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Database: UniProt
Entry: A0A3Q0HKA3_ALLSI
LinkDB: A0A3Q0HKA3_ALLSI
Original site: A0A3Q0HKA3_ALLSI 
ID   A0A3Q0HKA3_ALLSI        Unreviewed;       397 AA.
AC   A0A3Q0HKA3;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   RecName: Full=P2X purinoceptor {ECO:0000256|PIRNR:PIRNR005713, ECO:0000256|RuleBase:RU000681};
GN   Name=P2RX2 {ECO:0000313|RefSeq:XP_025072389.1};
OS   Alligator sinensis (Chinese alligator).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Crocodylia; Alligatoridae; Alligatorinae;
OC   Alligator.
OX   NCBI_TaxID=38654 {ECO:0000313|Proteomes:UP000189705, ECO:0000313|RefSeq:XP_025072389.1};
RN   [1] {ECO:0000313|RefSeq:XP_025072389.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (SEP-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}.
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DR   RefSeq; XP_025072389.1; XM_025216604.1.
DR   AlphaFoldDB; A0A3Q0HKA3; -.
DR   KEGG; asn:102383977; -.
DR   Proteomes; UP000189705; 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; 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|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:UP000189705};
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        57..75
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU000681"
FT   TRANSMEM        359..381
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU000681"
FT   BINDING         95..97
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005713-1"
FT   BINDING         210
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005713-1"
FT   BINDING         314..316
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005713-1"
FT   BINDING         333
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005713-1"
FT   DISULFID        139..190
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005713-2"
FT   DISULFID        150..173
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005713-2"
FT   DISULFID        156..184
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005713-2"
FT   DISULFID        240..250
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005713-2"
FT   DISULFID        284..293
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005713-2"
SQ   SEQUENCE   397 AA;  44834 MW;  D0865E95FF2DEB6B CRC64;
     MENSVFPQRL PFHPRPPTEE STVIGNTDAV RCWECFWEFW NYETPKVIVV KNHNLGILYR
     AMQLLILIYF IWYVFIIQKG YQESETGPES SVITKVKGIT HSHDKVWDVE EYVKPPEGGS
     VFSIITRVEV THSQTLKTCP ESMAVPNATC ISDSDCIAGK MDMLGNGERT GRCIPHYSGT
     VKTCEILAWC PVENGGAISD SLGKMAPQFT ILIKNSIHFP RFGFSKGNIK DDKNGYLKRC
     TFNETSDLYC PIFRLGFIVE QAGENFTELA EKGGVIGVII NWNCNLDLPD SACNPRYSFQ
     RLDPKTIQES SGYNYRFAKY FNCNGTNTRI LIKAYGIRID VIVHGQAGKF SLIPTIINLA
     TALTSVGVGS FLCDWILLTF MNKNKVYSTR KFDQERP
//
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