KCNJ5_PIG
ID KCNJ5_PIG Reviewed; 419 AA.
AC O02670;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=G protein-activated inward rectifier potassium channel 4;
DE Short=GIRK-4;
DE AltName: Full=Cardiac inward rectifier;
DE Short=CIR;
DE AltName: Full=Heart KATP channel;
DE AltName: Full=Inward rectifier K(+) channel Kir3.4;
DE AltName: Full=KATP-1;
DE AltName: Full=Potassium channel, inwardly rectifying subfamily J member 5;
GN Name=KCNJ5;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC TISSUE=Heart;
RX PubMed=8834003;
RA Iizuka M., Kubo Y., Tsunenari I., Pan C.X., Akiba I., Kono T.;
RT "Functional characterization and localization of a cardiac-type inwardly
RT rectifying K+ channel.";
RL Recept. Channels 3:299-315(1995).
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. Can be blocked by external barium.
CC {ECO:0000269|PubMed:8834003}.
CC -!- SUBUNIT: May associate with GIRK1 and GIRK2 to form a G-protein-
CC activated heteromultimer pore-forming unit. The resulting inward
CC current is much larger. {ECO:0000250|UniProtKB:P48548}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:P48548}; Multi-
CC pass membrane protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the inward rectifier-type potassium channel (TC
CC 1.A.2.1) family. KCNJ5 subfamily. {ECO:0000305}.
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DR EMBL; D50133; BAA08813.1; -; mRNA.
DR RefSeq; NP_999390.1; NM_214225.1.
DR AlphaFoldDB; O02670; -.
DR SMR; O02670; -.
DR STRING; 9823.ENSSSCP00000020421; -.
DR PaxDb; O02670; -.
DR PRIDE; O02670; -.
DR Ensembl; ENSSSCT00000027719; ENSSSCP00000020421; ENSSSCG00000021573.
DR Ensembl; ENSSSCT00005000513; ENSSSCP00005000219; ENSSSCG00005000442.
DR Ensembl; ENSSSCT00030053589; ENSSSCP00030024460; ENSSSCG00030038491.
DR Ensembl; ENSSSCT00035083732; ENSSSCP00035034819; ENSSSCG00035062294.
DR Ensembl; ENSSSCT00055056639; ENSSSCP00055045281; ENSSSCG00055028556.
DR Ensembl; ENSSSCT00060081065; ENSSSCP00060035102; ENSSSCG00060059432.
DR Ensembl; ENSSSCT00065055615; ENSSSCP00065024174; ENSSSCG00065040676.
DR GeneID; 397448; -.
DR KEGG; ssc:397448; -.
DR CTD; 3762; -.
DR VGNC; VGNC:89359; KCNJ5.
DR eggNOG; KOG3827; Eukaryota.
DR GeneTree; ENSGT01040000240379; -.
DR HOGENOM; CLU_022738_11_0_1; -.
DR InParanoid; O02670; -.
DR OMA; FMNQDME; -.
DR OrthoDB; 956263at2759; -.
DR TreeFam; TF313676; -.
DR Reactome; R-SSC-1296041; Activation of G protein gated Potassium channels.
DR Reactome; R-SSC-997272; Inhibition of voltage gated Ca2+ channels via Gbeta/gamma subunits.
DR Proteomes; UP000008227; Chromosome 9.
DR Proteomes; UP000314985; Unplaced.
DR Bgee; ENSSSCG00000021573; Expressed in heart left ventricle and 19 other tissues.
DR Genevisible; O02670; SS.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0008076; C:voltage-gated potassium channel complex; IEA:Ensembl.
DR GO; GO:0015467; F:G-protein activated inward rectifier potassium channel activity; IEA:InterPro.
DR GO; GO:0005242; F:inward rectifier potassium channel activity; IBA:GO_Central.
DR GO; GO:0086089; F:voltage-gated potassium channel activity involved in atrial cardiac muscle cell action potential repolarization; IEA:Ensembl.
DR GO; GO:0098914; P:membrane repolarization during atrial cardiac muscle cell action potential; IEA:Ensembl.
DR GO; GO:1990573; P:potassium ion import across plasma membrane; IBA:GO_Central.
DR GO; GO:0086091; P:regulation of heart rate by cardiac conduction; IEA:Ensembl.
DR GO; GO:0034765; P:regulation of ion transmembrane transport; IBA:GO_Central.
DR Gene3D; 2.60.40.1400; -; 1.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR041647; IRK_C.
DR InterPro; IPR016449; K_chnl_inward-rec_Kir.
DR InterPro; IPR003277; K_chnl_inward-rec_Kir3.4.
DR InterPro; IPR013518; K_chnl_inward-rec_Kir_cyto.
DR InterPro; IPR040445; Kir_TM.
DR PANTHER; PTHR11767; PTHR11767; 1.
DR Pfam; PF01007; IRK; 1.
DR Pfam; PF17655; IRK_C; 1.
DR PIRSF; PIRSF005465; GIRK_kir; 1.
DR PRINTS; PR01330; KIR34CHANNEL.
DR PRINTS; PR01320; KIRCHANNEL.
DR SUPFAM; SSF81296; SSF81296; 1.
PE 2: Evidence at transcript level;
KW Ion channel; Ion transport; Membrane; Phosphoprotein; Potassium;
KW Potassium transport; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport; Voltage-gated channel.
FT CHAIN 1..419
FT /note="G protein-activated inward rectifier potassium
FT channel 4"
FT /id="PRO_0000154936"
FT TOPO_DOM 1..86
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 87..111
FT /note="Helical; Name=M1"
FT /evidence="ECO:0000250"
FT TOPO_DOM 112..135
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT INTRAMEM 136..147
FT /note="Helical; Pore-forming; Name=H5"
FT /evidence="ECO:0000250"
FT INTRAMEM 148..154
FT /note="Pore-forming"
FT /evidence="ECO:0000250"
FT TOPO_DOM 155..163
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 164..185
FT /note="Helical; Name=M2"
FT /evidence="ECO:0000250"
FT TOPO_DOM 186..419
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 382..419
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 149..154
FT /note="Selectivity filter"
FT /evidence="ECO:0000250"
FT COMPBIAS 405..419
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 179
FT /note="Role in the control of polyamine-mediated channel
FT gating and in the blocking by intracellular magnesium"
FT /evidence="ECO:0000250"
FT MOD_RES 5
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P48542"
SQ SEQUENCE 419 AA; 47778 MW; 8FCB123056EB10AF CRC64;
MAGDSRNAMN QDMEIGVTPR DPKKIPKQAR DYIPIATDRT RLLAEGKKPR QRYMEKSGKC
NVHHGNVQET YRYLSDLFTT LVDLKWRFNL LVFTMVYTVT WLFFGFIWWL IAYIRGDLDH
VGDQEWIPCV ENLSGFVSAF LFSIETETTI GYGFRVITEK CPEGIVLLLV QAILGSIVNA
FMVGCMFVKI SQPKKRAETL MFSNHAVISL RDEKLCLMFR VGDLRNSHIV EASIRAKLIK
SRQTKEGEFI PLNQTDINVG FDTGDDRLFL VSPLIISHEI NEKSPFWEMS RAQLNQEEFE
VVVILEGMVE ATGMTCQARS SYMDTEVLWG HRFTPVLTLE KGFYEVDYNT FHDTYETNTP
SCCAKELAEM KREGRLLQYL PSPPLPGGCA GAELEAEAEQ EGEDEPEGLR GSRETRDSV
