P2RX7
entrez
5027
canonical
uniprot
Q99572
canonical
ensembl
ENSG00000089041
resolver
ensp
ENSP00000330696
resolver
ensp
ENSP00000573370
resolver
genesymbol
P2RX7
resolver
hgnc
HGNC:8537
resolver
uniprot
A8K2Z0
resolver
uniprot
E7EMK6
resolver
uniprot
F5H6P2
resolver
uniprot
F5H7E8
resolver
uniprot
F8W951
resolver
uniprot
O14991
resolver
uniprot
Q15G98
resolver
uniprot
Q4VKH8
resolver
uniprot
Q4VKH9
resolver
uniprot
Q4VKI0
resolver
uniprot
Q4VKI1
resolver
uniprot
Q4VKI2
resolver
uniprot
Q4VKI3
resolver
uniprot
Q4VKI4
resolver
uniprot
Q7Z771
resolver
uniprot
Q96EV7
resolver
uniprot_entry
P2RX7_HUMAN
resolver
uniprot_sec
A8K2Z0
resolver
uniprot_sec
E7EMK6
resolver
uniprot_sec
F5H6P2
resolver
uniprot_sec
F5H7E8
resolver
uniprot_sec
F8W951
resolver
uniprot_sec
O14991
resolver
uniprot_sec
Q15G98
resolver
uniprot_sec
Q4VKH8
resolver
uniprot_sec
Q4VKH9
resolver
uniprot_sec
Q4VKI0
resolver
uniprot_sec
Q4VKI1
resolver
uniprot_sec
Q4VKI2
resolver
uniprot_sec
Q4VKI3
resolver
uniprot_sec
Q4VKI4
resolver
uniprot_sec
Q7Z771
resolver
uniprot_sec
Q96EV7
resolver
activity_regulation
ACTIVITY REGULATION: Activated by high extracellular ATP levels (0.1-2.5 mM) (PubMed:17483156). The synthetic analog 2'(3')-O-(4-benzoylbenzoyl)ATP (BzATP) acts as a potent agonist (PubMed:20453110, PubMed:25281740). Does not undergo desensitization, instead, undergoes a facilitation process where currents progressively increase with repetitive or prolonged agonist application (PubMed:20453110, PubMed:25281740). Palmitoylation prevents channel desensitization (By similarity). The permeability of the P2RX7 channel is modulated by the amount of cholesterol in the plasma membrane (PubMed:25281740). {ECO:0000250|UniProtKB:Q64663, ECO:0000269|PubMed:17483156, ECO:0000269|PubMed:20453110, ECO:0000269|PubMed:25281740}.
uniprot
proteins
amino_acid_sequence
MPACCSCSDVFQYETNKVTRIQSMNYGTIKWFFHVIIFSYVCFALVSDKLYQRKEPVISSVHTKVKGIAEVKEEIVENGVKKLVHSVFDTADYTFPLQGNSFFVMTNFLKTEGQEQRLCPEYPTRRTLCSSDRGCKKGWMDPQSKGIQTGRCVVYEGNQKTCEVSAWCPIEAVEEAPRPALLNSAENFTVLIKNNIDFPGHNYTTRNILPGLNITCTFHKTQNPQCPIFRLGDIFRETGDNFSDVAIQGGIMGIEIYWDCNLDRWFHHCRPKYSFRRLDDKTTNVSLYPGYNFRYAKYYKENNVEKRTLIKVFGIRFDILVFGTGGKFDIIQLVVYIGSTLSYFGLAAVFIDFLIDTYSSNCCRSHIYPWCKCCQPCVVNEYYYRKKCESIVEPKPTLKYVSFVDESHIRMVNQQLLGRSLQDVKGQEVPRPAMDFTDLSRLPLALHDTPPIPGQPEEIQLLRKEATPRSRDSPVWCQCGSCLPSQLPESHRCLEELCCRKKPGACITTSELFRKLVLSRHVLQFLLLYQEPLLALDVDSTNSRLRHCAYRCYATWRFGSQDMADFAILPSCCRWRIRKEFPKSEGQYSGFKSPY
uniprot
proteins
function
FUNCTION: ATP-gated nonselective transmembrane cation channel that requires high millimolar concentrations of ATP for activation (PubMed:17483156, PubMed:25281740, PubMed:9038151). Upon ATP binding, it rapidly opens to allow the influx of small cations Na(+) and Ca(2+), and the K(+) efflux (PubMed:17483156, PubMed:20453110, PubMed:28235784, PubMed:39262850). Also has the ability to form a large pore in the cell membrane, allowing the passage of large cationic molecules (PubMed:17483156). In microglia, may mediate NADPH transport across the plasma membrane (PubMed:39142135). In immune cells, P2RX7 acts as a molecular sensor in pathological inflammatory states by detecting and responding to high local concentrations of extracellar ATP. In microglial cells, P2RX7 activation leads to the release of pro-inflammatory cytokines, such as IL-1beta and IL-18, through the activation of the NLRP3 inflammasome and caspase-1 (PubMed:26877061). Cooperates with KCNK6 to activate NLRP3 inflammasome (By similarity). Activates death pathways leading to apoptosis and autophagy (PubMed:21821797, PubMed:23303206, PubMed:28326637). Activates death pathways leading to pyroptosis (By similarity). {ECO:0000250|UniProtKB:Q9Z1M0, ECO:0000269|PubMed:17483156, ECO:0000269|PubMed:20453110, ECO:0000269|PubMed:21821797, ECO:0000269|PubMed:23303206, ECO:0000269|PubMed:25281740, ECO:0000269|PubMed:26877061, ECO:0000269|PubMed:28235784, ECO:0000269|PubMed:28326637, ECO:0000269|PubMed:39142135, ECO:0000269|PubMed:39262850, ECO:0000269|PubMed:9038151}.; FUNCTION: [Isoform B]: Shows ion channel activity but no macropore function. {ECO:0000269|PubMed:20453110}.; FUNCTION: [Isoform H]: Non-functional channel. {ECO:0000269|PubMed:15896293}.; FUNCTION: [Isoform J]: Non-functional channel. {ECO:0000269|PubMed:16624800}.
uniprot
proteins
mass_dalton
68585
uniprot
proteins
mutagenesis
MUTAGEN 14; /note="E->K: Loss of cation selectivity in favor of anion (Cl(-)) selectivity; when associated with K-342 and K-352."; /evidence="ECO:0000269|PubMed:39262850"; MUTAGEN 187; /note="N->A: Alters cell surface expression."; /evidence="ECO:0000269|PubMed:20450227"; MUTAGEN 342; /note="S->K: Decreases the selectivity for Na(+) over the larger organic cation Tris(+). Loss of cation selectivity in favor of anion (Cl(-)) selectivity; when associated with K-14 and K-352."; /evidence="ECO:0000269|PubMed:39142135, ECO:0000269|PubMed:39262850"; MUTAGEN 352; /note="D->K: Loss of cation selectivity in favor of anion (Cl(-)) selectivity; when associated with K-14 and K-352."; /evidence="ECO:0000269|PubMed:39262850
uniprot
proteins
post_translational_modification
PTM: Phosphorylation results in its inactivation. {ECO:0000269|PubMed:11707406}.; PTM: ADP-ribosylation at Arg-125 is necessary and sufficient to activate P2RX7 and gate the channel. {ECO:0000250|UniProtKB:Q9Z1M0}.; PTM: Palmitoylation of several cysteines in the C-terminal cytoplasmic tail is required for efficient localization to cell surface (PubMed:18971257). Palmitoylation prevents channel desensitization by physically anchoring the palmitoylated groups to the membrane (By similarity). {ECO:0000250|UniProtKB:Q64663, ECO:0000269|PubMed:18971257}.
uniprot
proteins
protein_family
P2X receptor family
uniprot
proteins
pubmed
11150303
uniprot
proteins
pubmed
11707406
uniprot
proteins
pubmed
12107182
uniprot
proteins
pubmed
12586825
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15123679
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15896293
uniprot
proteins
pubmed
16541075
uniprot
proteins
pubmed
16624800
uniprot
proteins
pubmed
16959974
uniprot
proteins
pubmed
17483156
uniprot
proteins
pubmed
18971257
uniprot
proteins
pubmed
20450227
uniprot
proteins
pubmed
20453110
uniprot
proteins
pubmed
21821797
uniprot
proteins
pubmed
23303206
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
25281740
uniprot
proteins
pubmed
26877061
uniprot
proteins
pubmed
28235784
uniprot
proteins
pubmed
28326637
uniprot
proteins
pubmed
39142135
uniprot
proteins
pubmed
39262850
uniprot
proteins
pubmed
9038151
uniprot
proteins
pubmed
9826911
uniprot
proteins
sequence_length
595
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12107182, ECO:0000269|PubMed:23303206, ECO:0000269|PubMed:28326637}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q64663}.
uniprot
proteins
transmembrane_region
TRANSMEM 23..46; /note="Helical; Name=1"; /evidence="ECO:0000250|UniProtKB:Q64663"; TRANSMEM 329..353; /note="Helical; Name=2"; /evidence="ECO:0000250|UniProtKB:Q64663
uniprot
proteins