ID M3XMD9_MUSPF Unreviewed; 397 AA.
AC M3XMD9;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE RecName: Full=P2X purinoceptor {ECO:0000256|PIRNR:PIRNR005713, ECO:0000256|RuleBase:RU000681};
GN Name=P2RX3 {ECO:0000313|Ensembl:ENSMPUP00000000239.1,
GN ECO:0000313|RefSeq:XP_004777633.1};
OS Mustela putorius furo (European domestic ferret) (Mustela furo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Mustelinae; Mustela.
OX NCBI_TaxID=9669 {ECO:0000313|Ensembl:ENSMPUP00000000239.1};
RN [1] {ECO:0000313|Ensembl:ENSMPUP00000000239.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (MAR-2023) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_004777633.1}
RP IDENTIFICATION.
RC TISSUE=Brain {ECO:0000313|RefSeq:XP_004777633.1};
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AEYP01091600; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_004777633.1; XM_004777576.2.
DR STRING; 9669.ENSMPUP00000000239; -.
DR Ensembl; ENSMPUT00000000243.1; ENSMPUP00000000239.1; ENSMPUG00000000242.1.
DR GeneID; 101685193; -.
DR KEGG; mpuf:101685193; -.
DR CTD; 5024; -.
DR eggNOG; ENOG502QUDE; Eukaryota.
DR GeneTree; ENSGT01020000230351; -.
DR HOGENOM; CLU_034469_8_0_1; -.
DR OMA; ITPMMEV; -.
DR OrthoDB; 5312692at2759; -.
DR Proteomes; UP000000715; Unplaced.
DR GO; GO:0030424; C:axon; IEA:Ensembl.
DR GO; GO:0098686; C:hippocampal mossy fiber to CA3 synapse; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0098794; C:postsynapse; IEA:GOC.
DR GO; GO:0043235; C:receptor complex; IEA:Ensembl.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IEA:Ensembl.
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:0048266; P:behavioral response to pain; IEA:Ensembl.
DR GO; GO:0071318; P:cellular response to ATP; IEA:Ensembl.
DR GO; GO:0051649; P:establishment of localization in cell; IEA:Ensembl.
DR GO; GO:0098662; P:inorganic cation transmembrane transport; IEA:Ensembl.
DR GO; GO:0007274; P:neuromuscular synaptic transmission; IEA:Ensembl.
DR GO; GO:0030432; P:peristalsis; IEA:Ensembl.
DR GO; GO:0070207; P:protein homotrimerization; IEA:Ensembl.
DR GO; GO:0048167; P:regulation of synaptic plasticity; IEA:Ensembl.
DR GO; GO:0009743; P:response to carbohydrate; IEA:Ensembl.
DR GO; GO:0009409; P:response to cold; IEA:Ensembl.
DR GO; GO:0009408; P:response to heat; IEA:Ensembl.
DR GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
DR GO; GO:0009612; P:response to mechanical stimulus; IEA:Ensembl.
DR GO; GO:0050909; P:sensory perception of taste; IEA:Ensembl.
DR GO; GO:0014832; P:urinary bladder smooth muscle contraction; IEA:Ensembl.
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; IPR003046; P2X3_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:SF8; P2X PURINOCEPTOR 3; 1.
DR Pfam; PF00864; P2X_receptor; 1.
DR PIRSF; PIRSF005713; P2X_purinoceptor; 1.
DR PRINTS; PR01310; P2X3RECEPTOR.
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:UP000000715};
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 326..347
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU000681"
FT REGION 372..397
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 63..65
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR005713-1"
FT BINDING 172
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR005713-1"
FT BINDING 279..281
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR005713-1"
FT BINDING 299
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR005713-1"
FT CARBOHYD 170
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000256|PIRSR:PIRSR005713-3"
FT DISULFID 107..153
FT /evidence="ECO:0000256|PIRSR:PIRSR005713-2"
FT DISULFID 116..137
FT /evidence="ECO:0000256|PIRSR:PIRSR005713-2"
FT DISULFID 122..147
FT /evidence="ECO:0000256|PIRSR:PIRSR005713-2"
FT DISULFID 203..213
FT /evidence="ECO:0000256|PIRSR:PIRSR005713-2"
FT DISULFID 247..256
FT /evidence="ECO:0000256|PIRSR:PIRSR005713-2"
SQ SEQUENCE 397 AA; 44309 MW; D3AF09EAA07CA346 CRC64;
MNCVSDFFTY ETTKSVVVKS WTIGVINRAV QLLIISYFVG WVFLHEKAYQ VRDTAIESSV
VTKVKGFGRY ANRVMDVSDY VTPPQGTSVF VIITKMIVTE NQMQGFCPES EEKYRCVSDS
QCGPQRFPGG GILTGRCVNY SSVLRTCEIQ GWCPTEVDTV EMPVMMEAEN FTIFIKNSIR
FPLFNFEKGN LLPNLTARDM KTCRFHPDKD PFCPILRVGD VVKFAGQDFA KLASTGGVLG
IKIGWVCDLD RAWDQCIPKY SFTRLDGVSE KSSVSPGYNF RFAKYYKMEN GSEYRTLLKA
FGIRFDVLVY GNAGKFNIIP TIISSVAAFT SVGVGTVLCD IILLNFLKGA DQYKAKKFEE
VDETTLKVTA SANPECSSDQ TTEEKQSTDS GAYSIGH
//
