ID A0A2I3TEQ1_PANTR Unreviewed; 379 AA.
AC A0A2I3TEQ1; A0A2J8IR48;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=P2X purinoceptor {ECO:0000256|PIRNR:PIRNR005713, ECO:0000256|RuleBase:RU000681};
GN Name=P2RX2 {ECO:0000313|Ensembl:ENSPTRP00000087718.1,
GN ECO:0000313|VGNC:VGNC:13334};
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598 {ECO:0000313|Ensembl:ENSPTRP00000087718.1, ECO:0000313|Proteomes:UP000002277};
RN [1] {ECO:0000313|Ensembl:ENSPTRP00000087718.1, ECO:0000313|Proteomes:UP000002277}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16136131; DOI=10.1038/nature04072;
RG Chimpanzee sequencing and analysis consortium;
RT "Initial sequence of the chimpanzee genome and comparison with the human
RT genome.";
RL Nature 437:69-87(2005).
RN [2] {ECO:0000313|Ensembl:ENSPTRP00000087718.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Receptor for ATP that acts as a ligand-gated ion channel.
CC {ECO:0000256|PIRNR:PIRNR005713, ECO:0000256|RuleBase:RU000681}.
CC -!- SUBUNIT: Functional P2XRs are organized as homomeric and heteromeric
CC trimers. {ECO:0000256|PIRNR:PIRNR005713}.
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|PIRNR:PIRNR005713,
CC ECO:0000256|RuleBase:RU000681}.
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DR EMBL; AACZ04060451; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A2I3TEQ1; -.
DR GlyCosmos; A0A2I3TEQ1; 1 site, No reported glycans.
DR Ensembl; ENSPTRT00000107655.1; ENSPTRP00000087718.1; ENSPTRG00000005653.6.
DR VGNC; VGNC:13334; P2RX2.
DR GeneTree; ENSGT01020000230351; -.
DR Proteomes; UP000002277; Chromosome 12.
DR Bgee; ENSPTRG00000005653; Expressed in thymus and 6 other cell types or tissues.
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-UniRule.
DR GO; GO:0004931; F:extracellularly ATP-gated monoatomic cation channel activity; IEA:UniProtKB-UniRule.
DR GO; GO:0001614; F:purinergic nucleotide receptor activity; IEA:UniProtKB-UniRule.
DR GO; GO:0033198; P:response to ATP; IEA:InterPro.
DR Gene3D; 2.60.490.10; atp-gated p2x4 ion channel domain; 1.
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:SF4; P2X PURINOCEPTOR 2; 1.
DR Pfam; PF00864; P2X_receptor; 1.
DR PIRSF; PIRSF005713; P2X_purinoceptor; 2.
DR PRINTS; PR01307; P2XRECEPTOR.
DR PROSITE; PS01212; P2X_RECEPTOR; 1.
PE 3: Inferred from homology;
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|PIRNR:PIRNR005713};
KW Ligand-gated ion channel {ECO:0000256|PIRNR:PIRNR005713};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR005713};
KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR005713-1};
KW Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|RuleBase:RU000681};
KW Reference proteome {ECO:0000313|Proteomes:UP000002277};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PIRNR:PIRNR005713}.
FT REGION 310..379
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 355..379
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 104
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR005713-1"
FT BINDING 208..210
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR005713-1"
FT BINDING 227
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR005713-1"
FT CARBOHYD 102
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000256|PIRSR:PIRSR005713-3"
FT DISULFID 44..67
FT /evidence="ECO:0000256|PIRSR:PIRSR005713-2"
FT DISULFID 50..78
FT /evidence="ECO:0000256|PIRSR:PIRSR005713-2"
FT DISULFID 134..144
FT /evidence="ECO:0000256|PIRSR:PIRSR005713-2"
FT DISULFID 178..187
FT /evidence="ECO:0000256|PIRSR:PIRSR005713-2"
SQ SEQUENCE 379 AA; 41191 MW; EE8C7E50484827D6 CRC64;
MAAAQPKYPA GATARRLARG CWSALWDYET PKVIVSIRVH NATCLSDADC VAGELNMLGN
GLRTGRCVPY YQGPSKTCEV FGWCPVEDGA SVSQFLGTMA PNFTILIKNS IHYPKFHFSK
GNIADRTDGY LKRCTFHEAS DLYCPIFKLG FIVEKAGESF TELAHKGGVI GVIINWDCDL
DLPASECNPK YSFRRLDPKH VPASSGYNFR FAKYYKINGT TTRTLIKAYG IRIDVIVHGQ
AGKFSLIPTI INLATALTSV GVGSFLCDWI LLTFMNKNKV YSHKKFDKVC TPSQPSGSWP
VTLARVLGQA PPEPGHCSED QHPSPPSGQE GQQGAECGPA FPPLRPCPIS APSEQMVDTP
ASEPAQASTP TDPKGLAQL
//
