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Database: UniProt
Entry: A0A2Y9KS52_ENHLU
LinkDB: A0A2Y9KS52_ENHLU
Original site: A0A2Y9KS52_ENHLU 
ID   A0A2Y9KS52_ENHLU        Unreviewed;       464 AA.
AC   A0A2Y9KS52;
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=LOC111158822 {ECO:0000313|RefSeq:XP_022376802.1};
OS   Enhydra lutris kenyoni (northern sea otter).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC   Lutrinae; Enhydra.
OX   NCBI_TaxID=391180 {ECO:0000313|Proteomes:UP000248482, ECO:0000313|RefSeq:XP_022376802.1};
RN   [1] {ECO:0000313|RefSeq:XP_022376802.1}
RP   IDENTIFICATION.
RC   TISSUE=Blood {ECO:0000313|RefSeq:XP_022376802.1};
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}.
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DR   RefSeq; XP_022376802.1; XM_022521094.1.
DR   AlphaFoldDB; A0A2Y9KS52; -.
DR   STRING; 391180.A0A2Y9KS52; -.
DR   KEGG; elk:111158822; -.
DR   OrthoDB; 5312692at2759; -.
DR   Proteomes; UP000248482; 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; 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; 1.
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|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:UP000248482};
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        31..50
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU000681"
FT   TRANSMEM        341..363
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU000681"
FT   REGION          386..415
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         189
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005713-1"
FT   BINDING         295..297
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005713-1"
FT   BINDING         315
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005713-1"
FT   DISULFID        118..169
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005713-2"
FT   DISULFID        129..152
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005713-2"
FT   DISULFID        135..163
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005713-2"
FT   DISULFID        220..229
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005713-2"
FT   DISULFID        263..272
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005713-2"
SQ   SEQUENCE   464 AA;  51504 MW;  EBEB020A7D71EAEF CRC64;
     MGQAGCKGLS QSLFDYKTEK YVIAKNKKVG LLYRLLQVSI LTYLVVWVFL VKKGYQDTDT
     SLQSSIITKV KGVTFTNTSE LGERLWDVAD YVIPPQGENV FFVVTNLIVT PNQRQETCAE
     SESIPDAWCY TDSDCPSGDP VVAGNGVKTG RCLRVGNMQR GTCEIFAWCP VETKSRPVKP
     LLGKAEDFTV YIKNFIRFPK FNFSKTNVLD TKDRAFLKSC QFGPKNPYCP IFRLGSVVSW
     TGSNFQEIAL QGGVIGIQIE WDCDLDKAPS ECNPHYSFSR LDNKFSENSI SSGYNFRFAK
     YYRDGAGVEF RTLMKAYGIR FDVMVNGKAG KFSIIPTIIN IGSGVALMGA GAFFCDLVLI
     YFIKKSHFYR DKKYEEVRIL RVPPGLAESS QQGRTPEAEE AEQPEVHHGG GSQKGNGCPC
     QQLLEPVSPH RAACLLCSPS IRIIAVPPST RLTLPATSLS SSYV
//
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