ID G1R9A7_NOMLE Unreviewed; 441 AA.
AC G1R9A7;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE RecName: Full=P2X purinoceptor {ECO:0000256|PIRNR:PIRNR005713, ECO:0000256|RuleBase:RU000681};
GN Name=P2RX6 {ECO:0000313|Ensembl:ENSNLEP00000009796.1};
OS Nomascus leucogenys (Northern white-cheeked gibbon) (Hylobates leucogenys).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hylobatidae;
OC Nomascus.
OX NCBI_TaxID=61853 {ECO:0000313|Ensembl:ENSNLEP00000009796.1, ECO:0000313|Proteomes:UP000001073};
RN [1] {ECO:0000313|Ensembl:ENSNLEP00000009796.1, ECO:0000313|Proteomes:UP000001073}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Gibbon Genome Sequencing Consortium;
RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSNLEP00000009796.1}
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}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|RuleBase:RU000681}.
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DR EMBL; ADFV01133832; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_003282110.1; XM_003282062.3.
DR AlphaFoldDB; G1R9A7; -.
DR STRING; 61853.ENSNLEP00000009796; -.
DR GlyCosmos; G1R9A7; 1 site, No reported glycans.
DR Ensembl; ENSNLET00000010267.2; ENSNLEP00000009796.1; ENSNLEG00000008025.2.
DR GeneID; 100588488; -.
DR KEGG; nle:100588488; -.
DR CTD; 9127; -.
DR eggNOG; ENOG502R480; Eukaryota.
DR GeneTree; ENSGT01020000230351; -.
DR HOGENOM; CLU_034469_1_0_1; -.
DR InParanoid; G1R9A7; -.
DR OMA; ATMVCDL; -.
DR OrthoDB; 5312692at2759; -.
DR TreeFam; TF328633; -.
DR Proteomes; UP000001073; Chromosome 7b.
DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IEA:InterPro.
DR GO; GO:0098794; C:postsynapse; IEA:GOC.
DR GO; GO:0043235; C:receptor complex; IEA:Ensembl.
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; IPR003049; P2X6_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:SF21; P2X PURINOCEPTOR 6; 1.
DR Pfam; PF00864; P2X_receptor; 1.
DR PIRSF; PIRSF005713; P2X_purinoceptor; 1.
DR PRINTS; PR01313; P2X6RECEPTOR.
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:UP000001073};
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 345..362
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU000681"
FT REGION 410..441
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 78..80
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR005713-1"
FT BINDING 197
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR005713-1"
FT BINDING 295..297
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR005713-1"
FT BINDING 315
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR005713-1"
FT CARBOHYD 195
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000256|PIRSR:PIRSR005713-3"
FT DISULFID 127..177
FT /evidence="ECO:0000256|PIRSR:PIRSR005713-2"
FT DISULFID 138..161
FT /evidence="ECO:0000256|PIRSR:PIRSR005713-2"
FT DISULFID 144..171
FT /evidence="ECO:0000256|PIRSR:PIRSR005713-2"
FT DISULFID 228..238
FT /evidence="ECO:0000256|PIRSR:PIRSR005713-2"
FT DISULFID 272..281
FT /evidence="ECO:0000256|PIRSR:PIRSR005713-2"
SQ SEQUENCE 441 AA; 48648 MW; 381020805BB2E2F6 CRC64;
MCPQLAGAGS MGSPGATTGW GLLDYKTEKY VMTRNWRVGA LQRLLQLGIV VYVVGWALLA
KKGYQERDLE PQISIITKLK GVSVTQIKEL GNRLWDVADF VKPPQGENVF FLVTNFLVTP
AQVQGRCPEH PSVPLANCWA DEDCPEGERG THSHGVKTGQ CVVFNGTHRT CEIWSWCPVE
SGVVPSRPLL AQAQNFTLFI KNMVTFSKFN FSKSNALETW DPTYFKHCRY EPQFSPYCPV
FCIGDLVAKA GGTFEDLALL GGSVGIRVHW DCDLDTGDSG CRPNYSFQLQ EKSYNFRTAT
HWWEQSGVEA RTLLKLYGIR FDILVTGQAG KFGLIPTAVT LGTGAAWLGV VTFFCDLLLL
YVDREAHFYW RTKYEEAKAP KATANSVWSE LALASQARLA ECLRQSSAPA PTATAAGSQT
QTPGWPCPSS DTHLPTHSGS L
//
