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Database: UniProt
Entry: A0A2Y9QXW4_TRIMA
LinkDB: A0A2Y9QXW4_TRIMA
Original site: A0A2Y9QXW4_TRIMA 
ID   A0A2Y9QXW4_TRIMA        Unreviewed;       503 AA.
AC   A0A2Y9QXW4;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=P2X purinoceptor {ECO:0000256|RuleBase:RU000681};
GN   Name=LOC101344030 {ECO:0000313|RefSeq:XP_023586912.1};
OS   Trichechus manatus latirostris (Florida manatee).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Afrotheria; Sirenia; Trichechidae; Trichechus.
OX   NCBI_TaxID=127582 {ECO:0000313|Proteomes:UP000248480, ECO:0000313|RefSeq:XP_023586912.1};
RN   [1] {ECO:0000313|RefSeq:XP_023586912.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (NOV-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}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|RuleBase:RU000681}.
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DR   RefSeq; XP_023586912.1; XM_023731144.1.
DR   AlphaFoldDB; A0A2Y9QXW4; -.
DR   Proteomes; UP000248480; 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; 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; 2.
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:UP000248480};
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   REGION          414..463
FT                   /note="Disordered"
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         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   DISULFID        118..168
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005713-2"
FT   DISULFID        129..152
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005713-2"
FT   DISULFID        135..162
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005713-2"
FT   DISULFID        219..228
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005713-2"
FT   DISULFID        262..271
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005713-2"
SQ   SEQUENCE   503 AA;  56128 MW;  83450FF3A19642E8 CRC64;
     MGQGGWKGLC LSLFDYKTEK YVIAKNKKVG LLYRLLQLSI LLYLVVWVFM VKKGYQDIDT
     SLQSAVITKV KGVAFTNTSE LGERLWDVAD YVIPPQGESV FVVMTNLIVT PNQRQDTCAE
     NEDILNAKCS KDSDCHPGEA VVAGNGVKTG RCLRVGSAKG TCEIFAWCPV ETKSKPAKLL
     LDEAEEFTIY IKNSIRFPKF NFSKTNVLDT KNSSFLKTCR FDLNNLYCPI FRLGSVVRWA
     GSNFQEMALE GGVIGIHIEW DCDLDKASSE CNPQYSFSRL DNRFAEKSIS SGYNFRFAKY
     YRDASGVEFR TLMKAYGIRF DVMVNGKAGK FSIIPTVINV SSGVALMGAR EAHPQLSMWV
     KLEQRDLGER HLKGAFFCDL VLIYFIKKSH FYRGKKYEEV RGRECRAQLV ESQRQGGAWE
     AKDAAGPGPG PRGVEQSPRA EPEGQRPGLP QRQEAQDRGG GSNGDGCVCR RLLEGCAQPA
     SSGHLEERKV NVEQLQTLQA VET
//
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