Q9Z1M0 (P2RX7_MOUSE) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 101.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: P2X purinoceptor 7 Short name=P2X7 Alternative name(s): ATP receptor P2Z receptor Purinergic receptor | ||||
| Gene names |
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| Organism | Mus musculus (Mouse) [Reference proteome] | ||||
| Taxonomic identifier | 10090 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus![]() |
Protein attributes
| Sequence length | 595 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence 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
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||
Molecule processing | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 595 | 595 | P2X purinoceptor 7 | PRO_0000161561 | |||||||
Regions | |||||||||||
| Topological domain | 1 – 25 | 25 | Cytoplasmic Potential | ||||||||
| Transmembrane | 26 – 46 | 21 | Helical; Name=1; Potential | ||||||||
| Topological domain | 47 – 334 | 288 | Extracellular Potential | ||||||||
| Transmembrane | 335 – 355 | 21 | Helical; Name=2; Potential | ||||||||
| Topological domain | 356 – 595 | 240 | Cytoplasmic Potential | ||||||||
Amino acid modifications | |||||||||||
| Modified residue | 125 | 1 | ADP-ribosylarginine; by ART2B | ||||||||
| Modified residue | 133 | 1 | ADP-ribosylarginine; by ART2B | ||||||||
| Modified residue | 343 | 1 | Phosphotyrosine By similarity | ||||||||
| Glycosylation | 74 | 1 | N-linked (GlcNAc...) Ref.4 | ||||||||
| Glycosylation | 187 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 202 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 213 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 241 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Disulfide bond | 119 ↔ 168 | By similarity | |||||||||
| Disulfide bond | 129 ↔ 152 | By similarity | |||||||||
| Disulfide bond | 135 ↔ 162 | By similarity | |||||||||
| Disulfide bond | 216 ↔ 226 | By similarity | |||||||||
| Disulfide bond | 260 ↔ 269 | By similarity | |||||||||
Experimental info | |||||||||||
| Mutagenesis | 125 | 1 | R → K: Abolishes calcium responses to NAD. Ref.3 | ||||||||
| Mutagenesis | 133 | 1 | R → K: No effect on calcium responses to NAD. Ref.3 | ||||||||
| Sequence conflict | 11 | 1 | L → F in CAA08853. Ref.1 | ||||||||
| Sequence conflict | 221 | 1 | T → A in CAA08853. Ref.1 | ||||||||
| Sequence conflict | 283 | 1 | T → M in CAA08853. Ref.1 | ||||||||
Sequences
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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. 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, MASS SPECTROMETRY. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AJ009823 mRNA. Translation: CAA08853.1. AC114632 Genomic DNA. No translation available. |
| IPI | IPI00130271. |
| RefSeq | NP_035157.2. NM_011027.2. |
| UniGene | Mm.42026. |
3D structure databases | |
| ProteinModelPortal | Q9Z1M0. |
| SMR | Q9Z1M0. Positions 35-355. |
| ModBase | Search... |
PTM databases | |
| PhosphoSite | Q9Z1M0. |
Proteomic databases | |
| PaxDb | Q9Z1M0. |
| PRIDE | Q9Z1M0. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| Ensembl | ENSMUST00000100737; ENSMUSP00000098303; ENSMUSG00000029468. |
| GeneID | 18439. |
| KEGG | mmu:18439. |
Organism-specific databases | |
| CTD | 5027. |
| MGI | MGI:1339957. P2rx7. |
Phylogenomic databases | |
| eggNOG | NOG38999. |
| GeneTree | ENSGT00390000016028. |
| HOVERGEN | HBG053086. |
| InParanoid | Q9Z1M0. |
| KO | K05220. |
| OMA | LCPEYPT. |
| OrthoDB | EOG4DJJWD. |
Gene expression databases | |
| ArrayExpress | Q9Z1M0. |
| Bgee | Q9Z1M0. |
| Genevestigator | Q9Z1M0. |
| GermOnline | ENSMUSG00000029468. Mus musculus. |
Family and domain databases | |
| Gene3D | 2.60.490.10. 1 hit. |
| InterPro | IPR003050. P2X7_purnocptor. IPR027309. P2X_extracellular_dom. IPR001429. P2X_purnocptor. [Graphical view] |
| PANTHER | PTHR10125. PTHR10125. 1 hit. PTHR10125:SF13. PTHR10125:SF13. 1 hit. |
| Pfam | PF00864. P2X_receptor. 1 hit. [Graphical view] |
| PRINTS | PR01314. P2X7RECEPTOR. PR01307. P2XRECEPTOR. |
| TIGRFAMs | TIGR00863. P2X. 1 hit. |
| PROSITE | PS01212. P2X_RECEPTOR. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other | |
| BindingDB | Q9Z1M0. |
| ChEMBL | CHEMBL5183. |
| NextBio | 294114. |
| SOURCE | Search... |
Entry information
| Entry name | P2RX7_MOUSE | ||||||||
| Accession | Primary (citable) accession number: Q9Z1M0 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| MGD cross-references Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot |
| SIMILARITY comments Index of protein domains and families |

Clusters with
