ID A0A1S3LR02_SALSA Unreviewed; 480 AA.
AC A0A1S3LR02;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=P2X purinoceptor {ECO:0000256|PIRNR:PIRNR005713, ECO:0000256|RuleBase:RU000681};
GN Name=p2rx5 {ECO:0000313|RefSeq:XP_013993408.1};
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_013993408.1};
RN [1] {ECO:0000313|RefSeq:XP_013993408.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_013993408.1};
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_013993408.1; XM_014137933.1.
DR AlphaFoldDB; A0A1S3LR02; -.
DR GlyCosmos; A0A1S3LR02; 1 site, No reported glycans.
DR Ensembl; ENSSSAT00000018825; ENSSSAP00000017722; ENSSSAG00000085000.
DR GeneID; 106567984; -.
DR OrthoDB; 5312692at2759; -.
DR Proteomes; UP000087266; Chromosome ssa13.
DR Bgee; ENSSSAG00000008442; Expressed in muscle tissue and 6 other cell types or tissues.
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; 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; 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 60..79
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU000681"
FT TRANSMEM 363..388
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU000681"
FT REGION 412..480
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 412..470
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 98..100
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR005713-1"
FT BINDING 214
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR005713-1"
FT BINDING 320..322
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR005713-1"
FT BINDING 340
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR005713-1"
FT CARBOHYD 212
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000256|PIRSR:PIRSR005713-3"
FT DISULFID 147..194
FT /evidence="ECO:0000256|PIRSR:PIRSR005713-2"
FT DISULFID 158..181
FT /evidence="ECO:0000256|PIRSR:PIRSR005713-2"
FT DISULFID 164..188
FT /evidence="ECO:0000256|PIRSR:PIRSR005713-2"
FT DISULFID 245..255
FT /evidence="ECO:0000256|PIRSR:PIRSR005713-2"
FT DISULFID 289..298
FT /evidence="ECO:0000256|PIRSR:PIRSR005713-2"
SQ SEQUENCE 480 AA; 54398 MW; D1299BEBC9F80326 CRC64;
MIAHAIATDF SAVSLTRAVT RLSKSGDRNM GELTWRIFFL GFLNFKTEKY VIAENRKLGI
SFRVFQICVL LYVIGWVLVY KKGYQSREET VQSSVITKLK GVVMTNNTES GLYLWGAEDY
VIPPTGEQVF FIVTNYLETP NQRLGFCAES PKVPDGQCVN NEDCAEGEVV IAGNGVKTGL
CLNSTGTCEI HGWCPVETGR KPSEALLSKA ENFTIYIKNF VRFPKFEFSK SNVLDTGNDS
YLKRCSYDNI LQPYCPIFRL GDLVSRTGHD FQDMAVVGGS VGILIEWNCD LDKDYSQCNP
KYSFTRLDIN LNSTVTSGYN FRYARYYKDE AGESFRTLYK VYGIRFDIMV NGRAGKFNII
PTVIAIGSGL AIMGMGKFVC DMIFIYMMST SSYFRDRKFE ILKKERIKKH KESAKTVVNR
DTRKHRTHAG EQHELTTLST KKEEKPEPTT QDAEKQDLKT GEKKEVHILS PRTVGQRLAD
//
