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Database: UniProt
Entry: A0A3Q1JLT6_ANATE
LinkDB: A0A3Q1JLT6_ANATE
Original site: A0A3Q1JLT6_ANATE 
ID   A0A3Q1JLT6_ANATE        Unreviewed;       419 AA.
AC   A0A3Q1JLT6;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   02-JUN-2021, sequence version 2.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=P2X purinoceptor {ECO:0000256|PIRNR:PIRNR005713, ECO:0000256|RuleBase:RU000681};
OS   Anabas testudineus (Climbing perch) (Anthias testudineus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Anabantaria; Anabantiformes; Anabantoidei; Anabantidae; Anabas.
OX   NCBI_TaxID=64144 {ECO:0000313|Ensembl:ENSATEP00000034100.2, ECO:0000313|Proteomes:UP000265040};
RN   [1] {ECO:0000313|Ensembl:ENSATEP00000034100.2}
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}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|RuleBase:RU000681}.
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DR   AlphaFoldDB; A0A3Q1JLT6; -.
DR   Ensembl; ENSATET00000034597.2; ENSATEP00000034100.2; ENSATEG00000023337.2.
DR   GeneTree; ENSGT01020000230351; -.
DR   InParanoid; A0A3Q1JLT6; -.
DR   Proteomes; UP000265040; 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-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; IPR027309; P2X_extracellular_dom_sf.
DR   InterPro; IPR001429; P2X_purnocptor.
DR   NCBIfam; TIGR00863; P2X; 1.
DR   PANTHER; PTHR10125; P2X PURINOCEPTOR; 1.
DR   PANTHER; PTHR10125:SF12; P2X PURINOCEPTOR 5; 1.
DR   Pfam; PF00864; P2X_receptor; 1.
DR   PIRSF; PIRSF005713; P2X_purinoceptor; 1.
DR   PRINTS; PR01307; P2XRECEPTOR.
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|RuleBase:RU000681};
KW   Reference proteome {ECO:0000313|Proteomes:UP000265040};
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        340..362
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU000681"
FT   BINDING         69..71
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005713-1"
FT   BINDING         188
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005713-1"
FT   BINDING         294..296
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005713-1"
FT   BINDING         314
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005713-1"
FT   CARBOHYD        186
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005713-3"
FT   DISULFID        118..168
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005713-2"
FT   DISULFID        128..151
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005713-2"
FT   DISULFID        134..162
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005713-2"
FT   DISULFID        219..229
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005713-2"
FT   DISULFID        263..271
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005713-2"
SQ   SEQUENCE   419 AA;  47748 MW;  5956780230DEA738 CRC64;
     MAGSFFKGRF LSLFDYKTEK YIVAKNRKVG LLYRLTQLTI LGYIIGWVFL SKKCYQETDE
     AIQSSVMTKL KGVSVTNTSE SGLLLWGPED YVIPPQGEAV LFIVTNFIET PNQTLGYCAE
     VRIFFMLCQK DKDCDEGKMV VAGNGIMTGQ CLKKDENSNG TCEIYAWCPI ERKYKPQEPL
     LTNAENFTIY IKNFIQFHKF GFSKSNVLEK TDNSYLKKCR YDEVLHPYCP IFRLGDITKR
     AGYNFQDMAT FGGSIGIMIR WDCDLDKSSY CHPQYHFTRL DVSDSKKTIA SGFNFRHTRY
     FKNAAGESYR SLIKVYGVRF HIMVHGKAGK FNIIPTAISI GSGLALMGAG AFFCDMVLLY
     LMKNGGSYRE KKFEKAEITQ DNTQEDEDDP KLMSSPFFNL QAVKDQVGQF ILTILCLIF
//
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