ID   KCNJ5_MOUSE             Reviewed;         419 AA.
AC   P48545; P97508; Q3TPX9;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 3.
DT   27-MAR-2024, entry version 175.
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   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC   TISSUE=Heart;
RX   PubMed=7499385; DOI=10.1074/jbc.270.48.28660;
RA   Lesage F., Guillemare E., Fink M., Duprat F., Heurteaux C., Fosset M.,
RA   Romey G., Barhanin J., Lazdunski M.;
RT   "Molecular properties of neuronal G-protein-activated inwardly rectifying
RT   K+ channels.";
RL   J. Biol. Chem. 270:28660-28667(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=129/SvJ;
RA   Wickman K.D., James M.R., Seldin M.F., Gendler S.J., Clapham D.E.;
RL   Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Embryo;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
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:7499385}.
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:P48544}; Multi-
CC       pass membrane protein {ECO:0000255}.
CC   -!- TISSUE SPECIFICITY: Predominantly atrial and pancreatic expression.
CC   -!- SIMILARITY: Belongs to the inward rectifier-type potassium channel
CC       (TC 1.A.2.1) family. KCNJ5 subfamily. {ECO:0000305}.
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DR   EMBL; U33631; AAB01687.1; -; mRNA.
DR   EMBL; AF403131; AAC53116.1; -; Genomic_DNA.
DR   EMBL; AK164058; BAE37606.1; -; mRNA.
DR   EMBL; CH466522; EDL25354.1; -; Genomic_DNA.
DR   CCDS; CCDS22952.1; -.
DR   RefSeq; NP_034735.3; NM_010605.4.
DR   RefSeq; XP_006510102.1; XM_006510039.3.
DR   RefSeq; XP_017168644.1; XM_017313155.1.
DR   AlphaFoldDB; P48545; -.
DR   SMR; P48545; -.
DR   BioGRID; 200903; 2.
DR   ComplexPortal; CPX-3277; I(KACh) inward rectifier potassium channel complex.
DR   STRING; 10090.ENSMUSP00000034533; -.
DR   DrugCentral; P48545; -.
DR   GuidetoPHARMACOLOGY; 437; -.
DR   iPTMnet; P48545; -.
DR   PhosphoSitePlus; P48545; -.
DR   MaxQB; P48545; -.
DR   PaxDb; 10090-ENSMUSP00000034533; -.
DR   ProteomicsDB; 263497; -.
DR   Antibodypedia; 2997; 238 antibodies from 29 providers.
DR   DNASU; 16521; -.
DR   Ensembl; ENSMUST00000034533.7; ENSMUSP00000034533.6; ENSMUSG00000032034.7.
DR   Ensembl; ENSMUST00000214223.2; ENSMUSP00000149000.2; ENSMUSG00000032034.7.
DR   GeneID; 16521; -.
DR   KEGG; mmu:16521; -.
DR   UCSC; uc009orw.1; mouse.
DR   AGR; MGI:104755; -.
DR   CTD; 3762; -.
DR   MGI; MGI:104755; Kcnj5.
DR   VEuPathDB; HostDB:ENSMUSG00000032034; -.
DR   eggNOG; KOG3827; Eukaryota.
DR   GeneTree; ENSGT01080000257365; -.
DR   HOGENOM; CLU_022738_11_0_1; -.
DR   InParanoid; P48545; -.
DR   OMA; RMDDGHE; -.
DR   OrthoDB; 4126787at2759; -.
DR   PhylomeDB; P48545; -.
DR   TreeFam; TF313676; -.
DR   Reactome; R-MMU-1296041; Activation of G protein gated Potassium channels.
DR   Reactome; R-MMU-997272; Inhibition of voltage gated Ca2+ channels via Gbeta/gamma subunits.
DR   BioGRID-ORCS; 16521; 1 hit in 81 CRISPR screens.
DR   PRO; PR:P48545; -.
DR   Proteomes; UP000000589; Chromosome 9.
DR   RNAct; P48545; Protein.
DR   Bgee; ENSMUSG00000032034; Expressed in cardiac atrium and 58 other cell types or tissues.
DR   ExpressionAtlas; P48545; baseline and differential.
DR   GO; GO:0009897; C:external side of plasma membrane; ISO:MGI.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0030315; C:T-tubule; ISO:MGI.
DR   GO; GO:0008076; C:voltage-gated potassium channel complex; ISO:MGI.
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:MGI.
DR   GO; GO:0098914; P:membrane repolarization during atrial cardiac muscle cell action potential; ISO:MGI.
DR   GO; GO:1990573; P:potassium ion import across plasma membrane; ISO:MGI.
DR   GO; GO:0086091; P:regulation of heart rate by cardiac conduction; ISO:MGI.
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; P48545; MM.
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_0000154935"
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          388..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        102
FT                   /note="L -> V (in Ref. 1; AAB01687)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        109
FT                   /note="W -> G (in Ref. 1; AAB01687)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        172
FT                   /note="A -> P (in Ref. 2; AAC53116)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        193
FT                   /note="P -> S (in Ref. 1; AAB01687)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        214
FT                   /note="K -> N (in Ref. 2; AAC53116)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        232
FT                   /note="A -> V (in Ref. 1; AAB01687)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        269
FT                   /note="F -> L (in Ref. 1; AAB01687)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        287
FT                   /note="W -> V (in Ref. 1; AAB01687)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        296
FT                   /note="Q -> P (in Ref. 2; AAC53116)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        351
FT                   /note="F -> S (in Ref. 2; AAC53116)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   419 AA;  47669 MW;  8383373921C7356A CRC64;
     MAGDSRNAMN QDMEIGVTSQ DHKKIPKQAR DYIPIATDRT RLLTEGKKPR 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 KRSGRLLQYL PSPPLLGGCA EAGNEAEAEK DEEGEPNGLS VSQATRGSM
//