KCNJ5_MOUSE
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 03-AUG-2022, entry version 166.
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 (TC
CC 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; P48545; -.
DR PRIDE; P48545; -.
DR ProteomicsDB; 263497; -.
DR Antibodypedia; 2997; 203 antibodies from 29 providers.
DR DNASU; 16521; -.
DR Ensembl; ENSMUST00000034533; ENSMUSP00000034533; ENSMUSG00000032034.
DR Ensembl; ENSMUST00000214223; ENSMUSP00000149000; ENSMUSG00000032034.
DR GeneID; 16521; -.
DR KEGG; mmu:16521; -.
DR UCSC; uc009orw.1; mouse.
DR CTD; 3762; -.
DR MGI; MGI:104755; Kcnj5.
DR VEuPathDB; HostDB:ENSMUSG00000032034; -.
DR eggNOG; KOG3827; Eukaryota.
DR GeneTree; ENSGT01040000240379; -.
DR HOGENOM; CLU_022738_11_0_1; -.
DR InParanoid; P48545; -.
DR OMA; FMNQDME; -.
DR OrthoDB; 956263at2759; -.
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 76 CRISPR screens.
DR PRO; PR:P48545; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; P48545; protein.
DR Bgee; ENSMUSG00000032034; Expressed in cardiac atrium and 55 other tissues.
DR ExpressionAtlas; P48545; baseline and differential.
DR Genevisible; P48545; MM.
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; ISO:MGI.
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 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_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
