ID A0A455AJ87_PHYMC Unreviewed; 406 AA.
AC A0A455AJ87;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=P2X purinoceptor {ECO:0000256|PIRNR:PIRNR005713, ECO:0000256|RuleBase:RU000681};
GN Name=P2RX6 {ECO:0000313|RefSeq:XP_028335898.1,
GN ECO:0000313|RefSeq:XP_028335899.1, ECO:0000313|RefSeq:XP_054936240.1,
GN ECO:0000313|RefSeq:XP_054936241.1, ECO:0000313|RefSeq:XP_054936242.1,
GN ECO:0000313|RefSeq:XP_054936243.1, ECO:0000313|RefSeq:XP_054936244.1};
OS Physeter macrocephalus (Sperm whale) (Physeter catodon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Physeteridae; Physeter.
OX NCBI_TaxID=9755 {ECO:0000313|Proteomes:UP000248484, ECO:0000313|RefSeq:XP_028335898.1};
RN [1] {ECO:0000313|RefSeq:XP_028335898.1, ECO:0000313|RefSeq:XP_028335899.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_028335898.1,
RC ECO:0000313|RefSeq:XP_028335899.1};
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}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|RuleBase:RU000681}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR RefSeq; XP_028335898.1; XM_028480097.2.
DR RefSeq; XP_028335899.1; XM_028480098.2.
DR RefSeq; XP_054936240.1; XM_055080265.1.
DR RefSeq; XP_054936241.1; XM_055080266.1.
DR RefSeq; XP_054936242.1; XM_055080267.1.
DR RefSeq; XP_054936243.1; XM_055080268.1.
DR RefSeq; XP_054936244.1; XM_055080269.1.
DR OrthoDB; 5312692at2759; -.
DR Proteomes; UP000248484; Chromosome 19.
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; IPR003049; P2X6_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:SF21; P2X PURINOCEPTOR 6; 1.
DR Pfam; PF00864; P2X_receptor; 1.
DR PIRSF; PIRSF005713; P2X_purinoceptor; 1.
DR PRINTS; PR01313; P2X6RECEPTOR.
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:UP000248484};
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 347..365
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU000681"
FT REGION 1..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 383..406
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..53
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 81..83
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR005713-1"
FT BINDING 200
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR005713-1"
FT BINDING 298..300
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR005713-1"
FT BINDING 318
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR005713-1"
FT CARBOHYD 198
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000256|PIRSR:PIRSR005713-3"
FT DISULFID 130..180
FT /evidence="ECO:0000256|PIRSR:PIRSR005713-2"
FT DISULFID 141..164
FT /evidence="ECO:0000256|PIRSR:PIRSR005713-2"
FT DISULFID 147..174
FT /evidence="ECO:0000256|PIRSR:PIRSR005713-2"
FT DISULFID 231..241
FT /evidence="ECO:0000256|PIRSR:PIRSR005713-2"
FT DISULFID 275..284
FT /evidence="ECO:0000256|PIRSR:PIRSR005713-2"
SQ SEQUENCE 406 AA; 45013 MW; B69707FEE32BCA89 CRC64;
MGPHVKVEEA SPQPPSPGGP RSKEHGQRAE DHRGSRREPW VLDDGDWQSG KTRSKHRGWA
LLAKKGYQEQ DLDPQISVIT KLKGVSVTQI KELGNRLWDV ADFVKPPQGE NMFFLVTNFL
VTPEQVQGRC PEHPSIPLAS CWADQDCPEG ETGTHSHGIK TGQCVVFNGT HRTCEIRGWC
PVESGAVPVK PLLVQAENFT LFIKNTITFS KFNFSKSNAL DTQDPTYFKR CRYDPRSSPS
CPVFRIGDLV AAAGGVFEDL ALLGGAMGVH VHWNCDLDAR GSDCRPHYSF QLQERSYNFR
MATHWWEASG VEARSLLKLY GIRFDILVTG QAGKFGLIPT LVTLGTGAAW LGVITFLCDL
LLLYVDGEAH FYWRTKYEEA KAPKVTASPE QTKPASAPLH LAAQAP
//
