ID H2NDG7_PONAB Unreviewed; 397 AA.
AC H2NDG7; A0A2J8WEI1;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 25-MAY-2022, sequence version 2.
DT 27-MAR-2024, entry version 70.
DE RecName: Full=P2X purinoceptor {ECO:0000256|PIRNR:PIRNR005713, ECO:0000256|RuleBase:RU000681};
GN Name=P2RX3 {ECO:0000313|Ensembl:ENSPPYP00000003765.2};
GN ORFNames=CR201_G0010842 {ECO:0000313|EMBL:PNJ68182.1};
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601 {ECO:0000313|Ensembl:ENSPPYP00000003765.2, ECO:0000313|Proteomes:UP000001595};
RN [1] {ECO:0000313|Ensembl:ENSPPYP00000003765.2, ECO:0000313|Proteomes:UP000001595}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Wilson R.K., Mardis E.;
RT "A 6x draft sequence assembly of the Pongo pygmaeus abelii genome.";
RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:PNJ68182.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Susie {ECO:0000313|EMBL:PNJ68182.1};
RA Pollen A., Hastie A., Hormozdiari F., Dougherty M., Liu R., Chaisson M.,
RA Hoppe E., Hill C., Pang A., Hillier L., Baker C., Armstrong J.,
RA Shendure J., Paten B., Wilson R., Chao H., Schneider V., Ventura M.,
RA Kronenberg Z., Murali S., Gordon D., Cantsilieris S., Munson K., Nelson B.,
RA Raja A., Underwood J., Diekhans M., Fiddes I., Haussler D., Eichler E.;
RT "High-resolution comparative analysis of great ape genomes.";
RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Ensembl:ENSPPYP00000003765.2}
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; NDHI03003391; PNJ68182.1; -; Genomic_DNA.
DR STRING; 9601.ENSPPYP00000003765; -.
DR Ensembl; ENSPPYT00000003906.2; ENSPPYP00000003765.2; ENSPPYG00000003277.2.
DR eggNOG; ENOG502QUDE; Eukaryota.
DR GeneTree; ENSGT01020000230351; -.
DR HOGENOM; CLU_034469_8_0_1; -.
DR OrthoDB; 5312692at2759; -.
DR TreeFam; TF328633; -.
DR Proteomes; UP000001595; Chromosome 11.
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; 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; 1.
DR PIRSF; PIRSF005713; P2X_purinoceptor; 1.
DR PRINTS; PR01310; P2X3RECEPTOR.
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:UP000001595};
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|PIRNR:PIRNR005713}.
FT TRANSMEM 21..44
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU000681"
FT TRANSMEM 326..347
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU000681"
FT REGION 378..397
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 63..65
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR005713-1"
FT BINDING 172
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR005713-1"
FT BINDING 279..281
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR005713-1"
FT BINDING 299
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR005713-1"
FT CARBOHYD 170
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000256|PIRSR:PIRSR005713-3"
FT DISULFID 107..153
FT /evidence="ECO:0000256|PIRSR:PIRSR005713-2"
FT DISULFID 116..137
FT /evidence="ECO:0000256|PIRSR:PIRSR005713-2"
FT DISULFID 122..147
FT /evidence="ECO:0000256|PIRSR:PIRSR005713-2"
FT DISULFID 203..213
FT /evidence="ECO:0000256|PIRSR:PIRSR005713-2"
FT DISULFID 247..256
FT /evidence="ECO:0000256|PIRSR:PIRSR005713-2"
SQ SEQUENCE 397 AA; 44304 MW; 4462094EE6A683F1 CRC64;
MNCISDFFTY ETTKSVVVKS WTIGIINRVV QLLIISYFVG WVFLHEKAYQ VRDTAIESSV
VTKVKGSGLY ANRVMDVSDY VTPPQGTSVF VIITKMIVTE NQMQGFCPES EEKYHCVSDS
QCGPERFPGG GILTGRCVNY SSVLRTCEIQ GWCPTEVDTV ETPIMMEAEN FTIFIKNSIR
FPLFNFEKGN LLPNLTARDM KTCRFHPDKD PFCPILRVGD VVKFAGQDFA KLARTGGVLG
IKIGWVCDLD KAWDQCIPKY SFTRLDSVSE KSSVSPGYNF RFAKYYKMEN GSEYRTLLKA
FGIRFDVLVY GNAGKFNIIP TIISSVAAFT SVGVGTVLCD IILLNFLKGA DQYKAKKFEE
VNETTLKIAA LTNPVYPSDQ TTAEKQSTDS GAFSIGH
//
