KCJ12_MOUSE
ID KCJ12_MOUSE Reviewed; 427 AA.
AC P52187; Q8CCR0; Q9QYF2;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 2.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=ATP-sensitive inward rectifier potassium channel 12;
DE AltName: Full=Inward rectifier K(+) channel Kir2.2;
DE Short=IRK-2;
DE AltName: Full=Potassium channel, inwardly rectifying subfamily J member 12;
GN Name=Kcnj12; Synonyms=Irk2;
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], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC STRAIN=BALB/cJ; TISSUE=Brain;
RX PubMed=8083233; DOI=10.1016/s0021-9258(17)31649-6;
RA Takahashi N., Morishige K., Jahangir A., Yamada M., Findlay I., Koyama H.,
RA Kurachi Y.;
RT "Molecular cloning and functional expression of cDNA encoding a second
RT class of inward rectifier potassium channels in the mouse brain.";
RL J. Biol. Chem. 269:23274-23279(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Olfactory bulb;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 10-420.
RC STRAIN=C57BL/6NJcl; TISSUE=Brain;
RA Ikeda K., Kobayashi T.;
RT "Inward recifier potassium channel IRK2.";
RL Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Inward rectifying potassium channel that is activated by
CC phosphatidylinositol 4,5-bisphosphate and that probably participates in
CC controlling the resting membrane potential in electrically excitable
CC cells. Probably participates in establishing action potential waveform
CC and excitability of neuronal and muscle tissues. Inward rectifier
CC potassium channels are characterized by a greater tendency to allow
CC potassium to flow into the cell rather than out of it. Their voltage
CC 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. {ECO:0000269|PubMed:8083233}.
CC -!- SUBUNIT: Homotetramer. Forms heteromer with KCNJ4. Association, via its
CC PDZ-recognition domain, with LIN7A, LIN7B, LIN7C, DLG1, CASK and APBA1
CC plays a key role in its localization and trafficking (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:8083233}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:8083233}. Cell membrane
CC {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Highest level in cerebellum.
CC {ECO:0000269|PubMed:8083233}.
CC -!- DOMAIN: Phosphatidylinositol 4,5-bisphosphate binding to the
CC cytoplasmic side of the channel triggers a conformation change leading
CC to channel opening. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the inward rectifier-type potassium channel (TC
CC 1.A.2.1) family. KCNJ12 subfamily. {ECO:0000305}.
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DR EMBL; X80417; CAA56622.1; -; mRNA.
DR EMBL; AK032271; BAC27788.1; -; mRNA.
DR EMBL; AL646093; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC115970; AAI15971.1; -; mRNA.
DR EMBL; BC116677; AAI16678.1; -; mRNA.
DR EMBL; AB035889; BAA88471.1; -; mRNA.
DR CCDS; CCDS24805.1; -.
DR RefSeq; NP_001254522.1; NM_001267593.1.
DR RefSeq; XP_006532381.1; XM_006532318.3.
DR AlphaFoldDB; P52187; -.
DR SMR; P52187; -.
DR STRING; 10090.ENSMUSP00000086588; -.
DR iPTMnet; P52187; -.
DR PhosphoSitePlus; P52187; -.
DR EPD; P52187; -.
DR PaxDb; P52187; -.
DR PRIDE; P52187; -.
DR ProteomicsDB; 263590; -.
DR DNASU; 16515; -.
DR Ensembl; ENSMUST00000089184; ENSMUSP00000086588; ENSMUSG00000042529.
DR Ensembl; ENSMUST00000108717; ENSMUSP00000104357; ENSMUSG00000042529.
DR GeneID; 16515; -.
DR KEGG; mmu:16515; -.
DR UCSC; uc007jgy.3; mouse.
DR CTD; 3768; -.
DR MGI; MGI:108495; Kcnj12.
DR VEuPathDB; HostDB:ENSMUSG00000042529; -.
DR eggNOG; KOG3827; Eukaryota.
DR GeneTree; ENSGT01030000234586; -.
DR HOGENOM; CLU_022738_11_1_1; -.
DR InParanoid; P52187; -.
DR OMA; MHGMNGF; -.
DR TreeFam; TF313676; -.
DR Reactome; R-MMU-1296041; Activation of G protein gated Potassium channels.
DR Reactome; R-MMU-1296053; Classical Kir channels.
DR Reactome; R-MMU-5576886; Phase 4 - resting membrane potential.
DR Reactome; R-MMU-997272; Inhibition of voltage gated Ca2+ channels via Gbeta/gamma subunits.
DR BioGRID-ORCS; 16515; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Kcnj12; mouse.
DR PRO; PR:P52187; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; P52187; protein.
DR Bgee; ENSMUSG00000042529; Expressed in hindlimb stylopod muscle and 79 other tissues.
DR ExpressionAtlas; P52187; baseline and differential.
DR Genevisible; P52187; MM.
DR GO; GO:0030425; C:dendrite; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031224; C:intrinsic component of membrane; ISS:UniProtKB.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0030315; C:T-tubule; ISO:MGI.
DR GO; GO:0005242; F:inward rectifier potassium channel activity; ISS:UniProtKB.
DR GO; GO:0030165; F:PDZ domain binding; ISO:MGI.
DR GO; GO:1990573; P:potassium ion import across plasma membrane; IBA:GO_Central.
DR GO; GO:0006813; P:potassium ion transport; ISS:UniProtKB.
DR GO; GO:0051289; P:protein homotetramerization; ISS:UniProtKB.
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; IPR003272; K_chnl_inward-rec_Kir2.2.
DR InterPro; IPR013518; K_chnl_inward-rec_Kir_cyto.
DR InterPro; IPR013673; K_chnl_inward-rec_Kir_N.
DR InterPro; IPR040445; Kir_TM.
DR PANTHER; PTHR11767; PTHR11767; 1.
DR PANTHER; PTHR11767:SF14; PTHR11767:SF14; 1.
DR Pfam; PF01007; IRK; 1.
DR Pfam; PF17655; IRK_C; 1.
DR Pfam; PF08466; IRK_N; 1.
DR PRINTS; PR01325; KIR22CHANNEL.
DR PRINTS; PR01320; KIRCHANNEL.
DR SUPFAM; SSF81296; SSF81296; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Disulfide bond; Ion channel; Ion transport; Membrane;
KW Potassium; Potassium transport; Reference proteome; S-nitrosylation;
KW Transmembrane; Transmembrane helix; Transport; Voltage-gated channel.
FT CHAIN 1..427
FT /note="ATP-sensitive inward rectifier potassium channel 12"
FT /id="PRO_0000154963"
FT TOPO_DOM 1..82
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 83..107
FT /note="Helical; Name=M1"
FT /evidence="ECO:0000250"
FT TOPO_DOM 108..123
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT INTRAMEM 124..128
FT /evidence="ECO:0000250"
FT INTRAMEM 129..141
FT /note="Helical; Pore-forming; Name=H5"
FT /evidence="ECO:0000250"
FT INTRAMEM 142..151
FT /note="Pore-forming"
FT /evidence="ECO:0000250"
FT TOPO_DOM 152..156
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 157..181
FT /note="Helical; Name=M2"
FT /evidence="ECO:0000250"
FT TOPO_DOM 182..427
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT REGION 387..427
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 79..81
FT /note="Interaction with phosphatidylinositides"
FT /evidence="ECO:0000250"
FT MOTIF 143..148
FT /note="Selectivity filter"
FT /evidence="ECO:0000250"
FT MOTIF 183..190
FT /note="Interaction with phosphatidylinositides"
FT /evidence="ECO:0000250"
FT MOTIF 425..427
FT /note="PDZ-binding"
FT /evidence="ECO:0000255"
FT COMPBIAS 387..406
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 173
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 75
FT /note="S-nitrosocysteine"
FT /evidence="ECO:0000250|UniProtKB:P63252"
FT DISULFID 155
FT /note="Interchain"
FT /evidence="ECO:0000250"
FT CONFLICT 177
FT /note="I -> N (in Ref. 1; CAA56622)"
FT /evidence="ECO:0000305"
FT CONFLICT 255
FT /note="F -> L (in Ref. 5; BAA88471)"
FT /evidence="ECO:0000305"
FT CONFLICT 385
FT /note="S -> I (in Ref. 1; CAA56622)"
FT /evidence="ECO:0000305"
FT CONFLICT 393
FT /note="A -> S (in Ref. 1; CAA56622)"
FT /evidence="ECO:0000305"
FT CONFLICT 398..400
FT /note="GRS -> VRT (in Ref. 1; CAA56622)"
FT /evidence="ECO:0000305"
FT CONFLICT 418
FT /note="E -> V (in Ref. 1; CAA56622)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 427 AA; 48427 MW; 3FA101CCF8BCF6AC CRC64;
MTAASRANPY SIVSSEEDGL HLVTMSGANG FGNGKVHTRR RCRNRFVKKN GQCNIEFANM
DEKSQRYLAD MFTTCVDIRW RYMLLIFSLA FLASWLLFGI IFWVIAVAHG DLEPAEGRGR
TPCVLQVHGF MAAFLFSIET QTTIGYGLRC VTEECPVAVF MVVAQSIVGC IIDSFMIGAI
MAKMARPKKR AQTLLFSHNA VVALRDGKLC LMWRVGNLRK SHIVEAHVRA QLIKPRVTEE
GEYIPLDQID IDVGFDKGLD RIFLVSPITI LHEIDEASPL FGISRQDLET DDFEIVVILE
GMVEATAMTT QARSSYLANE ILWGHRFEPV LFEEKNQYKI DYSHFHKTYE VPSTPRCSAK
DLVENKFLLP SANSFCYENE LAFLSRDEED EVATDRDGRS PQPEHDFDRL QASSAALERP
YRRESEI
