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Database: UniProt
Entry: R0KZE2_ANAPL
LinkDB: R0KZE2_ANAPL
Original site: R0KZE2_ANAPL 
ID   R0KZE2_ANAPL            Unreviewed;       399 AA.
AC   R0KZE2;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   24-JAN-2024, entry version 39.
DE   RecName: Full=P2X purinoceptor {ECO:0000256|RuleBase:RU000681};
DE   Flags: Fragment;
GN   ORFNames=Anapl_02636 {ECO:0000313|EMBL:EOA98693.1};
OS   Anas platyrhynchos (Mallard) (Anas boschas).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Anseriformes; Anatidae;
OC   Anatinae; Anas.
OX   NCBI_TaxID=8839 {ECO:0000313|EMBL:EOA98693.1, ECO:0000313|Proteomes:UP000296049};
RN   [1] {ECO:0000313|EMBL:EOA98693.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Li N.;
RT   "The genome sequence and transcriptome of duck provide insight into the
RT   interaction host.";
RL   Submitted (APR-2010) to the EMBL/GenBank/DDBJ databases.
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   EMBL; KB743446; EOA98693.1; -; Genomic_DNA.
DR   AlphaFoldDB; R0KZE2; -.
DR   Proteomes; UP000296049; Unassembled WGS sequence.
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; IPR003048; P2X5_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:SF12; P2X PURINOCEPTOR 5; 1.
DR   Pfam; PF00864; P2X_receptor; 1.
DR   PIRSF; PIRSF005713; P2X_purinoceptor; 1.
DR   PRINTS; PR01312; P2X5RECEPTOR.
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   Reference proteome {ECO:0000313|Proteomes:UP000296049};
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        31..50
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU000681"
FT   TRANSMEM        341..363
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU000681"
FT   REGION          376..399
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        381..399
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         69..71
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005713-1"
FT   BINDING         189
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        187
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005713-3"
FT   DISULFID        118..169
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005713-2"
FT   DISULFID        129..152
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005713-2"
FT   DISULFID        135..163
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005713-2"
FT   DISULFID        220..229
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005713-2"
FT   DISULFID        263..272
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005713-2"
FT   NON_TER         399
FT                   /evidence="ECO:0000313|EMBL:EOA98693.1"
SQ   SEQUENCE   399 AA;  44682 MW;  864548D3378EE40C CRC64;
     MGQVAWKGLF LSLFDYKTEK YVIAKNKKVG ILYRVVQLSI LAYLVGWVFV VKKGYQDTDT
     SLQSSVITKL KGVAFTNTSE LGERLWDVAD YVIPPQGENV FFVMTNLIVT PNQKQATCPE
     SASIPDALCY KDGDCPAGQA VVAGNGVKTG RCLKERDSIR GTCEILAWCP VEKRSKPKKP
     LLASAENFTV YIKNSIRFPK FKFSKMNVLV TDNESYLKSC RYSTEHPYCP IFLLGNIVRW
     AGSDFHEMAL EGGVIGIQIE WNCDLDKAPS ECNPHYSFSR LDNKFAEKSI SSGYNFRFAK
     YYRDANGVDY RTLFKAYGIR FDVMVNGKAG KFNIIPTVIN IGSGLALMGA GAFFCDLVLL
     YLIKKSNFYR GKKYEEVKSS SRKSLSSPTL NGNQSPDQL
//
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