KCNJ2_MOUSE
ID KCNJ2_MOUSE Reviewed; 428 AA.
AC P35561;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 195.
DE RecName: Full=Inward rectifier potassium channel 2;
DE AltName: Full=Inward rectifier K(+) channel Kir2.1;
DE Short=IRK-1;
DE AltName: Full=Potassium channel, inwardly rectifying subfamily J member 2;
GN Name=Kcnj2; Synonyms=Irk1;
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].
RC STRAIN=BALB/cJ; TISSUE=Macrophage;
RX PubMed=7680768; DOI=10.1038/362127a0;
RA Kubo Y., Baldwin T.J., Jan Y.N., Jan L.Y.;
RT "Primary structure and functional expression of a mouse inward rectifier
RT potassium channel.";
RL Nature 362:127-132(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=8282096; DOI=10.1016/0014-5793(93)80840-q;
RA Morishige K., Takahashi N., Findlay I., Koyama H., Zanelli J.S.,
RA Peterson C., Jenkins N.A., Copeland N.G., Mori N., Kurachi Y.;
RT "Molecular cloning, functional expression and localization of an inward
RT rectifier potassium channel in the mouse brain.";
RL FEBS Lett. 336:375-380(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Lens epithelium;
RX PubMed=9533862; DOI=10.1006/exer.1997.0432;
RA Rae J.L., Shepard A.R.;
RT "Inwardly rectifying potassium channels in lens epithelium are from the
RT IRK1 (Kir 2.1) family.";
RL Exp. Eye Res. 66:347-359(1998).
RN [4]
RP MUTAGENESIS OF THR-75.
RX PubMed=16571646; DOI=10.1136/jmg.2006.040816;
RA Lu C.W., Lin J.H., Rajawat Y.S., Jerng H., Rami T.G., Sanchez X.,
RA DeFreitas G., Carabello B., DeMayo F., Kearney D.L., Miller G., Li H.,
RA Pfaffinger P.J., Bowles N.E., Khoury D.S., Towbin J.A.;
RT "Functional and clinical characterization of a mutation in KCNJ2 associated
RT with Andersen-Tawil syndrome.";
RL J. Med. Genet. 43:653-659(2006).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
CC -!- FUNCTION: Probably participates in establishing action potential
CC waveform and excitability of neuronal and muscle tissues. 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 extracellular barium and cesium.
CC -!- SUBUNIT: Homomultimeric and heteromultimeric association with
CC KCNJ4/Kir2.3. Association, via its PDZ-recognition domain, with LIN7A,
CC LIN7B, LIN7C, DLG1, CASK and APBA1 plays a key role in its localization
CC and trafficking (By similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC P35561; P35561: Kcnj2; NbExp=7; IntAct=EBI-703793, EBI-703793;
CC P35561; P24588: AKAP5; Xeno; NbExp=2; IntAct=EBI-703793, EBI-703640;
CC P35561; B2RYN6: Ap1g1; Xeno; NbExp=2; IntAct=EBI-703793, EBI-4319005;
CC P35561; Q15700-4: DLG2; Xeno; NbExp=6; IntAct=EBI-703793, EBI-663057;
CC P35561; Q2YHQ3: FLNA; Xeno; NbExp=3; IntAct=EBI-703793, EBI-779542;
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. Membrane;
CC Lipid-anchor {ECO:0000250|UniProtKB:P63252}.
CC -!- TISSUE SPECIFICITY: Prominently expressed in the central nervous
CC system. Also found in other excitable tissues such as heart and
CC skeletal muscle.
CC -!- PTM: S-nitrosylation increases the open probability and inward
CC rectifying currents. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the inward rectifier-type potassium channel (TC
CC 1.A.2.1) family. KCNJ2 subfamily. {ECO:0000305}.
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DR EMBL; X73052; CAA51526.1; -; mRNA.
DR EMBL; AF021136; AAB88794.1; -; mRNA.
DR CCDS; CCDS25594.1; -.
DR PIR; S32351; S32351.
DR RefSeq; NP_032451.1; NM_008425.4.
DR PDB; 1U4F; X-ray; 2.41 A; A/B/C/D=41-63, A/B/C/D=188-428.
DR PDB; 2GIX; X-ray; 2.02 A; A/B/C/D=44-64, A/B/C/D=189-371.
DR PDB; 2XKY; Other; 17.20 A; I/J/K/L=1-67, I/J/K/L=189-428.
DR PDBsum; 1U4F; -.
DR PDBsum; 2GIX; -.
DR PDBsum; 2XKY; -.
DR AlphaFoldDB; P35561; -.
DR SMR; P35561; -.
DR BioGRID; 200900; 2.
DR ComplexPortal; CPX-3068; Inward rectifier potassium channel 2 complex.
DR IntAct; P35561; 11.
DR MINT; P35561; -.
DR STRING; 10090.ENSMUSP00000037192; -.
DR BindingDB; P35561; -.
DR ChEMBL; CHEMBL1293290; -.
DR GuidetoPHARMACOLOGY; 430; -.
DR iPTMnet; P35561; -.
DR PhosphoSitePlus; P35561; -.
DR SwissPalm; P35561; -.
DR PaxDb; P35561; -.
DR PeptideAtlas; P35561; -.
DR PRIDE; P35561; -.
DR ProteomicsDB; 269203; -.
DR ABCD; P35561; 1 sequenced antibody.
DR Antibodypedia; 31891; 327 antibodies from 36 providers.
DR DNASU; 16518; -.
DR Ensembl; ENSMUST00000042970; ENSMUSP00000037192; ENSMUSG00000041695.
DR GeneID; 16518; -.
DR KEGG; mmu:16518; -.
DR UCSC; uc007mdw.2; mouse.
DR CTD; 3759; -.
DR MGI; MGI:104744; Kcnj2.
DR VEuPathDB; HostDB:ENSMUSG00000041695; -.
DR eggNOG; KOG3827; Eukaryota.
DR GeneTree; ENSGT01030000234586; -.
DR HOGENOM; CLU_022738_3_0_1; -.
DR InParanoid; P35561; -.
DR OMA; NISETEH; -.
DR OrthoDB; 956263at2759; -.
DR PhylomeDB; P35561; -.
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; 16518; 4 hits in 75 CRISPR screens.
DR EvolutionaryTrace; P35561; -.
DR PRO; PR:P35561; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; P35561; protein.
DR Bgee; ENSMUSG00000041695; Expressed in hindlimb stylopod muscle and 68 other tissues.
DR ExpressionAtlas; P35561; baseline and differential.
DR Genevisible; P35561; MM.
DR GO; GO:0030425; C:dendrite; ISO:MGI.
DR GO; GO:0043197; C:dendritic spine; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0014704; C:intercalated disc; ISO:MGI.
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:0005791; C:rough endoplasmic reticulum; ISO:MGI.
DR GO; GO:0005790; C:smooth endoplasmic reticulum; ISO:MGI.
DR GO; GO:0030315; C:T-tubule; ISO:MGI.
DR GO; GO:0008076; C:voltage-gated potassium channel complex; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0005242; F:inward rectifier potassium channel activity; ISS:UniProtKB.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; ISO:MGI.
DR GO; GO:0086008; F:voltage-gated potassium channel activity involved in cardiac muscle cell action potential repolarization; ISO:MGI.
DR GO; GO:0086001; P:cardiac muscle cell action potential; IMP:MGI.
DR GO; GO:0086002; P:cardiac muscle cell action potential involved in contraction; ISO:MGI.
DR GO; GO:0071260; P:cellular response to mechanical stimulus; IEA:Ensembl.
DR GO; GO:0015693; P:magnesium ion transport; IDA:MGI.
DR GO; GO:0086011; P:membrane repolarization during action potential; ISO:MGI.
DR GO; GO:0086013; P:membrane repolarization during cardiac muscle cell action potential; ISO:MGI.
DR GO; GO:1901381; P:positive regulation of potassium ion transmembrane transport; ISO:MGI.
DR GO; GO:1990573; P:potassium ion import across plasma membrane; ISO:MGI.
DR GO; GO:0071805; P:potassium ion transmembrane transport; ISO:MGI.
DR GO; GO:0006813; P:potassium ion transport; ISS:UniProtKB.
DR GO; GO:0051289; P:protein homotetramerization; ISS:UniProtKB.
DR GO; GO:0086004; P:regulation of cardiac muscle cell contraction; 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 GO; GO:0060306; P:regulation of membrane repolarization; ISO:MGI.
DR GO; GO:0014861; P:regulation of skeletal muscle contraction via regulation of action potential; ISO:MGI.
DR GO; GO:0055119; P:relaxation of cardiac muscle; ISO:MGI.
DR GO; GO:0090076; P:relaxation of skeletal muscle; ISO:MGI.
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; IPR003271; K_chnl_inward-rec_Kir2.1.
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:SF43; PTHR11767:SF43; 1.
DR Pfam; PF01007; IRK; 1.
DR Pfam; PF17655; IRK_C; 1.
DR Pfam; PF08466; IRK_N; 1.
DR PIRSF; PIRSF005465; GIRK_kir; 1.
DR PRINTS; PR01324; KIR21CHANNEL.
DR PRINTS; PR01320; KIRCHANNEL.
DR SUPFAM; SSF81296; SSF81296; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Ion channel; Ion transport; Lipoprotein; Membrane; Myristate;
KW Potassium; Potassium transport; Reference proteome; S-nitrosylation;
KW Transmembrane; Transmembrane helix; Transport; Voltage-gated channel.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..428
FT /note="Inward rectifier potassium channel 2"
FT /id="PRO_0000154925"
FT TOPO_DOM 2..81
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 82..106
FT /note="Helical; Name=M1"
FT /evidence="ECO:0000250"
FT TOPO_DOM 107..128
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT INTRAMEM 129..140
FT /note="Helical; Pore-forming; Name=H5"
FT /evidence="ECO:0000250"
FT INTRAMEM 141..147
FT /note="Pore-forming"
FT /evidence="ECO:0000250"
FT TOPO_DOM 148..156
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 157..178
FT /note="Helical; Name=M2"
FT /evidence="ECO:0000250"
FT TOPO_DOM 179..428
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT REGION 383..428
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 142..147
FT /note="Selectivity filter"
FT /evidence="ECO:0000250"
FT MOTIF 426..428
FT /note="PDZ-binding"
FT /evidence="ECO:0000255"
FT SITE 172
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 76
FT /note="S-nitrosocysteine"
FT /evidence="ECO:0000250|UniProtKB:P63252"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000250|UniProtKB:P63252"
FT MUTAGEN 75
FT /note="T->R: The mutant protein is able to coassemble and
FT traffic to the cell membrane."
FT /evidence="ECO:0000269|PubMed:16571646"
FT TURN 188..190
FT /evidence="ECO:0007829|PDB:1U4F"
FT STRAND 192..195
FT /evidence="ECO:0007829|PDB:2GIX"
FT STRAND 199..204
FT /evidence="ECO:0007829|PDB:2GIX"
FT STRAND 207..216
FT /evidence="ECO:0007829|PDB:2GIX"
FT STRAND 218..220
FT /evidence="ECO:0007829|PDB:1U4F"
FT STRAND 222..236
FT /evidence="ECO:0007829|PDB:2GIX"
FT STRAND 242..250
FT /evidence="ECO:0007829|PDB:2GIX"
FT TURN 254..259
FT /evidence="ECO:0007829|PDB:2GIX"
FT STRAND 267..272
FT /evidence="ECO:0007829|PDB:2GIX"
FT TURN 278..281
FT /evidence="ECO:0007829|PDB:2GIX"
FT HELIX 284..288
FT /evidence="ECO:0007829|PDB:2GIX"
FT STRAND 293..302
FT /evidence="ECO:0007829|PDB:2GIX"
FT TURN 303..305
FT /evidence="ECO:0007829|PDB:2GIX"
FT STRAND 308..316
FT /evidence="ECO:0007829|PDB:2GIX"
FT HELIX 317..319
FT /evidence="ECO:0007829|PDB:2GIX"
FT STRAND 320..322
FT /evidence="ECO:0007829|PDB:2GIX"
FT STRAND 324..326
FT /evidence="ECO:0007829|PDB:2GIX"
FT STRAND 330..332
FT /evidence="ECO:0007829|PDB:2GIX"
FT STRAND 334..340
FT /evidence="ECO:0007829|PDB:2GIX"
FT HELIX 341..343
FT /evidence="ECO:0007829|PDB:2GIX"
FT STRAND 347..349
FT /evidence="ECO:0007829|PDB:2GIX"
FT HELIX 358..369
FT /evidence="ECO:0007829|PDB:2GIX"
SQ SEQUENCE 428 AA; 48389 MW; 5B4219F979BBA41C CRC64;
MGSVRTNRYS IVSSEEDGMK LATMAVANGF GNGKSKVHTR QQCRSRFVKK DGHCNVQFIN
VGEKGQRYLA DIFTTCVDIR WRWMLVIFCL AFVLSWLFFG CVFWLIALLH GDLDTSKVSK
ACVSEVNSFT AAFLFSIETQ TTIGYGFRCV TDECPIAVFM VVFQSIVGCI IDAFIIGAVM
AKMAKPKKRN ETLVFSHNAV IAMRDGKLCL MWRVGNLRKS HLVEAHVRAQ LLKSRITSEG
EYIPLDQIDI NVGFDSGIDR IFLVSPITIV HEIDEDSPLY DLSKQDIDNA DFEIVVILEG
MVEATAMTTQ CRSSYLANEI LWGHRYEPVL FEEKHYYKVD YSRFHKTYEV PNTPLCSARD
LAEKKYILSN ANSFCYENEV ALTSKEEEED SENGVPESTS TDSPPGIDLH NQASVPLEPR
PLRRESEI
