ID A0A2Y9E4J3_TRIMA Unreviewed; 422 AA.
AC A0A2Y9E4J3;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=P2X purinoceptor {ECO:0000256|PIRNR:PIRNR005713, ECO:0000256|RuleBase:RU000681};
GN Name=LOC101350747 {ECO:0000313|RefSeq:XP_004386276.1};
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_004386276.1};
RN [1] {ECO:0000313|RefSeq:XP_004386276.1}
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|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 RefSeq; XP_004386276.1; XM_004386219.3.
DR AlphaFoldDB; A0A2Y9E4J3; -.
DR STRING; 127582.A0A2Y9E4J3; -.
DR GlyCosmos; A0A2Y9E4J3; 1 site, No reported glycans.
DR GeneID; 101350747; -.
DR KEGG; tmu:101350747; -.
DR InParanoid; A0A2Y9E4J3; -.
DR OrthoDB; 5312692at2759; -.
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-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|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|PIRNR:PIRNR005713}.
FT TRANSMEM 333..351
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU000681"
FT REGION 393..422
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 68..70
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR005713-1"
FT BINDING 186
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR005713-1"
FT BINDING 284..286
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR005713-1"
FT BINDING 304
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR005713-1"
FT CARBOHYD 184
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000256|PIRSR:PIRSR005713-3"
FT DISULFID 116..166
FT /evidence="ECO:0000256|PIRSR:PIRSR005713-2"
FT DISULFID 127..150
FT /evidence="ECO:0000256|PIRSR:PIRSR005713-2"
FT DISULFID 133..160
FT /evidence="ECO:0000256|PIRSR:PIRSR005713-2"
FT DISULFID 217..227
FT /evidence="ECO:0000256|PIRSR:PIRSR005713-2"
FT DISULFID 261..270
FT /evidence="ECO:0000256|PIRSR:PIRSR005713-2"
SQ SEQUENCE 422 AA; 45882 MW; B6B05FAD402760D4 CRC64;
MGAPGAAAGW GLLDYKTEKY VMTRNWRVGA LQRLLQLGVA AYLVGWALLT KKGYQEQDLD
PEVSVITKLK GVSVTQIKDL GNQLWDMADF VKPPQGENVF LVTNFLVTPA QVQGKCPEHP
SVPLAACWTD EDCPEGETGT HSHGIKTGQC VVFNGTHSTC EIHGWCPVES GVVQGKPLLA
QAENFTLFIK NTVTFSKFNF SKSNALKTWD ATYFKRCRYD PHASPYCPVF RIGDLVQAAG
GVFEDLALLG GAVGIRVHWD CDLDAGGSDC QPHYSFQLQG RSYNFRTATH WWEATGVEAR
SLLKLYGIHF DILVTGQAGK FGLIPTTITL GTGAAWLGVV TFLCDLLLLY VDREAHFYWR
TKYEEAKAPK VTANSVCNEL AFIPPLAGPA RTPTNAAGSL TPTPGRPRLG AGTSGSHSLA
PS
//
