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Database: UniProt
Entry: A0A3Q0DFC8_MESAU
LinkDB: A0A3Q0DFC8_MESAU
Original site: A0A3Q0DFC8_MESAU 
ID   A0A3Q0DFC8_MESAU        Unreviewed;       495 AA.
AC   A0A3Q0DFC8;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=P2X purinoceptor {ECO:0000256|RuleBase:RU000681};
GN   Name=P2rx2 {ECO:0000313|RefSeq:XP_021091717.1};
OS   Mesocricetus auratus (Golden hamster).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC   Cricetidae; Cricetinae; Mesocricetus.
OX   NCBI_TaxID=10036 {ECO:0000313|Proteomes:UP000189706, ECO:0000313|RefSeq:XP_021091717.1};
RN   [1] {ECO:0000313|RefSeq:XP_021091717.1}
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}.
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DR   RefSeq; XP_021091717.1; XM_021236058.1.
DR   AlphaFoldDB; A0A3Q0DFC8; -.
DR   GlyCosmos; A0A3Q0DFC8; 1 site, No reported glycans.
DR   Proteomes; UP000189706; 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; IPR003045; P2X2_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:SF4; P2X PURINOCEPTOR 2; 1.
DR   Pfam; PF00864; P2X_receptor; 1.
DR   PIRSF; PIRSF005713; P2X_purinoceptor; 1.
DR   PRINTS; PR01309; P2X2RECEPTOR.
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}; Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Nucleotide-binding {ECO:0000256|PIRSR:PIRSR005713-1};
KW   Receptor {ECO:0000256|RuleBase:RU000681};
KW   Reference proteome {ECO:0000313|Proteomes:UP000189706};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU000681}.
FT   REGION          416..437
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          469..495
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        477..495
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         94..96
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005713-1"
FT   BINDING         209
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005713-1"
FT   BINDING         311..313
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005713-1"
FT   BINDING         331
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005713-1"
FT   CARBOHYD        207
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005713-3"
FT   DISULFID        138..189
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005713-2"
FT   DISULFID        149..172
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005713-2"
FT   DISULFID        155..183
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005713-2"
FT   DISULFID        237..247
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005713-2"
FT   DISULFID        281..290
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005713-2"
SQ   SEQUENCE   495 AA;  54787 MW;  01A1A67364CFAB6F CRC64;
     MAAAQPGLPA GAAMVQRLVR GCWSAFWDYE TPKVIVVRNR RLGFVHRTVQ LLILLYFVWV
     ASRTGTALFL RYVFIVQKSY QDSETGPESS IITKVKGITI SEHKVWDVEE YVKPPEGGSV
     VSIITRMEVT PSQTLGTCPE SMKVHSSACH SDDDCVAGQL DMQGNGIRTG HCVPYYHGDS
     KTCEVSAWCP VEDGTSENQF LGKMAPNFTI LIKNNIHYPK FKFSKGNIAS QKNLKHCTFD
     QDSDPYCPIF KLGFIVEQAG ENFTELAHKG GVIGVIINWN CDLDLSESEC NPKYSFRRLD
     PKYDPASSGY NFRFAKYYKI NSTTTTRTLI KAYGIRIDVI VHGQAGKFSL IPTIINLATA
     LTSIGVGSFL CDWILLTFMN KNKLYSHKKF DKVRTPRHTS NSWPVTLALV LGQIPPPPSH
     YPQDQSPSPP SGRGSTLGEV AELPLAVQPP RPCSISALTE QVVDTLDLHV GQRLPVPEPS
     QQDSTSTDPK GLAQL
//
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