ID KCNJ5_RAT Reviewed; 419 AA. AC P48548; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 2. DT 24-JAN-2024, entry version 162. 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; Synonyms=Girk4; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=Sprague-Dawley; TISSUE=Heart; RX PubMed=8047164; DOI=10.1038/370456a0; RA Ashford M.L.J., Bond C.T., Blair T.A., Adelman J.P.; RT "Cloning and functional expression of a rat heart KATP channel."; RL Nature 370:456-459(1994). RN [2] RP ERRATUM OF PUBMED:8047164. RX PubMed=8524415; DOI=10.1038/378792a0; RA Ashford M.L.J., Bond C.T., Blair T.A., Adelman J.P.; RL Nature 378:792-792(1995). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 31-39 AND 333-341, RP FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, AND TISSUE SPECIFICITY. RC STRAIN=Sprague-Dawley; TISSUE=Neonatal heart atrium; RX PubMed=7877685; DOI=10.1038/374135a0; RA Krapivinsky G.B., Gordon E.A., Wickman K., Velimirovic B., RA Krapivinsky L.D., Clapham D.E.; RT "The G-protein-gated atrial K+ channel IKACh is a heteromultimer of two RT inwardly rectifying K(+)-channel proteins."; RL Nature 374:135-141(1995). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBUNIT. RC TISSUE=Pancreatic islet; RX PubMed=7592809; DOI=10.1074/jbc.270.44.26086; RA Ferrer J., Nichols C.G., Makhina E.N., Salkoff L., Bernstein J., RA Gerhard D., Wasson J., Ramanadham S., Permutt A.; RT "Pancreatic islet cells express a family of inwardly rectifying K+ channel RT subunits which interact to form G-protein-activated channels."; RL J. Biol. Chem. 270:26086-26091(1995). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY. RC STRAIN=Sprague-Dawley; 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). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Heart; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). 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:7592809, ECO:0000269|PubMed:7877685, CC ECO:0000269|PubMed:8834003}. CC -!- SUBUNIT: Associates with GIRK1 or GIRK2 to form a G-protein-activated CC heteromultimer pore-forming unit. The resulting inward current is much CC larger. {ECO:0000269|PubMed:7592809, ECO:0000269|PubMed:7877685}. CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:7877685}; Multi-pass CC membrane protein {ECO:0000255}. CC -!- TISSUE SPECIFICITY: Most abundant in heart tissue where it is found CC predominantly in atria. Also found in brain, kidney, liver, spleen, CC lung and thymus. {ECO:0000269|PubMed:7877685, CC ECO:0000269|PubMed:8834003}. CC -!- SIMILARITY: Belongs to the inward rectifier-type potassium channel CC (TC 1.A.2.1) family. KCNJ5 subfamily. {ECO:0000305}. 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 EMBL; X83584; CAA58567.1; -; mRNA. DR EMBL; L35771; AAC42048.1; -; mRNA. DR EMBL; D50135; BAA08815.1; -; mRNA. DR EMBL; BC087022; AAH87022.1; -; mRNA. DR PIR; S48077; S48077. DR RefSeq; NP_058993.1; NM_017297.2. DR AlphaFoldDB; P48548; -. DR SMR; P48548; -. DR ComplexPortal; CPX-3276; I(KACh) inward rectifier potassium channel complex. DR STRING; 10116.ENSRNOP00000048134; -. DR ChEMBL; CHEMBL3714708; -. DR GuidetoPHARMACOLOGY; 437; -. DR iPTMnet; P48548; -. DR PhosphoSitePlus; P48548; -. DR PaxDb; 10116-ENSRNOP00000048134; -. DR DNASU; 29713; -. DR Ensembl; ENSRNOT00000041038.6; ENSRNOP00000048134.5; ENSRNOG00000033796.6. DR Ensembl; ENSRNOT00055015036; ENSRNOP00055012003; ENSRNOG00055008907. DR Ensembl; ENSRNOT00060019915; ENSRNOP00060015645; ENSRNOG00060011773. DR GeneID; 29713; -. DR KEGG; rno:29713; -. DR UCSC; RGD:61971; rat. DR AGR; RGD:61971; -. DR CTD; 3762; -. DR RGD; 61971; Kcnj5. DR eggNOG; KOG3827; Eukaryota. DR GeneTree; ENSGT01080000257365; -. DR HOGENOM; CLU_022738_11_0_1; -. DR InParanoid; P48548; -. DR OrthoDB; 4126787at2759; -. DR PhylomeDB; P48548; -. DR Reactome; R-RNO-1296041; Activation of G protein gated Potassium channels. DR Reactome; R-RNO-997272; Inhibition of voltage gated Ca2+ channels via Gbeta/gamma subunits. DR PRO; PR:P48548; -. DR Proteomes; UP000002494; Chromosome 8. DR Bgee; ENSRNOG00000033796; Expressed in heart and 12 other cell types or tissues. DR GO; GO:0009897; C:external side of plasma membrane; IDA:RGD. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. DR GO; GO:0030315; C:T-tubule; IDA:RGD. DR GO; GO:0008076; C:voltage-gated potassium channel complex; ISO:RGD. 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; ISO:RGD. DR GO; GO:0098914; P:membrane repolarization during atrial cardiac muscle cell action potential; ISO:RGD. DR GO; GO:1990573; P:potassium ion import across plasma membrane; ISO:RGD. DR GO; GO:0086091; P:regulation of heart rate by cardiac conduction; ISO:RGD. DR GO; GO:0034765; P:regulation of monoatomic ion transmembrane transport; IBA:GO_Central. 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; IPR003277; K_chnl_inward-rec_Kir3.4. 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 PIRSF; PIRSF005465; GIRK_kir; 1. DR PRINTS; PR01330; KIR34CHANNEL. DR PRINTS; PR01320; KIRCHANNEL. DR SUPFAM; SSF81296; E set domains; 1. DR SUPFAM; SSF81324; Voltage-gated potassium channels; 1. DR Genevisible; P48548; RN. PE 1: Evidence at protein level; KW Direct protein sequencing; Ion channel; Ion transport; Membrane; KW Phosphoprotein; Potassium; Potassium transport; Reference proteome; KW Transmembrane; Transmembrane helix; Transport; Voltage-gated channel. FT CHAIN 1..419 FT /note="G protein-activated inward rectifier potassium FT channel 4" FT /id="PRO_0000154937" 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 380..419 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 149..154 FT /note="Selectivity filter" FT /evidence="ECO:0000250" 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" FT CONFLICT 188 FT /note="V -> I (in Ref. 1; CAA58567)" FT /evidence="ECO:0000305" FT CONFLICT 375 FT /note="Q -> E (in Ref. 1; CAA58567)" FT /evidence="ECO:0000305" SQ SEQUENCE 419 AA; 47783 MW; DFF537CD79A7370D CRC64; MAGDSRNAMN QDMEIGVTSQ DHKKIPKQAR DYIPIATDRT RLLPEGKKPR QRYMEKTGKC NVHHGNVQET YRYLSDLFTT LVDLKWRFNL LVFTMVYTIT WLFFGFIWWL IAYVRGDLDH VGDQEWIPCV ENLSGFVSAF LFSIETETTI GYGFRVITEK CPEGIILLLV QAILGSIVNA FMVGCMFVKI SQPKKRAETL MFSNNAVISM RDEKLCLMFR VGDLRNSHIV EASIRAKLIK SRQTKEGEFI PLNQTDINVG FDTGDDRLFL VSPLIISHEI NEKSPFWEMS RAQLEQEEFE VVVILEGMVE ATGMTCQARS SYMDTEVLWG HRFTPVLTLE KGFYEVDYNT FHDTYETNTP SCCAKELAEM KRNGQLLQSL PSPPLLGGCA EAEKEAEAEH DEEEEPNGLS VSRATRGSM //