ID A2AW03_MOUSE Unreviewed; 373 AA.
AC A2AW03;
DT 20-FEB-2007, integrated into UniProtKB/TrEMBL.
DT 20-FEB-2007, sequence version 1.
DT 27-MAR-2024, entry version 116.
DE RecName: Full=P2X purinoceptor {ECO:0000256|RuleBase:RU000681};
GN Name=P2rx3 {ECO:0000313|Ensembl:ENSMUSP00000107243.3,
GN ECO:0000313|MGI:MGI:1097160};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090 {ECO:0000313|Ensembl:ENSMUSP00000107243.3, ECO:0000313|Proteomes:UP000000589};
RN [1] {ECO:0000313|Ensembl:ENSMUSP00000107243.3, ECO:0000313|Proteomes:UP000000589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000107243.3,
RC ECO:0000313|Proteomes:UP000000589};
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2] {ECO:0000313|Ensembl:ENSMUSP00000107243.3}
RP IDENTIFICATION.
RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000107243.3};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Receptor for ATP that acts as a ligand-gated ion channel.
CC {ECO:0000256|RuleBase:RU000681}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141,
CC ECO:0000256|RuleBase:RU000681}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU000681}.
CC -!- SIMILARITY: Belongs to the P2X receptor family.
CC {ECO:0000256|ARBA:ARBA00009848, ECO:0000256|RuleBase:RU000681}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|RuleBase:RU000681}.
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DR AlphaFoldDB; A2AW03; -.
DR SMR; A2AW03; -.
DR GlyCosmos; A2AW03; 1 site, No reported glycans.
DR MaxQB; A2AW03; -.
DR Antibodypedia; 14096; 306 antibodies from 31 providers.
DR Ensembl; ENSMUST00000111616.3; ENSMUSP00000107243.3; ENSMUSG00000027071.15.
DR AGR; MGI:1097160; -.
DR MGI; MGI:1097160; P2rx3.
DR VEuPathDB; HostDB:ENSMUSG00000027071; -.
DR GeneTree; ENSGT01020000230351; -.
DR HOGENOM; CLU_034469_2_0_1; -.
DR ChiTaRS; P2rx3; mouse.
DR Proteomes; UP000000589; Chromosome 2.
DR Bgee; ENSMUSG00000027071; Expressed in lumbar dorsal root ganglion and 61 other cell types or tissues.
DR ExpressionAtlas; A2AW03; baseline and differential.
DR GO; GO:0005886; C:plasma membrane; IEA:InterPro.
DR GO; GO:0098794; C:postsynapse; IEA:GOC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004931; F:extracellularly ATP-gated monoatomic cation channel activity; IEA:InterPro.
DR GO; GO:0001614; F:purinergic nucleotide receptor activity; IEA:InterPro.
DR GO; GO:0033198; P:response to ATP; IEA:InterPro.
DR Gene3D; 1.10.287.940; atp-gated p2x4 ion channel; 1.
DR Gene3D; 2.60.490.10; atp-gated p2x4 ion channel domain; 1.
DR InterPro; IPR003046; P2X3_purnocptor.
DR InterPro; IPR027309; P2X_extracellular_dom_sf.
DR InterPro; IPR001429; P2X_purnocptor.
DR NCBIfam; TIGR00863; P2X; 1.
DR PANTHER; PTHR10125; P2X PURINOCEPTOR; 1.
DR PANTHER; PTHR10125:SF8; P2X PURINOCEPTOR 3; 1.
DR Pfam; PF00864; P2X_receptor; 2.
DR PIRSF; PIRSF005713; P2X_purinoceptor; 2.
DR PRINTS; PR01310; P2X3RECEPTOR.
DR PRINTS; PR01307; P2XRECEPTOR.
DR PROSITE; PS01212; P2X_RECEPTOR; 1.
PE 1: Evidence at protein level;
KW ATP-binding {ECO:0000256|PIRSR:PIRSR005713-1};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW ECO:0000256|PIRSR:PIRSR005713-2};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Ion channel {ECO:0000256|RuleBase:RU000681};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065,
KW ECO:0000256|RuleBase:RU000681};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU000681};
KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR005713-1};
KW Proteomics identification {ECO:0007829|EPD:A2AW03};
KW Receptor {ECO:0000256|RuleBase:RU000681};
KW Reference proteome {ECO:0000313|Proteomes:UP000000589};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU000681};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU000681};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU000681}.
FT TRANSMEM 302..323
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU000681"
FT BINDING 63..65
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR005713-1"
FT BINDING 148
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR005713-1"
FT BINDING 255..257
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR005713-1"
FT BINDING 275
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR005713-1"
FT CARBOHYD 146
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000256|PIRSR:PIRSR005713-3"
FT DISULFID 92..113
FT /evidence="ECO:0000256|PIRSR:PIRSR005713-2"
FT DISULFID 98..123
FT /evidence="ECO:0000256|PIRSR:PIRSR005713-2"
FT DISULFID 179..189
FT /evidence="ECO:0000256|PIRSR:PIRSR005713-2"
FT DISULFID 223..232
FT /evidence="ECO:0000256|PIRSR:PIRSR005713-2"
SQ SEQUENCE 373 AA; 41782 MW; EEC091057C2825BC CRC64;
MNCISDFFTY ETTKSVVVKS WTIGIINRAV QLLIISYFVG WVFLHEKAYQ VRDTAIESSV
VTKVKGFGRY ANRVMDVSDY VTPPQNEEKY RCVSDSQCGP ERFPGGGILT GRCVNYSSVR
RTCEIQGWCP TEVDTVEMPI MMEAENFTIF IKNSIRFPLF NFEKGNLLPN LTDKDIKKCR
FHPEKAPFCP ILRVGDVVKF AGQDFAKLAR TGGVLGIKIG WVCDLDKAWD QCIPKYSFTR
LDGVSEKSSV SPGYNFRFAK YYKMENGSEY RTLLKAFGIR FDVLVYGNAG KFNIIPTIIS
SVAAFTSVGV GTVLCDIILL NFLKGADHYK ARKFEEVTET TLKGTASTNP VFTSDQATVE
KQSTDSGAYS IGH
//
