raft

Inferred from direct assay PubMed 16415476. Source: RGD

neuromuscular junction

Inferred from electronic annotation. Source: Ensembl

neuron projection

Inferred from direct assay PubMed 16018975. Source: RGD

neuronal cell body

Inferred from electronic annotation. Source: Ensembl

plasma membrane

Inferred from direct assay PubMed 12857854PubMed 17785580. Source: BHF-UCL

protein complex

Inferred from direct assay PubMed 19416975. Source: RGD

terminal bouton

Inferred from direct assay PubMed 16018975. Source: RGD

   Molecular_functionATP binding

Inferred from direct assay PubMed 17394459. Source: RGD

channel activity

Inferred from direct assay PubMed 18519738. Source: MGI

copper ion binding

Inferred from direct assay PubMed 17394459. Source: RGD

extracellular ATP-gated cation channel activity

Inferred from direct assay Ref.1. Source: BHF-UCL

lipopolysaccharide binding

Inferred from electronic annotation. Source: Ensembl

magnesium ion binding

Inferred from direct assay PubMed 17394459. Source: RGD

protein binding

Inferred from physical interaction PubMed 17036048. Source: UniProtKB

protein serine/threonine kinase activator activity

Inferred from mutant phenotype PubMed 15023862. Source: RGD

purinergic nucleotide receptor activity

Inferred from direct assay Ref.1. Source: BHF-UCL

receptor binding

Inferred from physical interaction PubMed 17785580. Source: BHF-UCL

scaffold protein binding

Inferred from physical interaction PubMed 19416975. Source: RGD

zinc ion binding

Inferred from direct assay PubMed 17394459. Source: RGD

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 595595P2X purinoceptor 7
PRO_0000161562

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 similarity
Glycosylation741N-linked (GlcNAc...) Potential
Glycosylation1871N-linked (GlcNAc...) Potential
Glycosylation2021N-linked (GlcNAc...) Potential
Glycosylation2131N-linked (GlcNAc...) Potential
Glycosylation2411N-linked (GlcNAc...) Potential
Glycosylation2841N-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

Sequences

Sequence LengthMass (Da)Tools
Q64663 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 4A6DD6058E5988D3

FASTA59568,392
        10         20         30         40         50         60 
MPACCSWNDV FQYETNKVTR IQSVNYGTIK WILHMTVFSY VSFALMSDKL YQRKEPLISS 

        70         80         90        100        110        120 
VHTKVKGVAE VTENVTEGGV TKLVHGIFDT ADYTLPLQGN SFFVMTNYLK SEGQEQKLCP 

       130        140        150        160        170        180 
EYPSRGKQCH SDQGCIKGWM DPQSKGIQTG RCIPYDQKRK TCEIFAWCPA EEGKEAPRPA 

       190        200        210        220        230        240 
LLRSAENFTV LIKNNIDFPG HNYTTRNILP GMNISCTFHK TWNPQCPIFR LGDIFQEIGE 

       250        260        270        280        290        300 
NFTEVAVQGG IMGIEIYWDC NLDSWSHRCQ PKYSFRRLDD KYTNESLFPG YNFRYAKYYK 

       310        320        330        340        350        360 
ENGMEKRTLI KAFGVRFDIL VFGTGGKFDI IQLVVYIGST LSYFGLATVC IDLIINTYAS 

       370        380        390        400        410        420 
TCCRSRVYPS CKCCEPCAVN EYYYRKKCEP IVEPKPTLKY VSFVDEPHIW MVDQQLLGKS 

       430        440        450        460        470        480 
LQDVKGQEVP RPQTDFLELS RLSLSLHHSP PIPGQPEEMQ LLQIEAVPRS RDSPDWCQCG 

       490        500        510        520        530        540 
NCLPSQLPEN RRALEELCCR RKPGQCITTS ELFSKIVLSR EALQLLLLYQ EPLLALEGEA 

       550        560        570        580        590 
INSKLRHCAY RSYATWRFVS QDMADFAILP SCCRWKIRKE FPKTQGQYSG FKYPY 

« Hide

References

[1]"The cytolytic P2Z receptor for extracellular ATP identified as a P2X receptor (P2X7)."
Surprenant A., Rassendren F., Kawashima E., North R.A., Buell G.N.
Science 272:735-738(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: M33.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X95882 mRNA. Translation: CAA65131.1.
RefSeqNP_062129.1. NM_019256.1.
UniGeneRn.10510.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid248286. 11 interactions.
IntActQ64663. 2 interactions.
MINTMINT-3379474.

Chemistry

BindingDBQ64663.
ChEMBLCHEMBL2496.
GuidetoPHARMACOLOGY484.

PTM databases

PhosphoSiteQ64663.

Proteomic databases

PaxDbQ64663.
PRIDEQ64663.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000001746; ENSRNOP00000001746; ENSRNOG00000001296.
GeneID29665.
KEGGrno:29665.
UCSCRGD:3241. rat.

Organism-specific databases

CTD5027.
RGD3241. P2rx7.

Phylogenomic databases

eggNOGNOG38999.
GeneTreeENSGT00390000016028.
HOGENOMHOG000232042.
HOVERGENHBG053086.
InParanoidQ64663.
KOK05220.
OMALCPEYPT.
OrthoDBEOG78PV92.
PhylomeDBQ64663.
TreeFamTF328633.

Enzyme and pathway databases

ReactomeREACT_227097. Immune System.

Gene expression databases

GenevestigatorQ64663.

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

NextBio609971.
PROQ64663.

Entry information

Entry nameP2RX7_RAT
AccessionPrimary (citable) accession number: Q64663
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: July 9, 2014
This is version 111 of the entry and version 1 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