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Database: UniProt
Entry: A0A1S3REW4_SALSA
LinkDB: A0A1S3REW4_SALSA
Original site: A0A1S3REW4_SALSA 
ID   A0A1S3REW4_SALSA        Unreviewed;       403 AA.
AC   A0A1S3REW4;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=P2X purinoceptor {ECO:0000256|PIRNR:PIRNR005713, ECO:0000256|RuleBase:RU000681};
GN   Name=LOC106602642 {ECO:0000313|RefSeq:XP_014050863.1};
OS   Salmo salar (Atlantic salmon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC   Salmonidae; Salmoninae; Salmo.
OX   NCBI_TaxID=8030 {ECO:0000313|Proteomes:UP000087266, ECO:0000313|RefSeq:XP_014050863.1};
RN   [1] {ECO:0000313|RefSeq:XP_014050863.1}
RP   IDENTIFICATION.
RC   TISSUE=Muscle {ECO:0000313|RefSeq:XP_014050863.1};
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_014050863.1; XM_014195388.1.
DR   AlphaFoldDB; A0A1S3REW4; -.
DR   STRING; 8030.ENSSSAP00000102718; -.
DR   PaxDb; 8030-ENSSSAP00000102718; -.
DR   KEGG; sasa:106602642; -.
DR   OrthoDB; 5312692at2759; -.
DR   Proteomes; UP000087266; Chromosome ssa04.
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; 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:UP000087266};
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        26..45
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU000681"
FT   TRANSMEM        325..350
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU000681"
FT   BINDING         64..66
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005713-1"
FT   BINDING         175
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005713-1"
FT   BINDING         282..284
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005713-1"
FT   BINDING         302
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005713-1"
FT   DISULFID        108..156
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005713-2"
FT   DISULFID        117..140
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005713-2"
FT   DISULFID        123..150
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005713-2"
FT   DISULFID        206..216
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005713-2"
FT   DISULFID        250..259
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005713-2"
SQ   SEQUENCE   403 AA;  45855 MW;  B2321FA10990A595 CRC64;
     MWTCITDFFT YETTKSVVVK SWTIGIINRV VQLLIIIYFI GWVFVYEKAY QIRDTAIESS
     VMTKVKGFGL YNNRVMDVAE YVTPSQGASV FCIITKLITT ENQVQGYCPE SEMKYKCTHD
     NNCTKFLNKP GGNGLPTGRC VRFNDTLNTC EIRGWCQAEI DYIKTHPMME VEDFTIFIKN
     SIRFPLFNFT KGNFLPTITP QYIKACNFDH ENNTYCPIFR VGDVIRYAHQ NFTMLAQKGG
     VIGIKIGWMC DLDKSEDECN PSYSFTRLDA MSEKNSVSPG YNFRYAKYYK MDNGTDYRTL
     LKAYAIRFDV LVNGNAGKFN MIPTLINMVA AFTSVGVGTV LCDIILLNFL KGAEQYKAKK
     FEEVSDTQIE NSLSSNGLYR SREFIGVEKQ SNDSGAFSIG QYG
//
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