ID A0A3B4BEB8_9GOBI Unreviewed; 361 AA.
AC A0A3B4BEB8;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=P2X purinoceptor {ECO:0000256|RuleBase:RU000681};
OS Periophthalmus magnuspinnatus.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Gobiaria; Gobiiformes; Gobioidei; Gobiidae; Oxudercinae; Periophthalmus.
OX NCBI_TaxID=409849 {ECO:0000313|Ensembl:ENSPMGP00000027899.1, ECO:0000313|Proteomes:UP000261520};
RN [1] {ECO:0000313|Ensembl:ENSPMGP00000027899.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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}.
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DR AlphaFoldDB; A0A3B4BEB8; -.
DR STRING; 409849.ENSPMGP00000027899; -.
DR Ensembl; ENSPMGT00000029716.1; ENSPMGP00000027899.1; ENSPMGG00000022502.1.
DR Proteomes; UP000261520; Unplaced.
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; 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; 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|RuleBase:RU000681};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU000681};
KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR005713-1};
KW Receptor {ECO:0000256|RuleBase:RU000681};
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 26..45
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU000681"
FT TRANSMEM 299..324
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU000681"
FT BINDING 64..66
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR005713-1"
FT BINDING 149
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR005713-1"
FT BINDING 256..258
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR005713-1"
FT BINDING 276
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR005713-1"
FT CARBOHYD 147
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000256|PIRSR:PIRSR005713-3"
FT DISULFID 93..114
FT /evidence="ECO:0000256|PIRSR:PIRSR005713-2"
FT DISULFID 99..124
FT /evidence="ECO:0000256|PIRSR:PIRSR005713-2"
FT DISULFID 180..190
FT /evidence="ECO:0000256|PIRSR:PIRSR005713-2"
FT DISULFID 224..233
FT /evidence="ECO:0000256|PIRSR:PIRSR005713-2"
SQ SEQUENCE 361 AA; 40847 MW; 37F1076C9FA2F6F1 CRC64;
MWSCITDFFT YETTKSVVVK SWTIGIINRV VQLLIITYFV GWVFLHEKAY QSRDTAIESS
VMTKVKGFGI YNDRVMDVAD YVTPTQSESK HICKTDSECK AGKPGSNGIL TGKCVQWNSV
NKTCEIQGWC PAEVDTIKTT PMPEVENFTI FIKNSIRFPT FKYTKGNFLP TITEKYIQSC
NYDTENNTYC PIFRVGDVIR YAQQNFTTLA NKGGVIGIKI GWMCDLDKSD DHCNPEYSFT
RLDAMSQKNA VSPGYNFRFA KYYKTENGTD YRTLIKAYAI RFDVLVNGNA GKFDMIPTLI
NMVAAFTSVG VGTVLCDIIL LNFLKGAEQY KAKKFEELSL RTTDILMKSS DSGAFSIEHY
T
//
