GenomeNet

Database: UniProt
Entry: A0A3B3QPP1_9TELE
LinkDB: A0A3B3QPP1_9TELE
Original site: A0A3B3QPP1_9TELE 
ID   A0A3B3QPP1_9TELE        Unreviewed;       422 AA.
AC   A0A3B3QPP1;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   RecName: Full=G protein-activated inward rectifier potassium channel 1 {ECO:0000256|ARBA:ARBA00015495};
DE   AltName: Full=Inward rectifier K(+) channel Kir3.1 {ECO:0000256|ARBA:ARBA00032145};
DE   AltName: Full=Potassium channel, inwardly rectifying subfamily J member 3 {ECO:0000256|ARBA:ARBA00031390};
GN   Name=KCNJ5 {ECO:0000313|Ensembl:ENSPKIP00000008667.1};
OS   Paramormyrops kingsleyae.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Osteoglossocephala;
OC   Osteoglossomorpha; Osteoglossiformes; Mormyridae; Paramormyrops.
OX   NCBI_TaxID=1676925 {ECO:0000313|Ensembl:ENSPKIP00000008667.1, ECO:0000313|Proteomes:UP000261540};
RN   [1] {ECO:0000313|Ensembl:ENSPKIP00000008667.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- FUNCTION: This potassium channel is controlled by G proteins. Inward
CC       rectifier potassium channels are characterized by a greater tendency to
CC       allow potassium to flow into the cell rather than out of it. Their
CC       voltage dependence is regulated by the concentration of extracellular
CC       potassium; as external potassium is raised, the voltage range of the
CC       channel opening shifts to more positive voltages. The inward
CC       rectification is mainly due to the blockage of outward current by
CC       internal magnesium. This receptor plays a crucial role in regulating
CC       the heartbeat. {ECO:0000256|ARBA:ARBA00024877}.
CC   -!- SUBUNIT: Associates with GIRK2, GIRK3 or GIRK4 to form a G-protein
CC       activated heteromultimer pore-forming unit. The resulting inward
CC       current is much larger. {ECO:0000256|ARBA:ARBA00025883}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141,
CC       ECO:0000256|RuleBase:RU003822}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU003822}.
CC   -!- SIMILARITY: Belongs to the inward rectifier-type potassium channel (TC
CC       1.A.2.1) family. KCNJ3 subfamily. {ECO:0000256|ARBA:ARBA00009002}.
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   AlphaFoldDB; A0A3B3QPP1; -.
DR   STRING; 1676925.ENSPKIP00000008667; -.
DR   Ensembl; ENSPKIT00000032750.1; ENSPKIP00000008667.1; ENSPKIG00000024064.1.
DR   GeneTree; ENSGT01080000257365; -.
DR   OrthoDB; 4126787at2759; -.
DR   Proteomes; UP000261540; Unplaced.
DR   GO; GO:0034702; C:monoatomic ion channel complex; IEA:UniProtKB-KW.
DR   GO; GO:0015467; F:G-protein activated inward rectifier potassium channel activity; IEA:InterPro.
DR   Gene3D; 1.10.287.70; -; 1.
DR   Gene3D; 2.60.40.1400; G protein-activated inward rectifier potassium channel 1; 1.
DR   InterPro; IPR014756; Ig_E-set.
DR   InterPro; IPR041647; IRK_C.
DR   InterPro; IPR016449; K_chnl_inward-rec_Kir.
DR   InterPro; IPR003274; K_chnl_inward-rec_Kir3.1.
DR   InterPro; IPR013518; K_chnl_inward-rec_Kir_cyto.
DR   InterPro; IPR040445; Kir_TM.
DR   PANTHER; PTHR11767:SF52; G PROTEIN-ACTIVATED INWARD RECTIFIER POTASSIUM CHANNEL 4; 1.
DR   PANTHER; PTHR11767; INWARD RECTIFIER POTASSIUM CHANNEL; 1.
DR   Pfam; PF01007; IRK; 1.
DR   Pfam; PF17655; IRK_C; 1.
DR   PRINTS; PR01327; KIR31CHANNEL.
DR   PRINTS; PR01320; KIRCHANNEL.
DR   SUPFAM; SSF81296; E set domains; 1.
DR   SUPFAM; SSF81324; Voltage-gated potassium channels; 1.
PE   3: Inferred from homology;
KW   Ion channel {ECO:0000256|ARBA:ARBA00023303, ECO:0000256|RuleBase:RU003822};
KW   Ion transport {ECO:0000256|ARBA:ARBA00023065,
KW   ECO:0000256|RuleBase:RU003822};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Potassium {ECO:0000256|ARBA:ARBA00022958, ECO:0000256|RuleBase:RU003822};
KW   Potassium transport {ECO:0000256|ARBA:ARBA00022538,
KW   ECO:0000256|RuleBase:RU003822};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU003822};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU003822};
KW   Voltage-gated channel {ECO:0000256|ARBA:ARBA00022882,
KW   ECO:0000256|RuleBase:RU003822}.
FT   TRANSMEM        88..111
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        165..188
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          54..193
FT                   /note="Potassium channel inwardly rectifying transmembrane"
FT                   /evidence="ECO:0000259|Pfam:PF01007"
FT   DOMAIN          200..368
FT                   /note="Inward rectifier potassium channel C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17655"
FT   REGION          363..387
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   422 AA;  47719 MW;  7648DD3781C815D7 CRC64;
     MAGDSRAYTD HDLEIGVLST KVKKLPKPVR EIPICTDRMC LVSESAKKPR QRYVQKDGKC
     NVHHGNVQET YRYLSDLFTT LVDLEWHFSL LVFTLVYCVT WLFFGLLWWL IAYARGDLGH
     LGEESWTPCV ENLNSFVSAF LFSIETETTI GYGHRVITDK CPEGIILLLL QAILGSIVNA
     LMVGCMFVKI SQPKKRAETL VFSHKAVVSV RDGRLCLMFR VGDLRNSHIV EASIRAKLIR
     SQQTKEGEFI PLNQTDINVG FDTGDDRLFL VSPLTIAHEI NERSPFWEWS QARMEKEEFE
     MVVILEGMVE ATGMTCQARS SYLDTEVLWG YRFTPVLSLE QGFYEVDYTS FHEIYATDTP
     SCSAKELANG PRGPQTSPLL PRPDPAPRLH LRDLPMILEP LLLECDEEGE VEESNSPTGG
     VG
//
DBGET integrated database retrieval system