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P2X purinoceptor 7 (P2X7) (ATP receptor) (P2Z receptor) (Purinergic receptor)

 P2RX7_MOUSE             Reviewed;         595 AA.
Q9Z1M0;
30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
27-JUL-2011, sequence version 2.
31-JAN-2018, entry version 146.
RecName: Full=P2X purinoceptor 7;
Short=P2X7;
AltName: Full=ATP receptor;
AltName: Full=P2Z receptor;
AltName: Full=Purinergic receptor;
Name=P2rx7; Synonyms=P2x7;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=9849870; DOI=10.1016/S0014-5793(98)01332-5;
Chessell I.P., Simon J., Hibell A.D., Michel A.D., Barnard E.A.,
Humphrey P.P.;
"Cloning and functional characterisation of the mouse P2X7 receptor.";
FEBS Lett. 439:26-30(1998).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
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., 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.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[3]
ADP-RIBOSYLATION AT ARG-125 AND ARG-133 BY ART2B, AND MUTAGENESIS OF
ARG-125 AND ARG-133.
PubMed=17928361; DOI=10.1096/fj.07-9294com;
Adriouch S., Bannas P., Schwarz N., Fliegert R., Guse A.H., Seman M.,
Haag F., Koch-Nolte F.;
"ADP-ribosylation at R125 gates the P2X7 ion channel by presenting a
covalent ligand to its nucleotide binding site.";
FASEB J. 22:861-869(2008).
[4]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-74.
PubMed=19349973; DOI=10.1038/nbt.1532;
Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
Schiess R., Aebersold R., Watts J.D.;
"Mass-spectrometric identification and relative quantification of N-
linked cell surface glycoproteins.";
Nat. Biotechnol. 27:378-386(2009).
[5]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Lung;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- 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. In the absence
of its natural ligand, ATP, functions as a scavenger receptor in
the recognition and engulfment of apoptotic cells.
{ECO:0000250|UniProtKB:Q99572}.
-!- SUBUNIT: 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).
{ECO:0000250|UniProtKB:Q99572}.
-!- SUBCELLULAR LOCATION: Cell membrane
{ECO:0000250|UniProtKB:Q99572}; Multi-pass membrane protein
{ECO:0000255}.
-!- PTM: Phosphorylation results in its inactivation.
{ECO:0000250|UniProtKB:Q99572}.
-!- PTM: ADP-ribosylation at Arg-125 is necessary and sufficient to
activate P2RX7 and gate the channel.
-!- PTM: Palmitoylation of several cysteines in the C-terminal
cytoplasmic tail is required for efficient localization to cell
surface. {ECO:0000250|UniProtKB:Q99572}.
-!- SIMILARITY: Belongs to the P2X receptor family. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AJ009823; CAA08853.1; -; mRNA.
EMBL; AC114632; -; NOT_ANNOTATED_CDS; Genomic_DNA.
CCDS; CCDS19652.1; -.
RefSeq; NP_035157.2; NM_011027.3.
UniGene; Mm.42026; -.
ProteinModelPortal; Q9Z1M0; -.
SMR; Q9Z1M0; -.
BioGrid; 202002; 2.
STRING; 10090.ENSMUSP00000098303; -.
BindingDB; Q9Z1M0; -.
ChEMBL; CHEMBL5183; -.
GuidetoPHARMACOLOGY; 484; -.
iPTMnet; Q9Z1M0; -.
PhosphoSitePlus; Q9Z1M0; -.
SwissPalm; Q9Z1M0; -.
MaxQB; Q9Z1M0; -.
PaxDb; Q9Z1M0; -.
PRIDE; Q9Z1M0; -.
Ensembl; ENSMUST00000100737; ENSMUSP00000098303; ENSMUSG00000029468.
GeneID; 18439; -.
KEGG; mmu:18439; -.
UCSC; uc008zlq.2; mouse.
CTD; 5027; -.
MGI; MGI:1339957; P2rx7.
eggNOG; ENOG410IK4U; Eukaryota.
eggNOG; ENOG4110DDY; LUCA.
GeneTree; ENSGT00390000016028; -.
HOVERGEN; HBG053086; -.
InParanoid; Q9Z1M0; -.
KO; K05220; -.
OMA; YPGYNFR; -.
OrthoDB; EOG091G0A2U; -.
TreeFam; TF328633; -.
Reactome; R-MMU-139853; Elevation of cytosolic Ca2+ levels.
Reactome; R-MMU-418346; Platelet homeostasis.
Reactome; R-MMU-844456; The NLRP3 inflammasome.
PRO; PR:Q9Z1M0; -.
Proteomes; UP000000589; Chromosome 5.
Bgee; ENSMUSG00000029468; -.
ExpressionAtlas; Q9Z1M0; baseline and differential.
Genevisible; Q9Z1M0; MM.
GO; GO:0005911; C:cell-cell junction; IDA:MGI.
GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
GO; GO:0005639; C:integral component of nuclear inner membrane; IBA:GO_Central.
GO; GO:0005887; C:integral component of plasma membrane; IMP:MGI.
GO; GO:0016020; C:membrane; IDA:MGI.
GO; GO:0031594; C:neuromuscular junction; IDA:MGI.
GO; GO:0043025; C:neuronal cell body; IDA:MGI.
GO; GO:0005886; C:plasma membrane; IDA:MGI.
GO; GO:0098794; C:postsynapse; IEA:GOC.
GO; GO:0098793; C:presynapse; IEA:GOC.
GO; GO:0045202; C:synapse; IDA:MGI.
GO; GO:0005524; F:ATP binding; IMP:MGI.
GO; GO:0015267; F:channel activity; IMP:MGI.
GO; GO:0004931; F:extracellularly ATP-gated cation channel activity; IMP:MGI.
GO; GO:0001530; F:lipopolysaccharide binding; IDA:MGI.
GO; GO:0001614; F:purinergic nucleotide receptor activity; ISO:MGI.
GO; GO:0004872; F:receptor activity; IMP:MGI.
GO; GO:0000187; P:activation of MAPK activity; IMP:MGI.
GO; GO:0032060; P:bleb assembly; IMP:UniProtKB.
GO; GO:0006816; P:calcium ion transport; IMP:MGI.
GO; GO:0006812; P:cation transport; IMP:MGI.
GO; GO:0000902; P:cell morphogenesis; IMP:MGI.
GO; GO:0006884; P:cell volume homeostasis; IDA:MGI.
GO; GO:0071359; P:cellular response to dsRNA; IMP:MGI.
GO; GO:0031668; P:cellular response to extracellular stimulus; IMP:MGI.
GO; GO:0071407; P:cellular response to organic cyclic compound; IDA:MGI.
GO; GO:0046513; P:ceramide biosynthetic process; IDA:MGI.
GO; GO:0032963; P:collagen metabolic process; IMP:MGI.
GO; GO:0019835; P:cytolysis; IDA:MGI.
GO; GO:0050830; P:defense response to Gram-positive bacterium; IMP:MGI.
GO; GO:0097191; P:extrinsic apoptotic signaling pathway; IMP:MGI.
GO; GO:0010467; P:gene expression; IMP:MGI.
GO; GO:0048873; P:homeostasis of number of cells within a tissue; IMP:MGI.
GO; GO:0006954; P:inflammatory response; IMP:MGI.
GO; GO:0051899; P:membrane depolarization; ISO:MGI.
GO; GO:0006509; P:membrane protein ectodomain proteolysis; IMP:MGI.
GO; GO:0007005; P:mitochondrion organization; IDA:MGI.
GO; GO:0044254; P:multicellular organismal protein catabolic process; IDA:MGI.
GO; GO:0043132; P:NAD transport; IMP:MGI.
GO; GO:0045779; P:negative regulation of bone resorption; IMP:MGI.
GO; GO:0045794; P:negative regulation of cell volume; IMP:UniProtKB.
GO; GO:0043409; P:negative regulation of MAPK cascade; IDA:MGI.
GO; GO:0001845; P:phagolysosome assembly; IMP:MGI.
GO; GO:0017121; P:phospholipid scrambling; ISO:MGI.
GO; GO:0006649; P:phospholipid transfer to membrane; IMP:MGI.
GO; GO:0045332; P:phospholipid translocation; IDA:MGI.
GO; GO:0007009; P:plasma membrane organization; IDA:MGI.
GO; GO:0046931; P:pore complex assembly; IMP:MGI.
GO; GO:0043065; P:positive regulation of apoptotic process; IMP:MGI.
GO; GO:1904172; P:positive regulation of bleb assembly; ISO:MGI.
GO; GO:0030501; P:positive regulation of bone mineralization; IMP:MGI.
GO; GO:0010524; P:positive regulation of calcium ion transport into cytosol; ISO:MGI.
GO; GO:0043085; P:positive regulation of catalytic activity; IMP:MGI.
GO; GO:0050715; P:positive regulation of cytokine secretion; IMP:MGI.
GO; GO:0014054; P:positive regulation of gamma-aminobutyric acid secretion; IMP:MGI.
GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI.
GO; GO:0014049; P:positive regulation of glutamate secretion; IMP:MGI.
GO; GO:0045821; P:positive regulation of glycolytic process; ISO:MGI.
GO; GO:0050717; P:positive regulation of interleukin-1 alpha secretion; IMP:MGI.
GO; GO:0032731; P:positive regulation of interleukin-1 beta production; IMP:MGI.
GO; GO:0050718; P:positive regulation of interleukin-1 beta secretion; IMP:MGI.
GO; GO:0032755; P:positive regulation of interleukin-6 production; IMP:MGI.
GO; GO:0034767; P:positive regulation of ion transmembrane transport; ISO:MGI.
GO; GO:0070230; P:positive regulation of lymphocyte apoptotic process; IMP:MGI.
GO; GO:0043410; P:positive regulation of MAPK cascade; IMP:MGI.
GO; GO:0051901; P:positive regulation of mitochondrial depolarization; IMP:MGI.
GO; GO:0045778; P:positive regulation of ossification; IMP:MGI.
GO; GO:0032308; P:positive regulation of prostaglandin secretion; IMP:MGI.
GO; GO:0001934; P:positive regulation of protein phosphorylation; IMP:MGI.
GO; GO:0050714; P:positive regulation of protein secretion; IDA:MGI.
GO; GO:0001916; P:positive regulation of T cell mediated cytotoxicity; IMP:MGI.
GO; GO:0012501; P:programmed cell death; IDA:MGI.
GO; GO:0051259; P:protein oligomerization; IDA:MGI.
GO; GO:0006468; P:protein phosphorylation; IMP:MGI.
GO; GO:0016485; P:protein processing; IMP:MGI.
GO; GO:0035590; P:purinergic nucleotide receptor signaling pathway; ISO:MGI.
GO; GO:0072593; P:reactive oxygen species metabolic process; IMP:MGI.
GO; GO:0051209; P:release of sequestered calcium ion into cytosol; IMP:MGI.
GO; GO:0033198; P:response to ATP; IDA:MGI.
GO; GO:0009617; P:response to bacterium; IMP:MGI.
GO; GO:0051592; P:response to calcium ion; IDA:MGI.
GO; GO:0042493; P:response to drug; IMP:MGI.
GO; GO:0051602; P:response to electrical stimulus; IMP:MGI.
GO; GO:0034405; P:response to fluid shear stress; IMP:MGI.
GO; GO:0032496; P:response to lipopolysaccharide; IDA:MGI.
GO; GO:0009612; P:response to mechanical stimulus; IMP:MGI.
GO; GO:0014070; P:response to organic cyclic compound; IDA:MGI.
GO; GO:0010033; P:response to organic substance; IMP:MGI.
GO; GO:0010043; P:response to zinc ion; IMP:MGI.
GO; GO:0019233; P:sensory perception of pain; IMP:BHF-UCL.
GO; GO:0048705; P:skeletal system morphogenesis; IMP:MGI.
GO; GO:0016079; P:synaptic vesicle exocytosis; IMP:MGI.
GO; GO:0043029; P:T cell homeostasis; IMP:MGI.
GO; GO:0042098; P:T cell proliferation; IMP:MGI.
GO; GO:0006900; P:vesicle budding from membrane; IMP:MGI.
Gene3D; 2.60.490.10; -; 1.
InterPro; IPR003050; P2X7_purinoceptor.
InterPro; IPR027309; P2X_extracellular_dom_sf.
InterPro; IPR001429; P2X_purnocptor.
PANTHER; PTHR10125; PTHR10125; 1.
PANTHER; PTHR10125:SF13; PTHR10125:SF13; 1.
Pfam; PF00864; P2X_receptor; 1.
PRINTS; PR01314; P2X7RECEPTOR.
PRINTS; PR01307; P2XRECEPTOR.
TIGRFAMs; TIGR00863; P2X; 1.
PROSITE; PS01212; P2X_RECEPTOR; 1.
1: Evidence at protein level;
ADP-ribosylation; Cell membrane; Complete proteome; Disulfide bond;
Glycoprotein; Ion channel; Ion transport; Ligand-gated ion channel;
Lipoprotein; Membrane; Palmitate; Phosphoprotein; Receptor;
Reference proteome; Transmembrane; Transmembrane helix; Transport.
CHAIN 1 595 P2X purinoceptor 7.
/FTId=PRO_0000161561.
TOPO_DOM 1 25 Cytoplasmic. {ECO:0000255}.
TRANSMEM 26 46 Helical; Name=1. {ECO:0000255}.
TOPO_DOM 47 334 Extracellular. {ECO:0000255}.
TRANSMEM 335 355 Helical; Name=2. {ECO:0000255}.
TOPO_DOM 356 595 Cytoplasmic. {ECO:0000255}.
MOD_RES 125 125 ADP-ribosylarginine; by ART2B.
{ECO:0000269|PubMed:17928361}.
MOD_RES 133 133 ADP-ribosylarginine; by ART2B.
{ECO:0000269|PubMed:17928361}.
MOD_RES 390 390 Phosphoserine.
{ECO:0000250|UniProtKB:Q99572}.
CARBOHYD 74 74 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19349973}.
CARBOHYD 187 187 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 202 202 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 213 213 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 241 241 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 119 168 {ECO:0000250}.
DISULFID 129 152 {ECO:0000250}.
DISULFID 135 162 {ECO:0000250}.
DISULFID 216 226 {ECO:0000250}.
DISULFID 260 269 {ECO:0000250}.
MUTAGEN 125 125 R->K: Abolishes calcium responses to NAD.
{ECO:0000269|PubMed:17928361}.
MUTAGEN 133 133 R->K: No effect on calcium responses to
NAD. {ECO:0000269|PubMed:17928361}.
CONFLICT 11 11 L -> F (in Ref. 1; CAA08853).
{ECO:0000305}.
CONFLICT 221 221 T -> A (in Ref. 1; CAA08853).
{ECO:0000305}.
CONFLICT 283 283 T -> M (in Ref. 1; CAA08853).
{ECO:0000305}.
SEQUENCE 595 AA; 68388 MW; BE007FE195AF50A4 CRC64;
MPACCSWNDV LQYETNKVTR IQSTNYGTVK WVLHMIVFSY ISFALVSDKL YQRKEPVISS
VHTKVKGIAE VTENVTEGGV TKLGHSIFDT ADYTFPLQGN SFFVMTNYVK SEGQVQTLCP
EYPRRGAQCS SDRRCKKGWM DPQSKGIQTG RCVPYDKTRK TCEVSAWCPT EEEKEAPRPA
LLRSAENFTV LIKNNIHFPG HNYTTRNILP TMNGSCTFHK TWDPQCSIFR LGDIFQEAGE
NFTEVAVQGG IMGIEIYWDC NLDSWSHHCR PRYSFRRLDD KNTDESFVPG YNFRYAKYYK
ENNVEKRTLI KAFGIRFDIL VFGTGGKFDI IQLVVYIGST LSYFGLATVC IDLLINTYSS
AFCRSGVYPY CKCCEPCTVN EYYYRKKCES IMEPKPTLKY VSFVDEPHIR MVDQQLLGKS
LQVVKGQEVP RPQMDFSDLS RLSLSLHDSP LTPGQSEEIQ LLHEEVAPKS GDSPSWCQCG
NCLPSRLPEQ RRALEELCCR RKPGRCITTS KLFHKLVLSR DTLQLLLLYQ DPLLVLGEEA
TNSRLRHRAY RCYATWRFGS QDMADFAILP SCCRWRIRKE FPKTEGQYSG FKYPY


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