GenomeNet

Database: UniProt
Entry: KCNJ2_MOUSE
LinkDB: KCNJ2_MOUSE
Original site: 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   16-OCT-2019, entry version 182.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; 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
RT   rectifier 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
RT   inward 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
RT   the 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
RT   associated 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
CC       tendency to allow potassium to flow into the cell rather than out
CC       of it. Their voltage dependence is regulated by the concentration
CC       of extracellular potassium; as external potassium is raised, the
CC       voltage range of the channel opening shifts to more positive
CC       voltages. The inward rectification is mainly due to the blockage
CC       of outward current by internal magnesium. Can be blocked by
CC       extracellular barium and cesium.
CC   -!- SUBUNIT: Homomultimeric and heteromultimeric association with
CC       KCNJ4/Kir2.3. Association, via its PDZ-recognition domain, with
CC       LIN7A, LIN7B, LIN7C, DLG1, CASK and APBA1 plays a key role in its
CC       localization and trafficking (By similarity). {ECO:0000250}.
CC   -!- INTERACTION:
CC       Self; NbExp=7; IntAct=EBI-703793, EBI-703793;
CC       P24588:AKAP5 (xeno); NbExp=2; IntAct=EBI-703793, EBI-703640;
CC       B2RYN6:Ap1g1 (xeno); NbExp=2; IntAct=EBI-703793, EBI-4319005;
CC       Q15700-4:DLG2 (xeno); NbExp=6; IntAct=EBI-703793, EBI-663057;
CC       Q2YHQ3:FLNA (xeno); NbExp=3; IntAct=EBI-703793, EBI-779542;
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC       Membrane; 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
CC       (TC 1.A.2.1) family. KCNJ2 subfamily. {ECO:0000305}.
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   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   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   eggNOG; KOG3827; Eukaryota.
DR   eggNOG; ENOG410XQ62; LUCA.
DR   GeneTree; ENSGT00960000186595; -.
DR   HOGENOM; HOG000237325; -.
DR   InParanoid; P35561; -.
DR   KO; K04996; -.
DR   OMA; KVHTRHQ; -.
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   EvolutionaryTrace; P35561; -.
DR   PRO; PR:P35561; -.
DR   Proteomes; UP000000589; Chromosome 11.
DR   Bgee; ENSMUSG00000041695; Expressed in 43 organ(s), highest expression level in bone marrow macrophage.
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: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; Complete proteome; Ion channel; Ion transport;
KW   Lipoprotein; Membrane; Myristate; Potassium; Potassium transport;
KW   Reference proteome; S-nitrosylation; Transmembrane;
KW   Transmembrane helix; Transport; Voltage-gated channel.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    428       Inward rectifier potassium channel 2.
FT                                /FTId=PRO_0000154925.
FT   TOPO_DOM      2     81       Cytoplasmic. {ECO:0000250}.
FT   TRANSMEM     82    106       Helical; Name=M1. {ECO:0000250}.
FT   TOPO_DOM    107    128       Extracellular. {ECO:0000250}.
FT   INTRAMEM    129    140       Helical; Pore-forming; Name=H5.
FT                                {ECO:0000250}.
FT   INTRAMEM    141    147       Pore-forming. {ECO:0000250}.
FT   TOPO_DOM    148    156       Extracellular. {ECO:0000250}.
FT   TRANSMEM    157    178       Helical; Name=M2. {ECO:0000250}.
FT   TOPO_DOM    179    428       Cytoplasmic. {ECO:0000250}.
FT   MOTIF       142    147       Selectivity filter. {ECO:0000250}.
FT   MOTIF       426    428       PDZ-binding. {ECO:0000255}.
FT   SITE        172    172       Role in the control of polyamine-mediated
FT                                channel gating and in the blocking by
FT                                intracellular magnesium. {ECO:0000250}.
FT   MOD_RES      76     76       S-nitrosocysteine.
FT                                {ECO:0000250|UniProtKB:P63252}.
FT   LIPID         2      2       N-myristoyl glycine.
FT                                {ECO:0000250|UniProtKB:P63252}.
FT   MUTAGEN      75     75       T->R: The mutant protein is able to
FT                                coassemble and traffic to the cell
FT                                membrane. {ECO:0000269|PubMed:16571646}.
FT   TURN        188    190       {ECO:0000244|PDB:1U4F}.
FT   STRAND      192    195       {ECO:0000244|PDB:2GIX}.
FT   STRAND      199    204       {ECO:0000244|PDB:2GIX}.
FT   STRAND      207    216       {ECO:0000244|PDB:2GIX}.
FT   STRAND      218    220       {ECO:0000244|PDB:1U4F}.
FT   STRAND      222    236       {ECO:0000244|PDB:2GIX}.
FT   STRAND      242    250       {ECO:0000244|PDB:2GIX}.
FT   TURN        254    259       {ECO:0000244|PDB:2GIX}.
FT   STRAND      267    272       {ECO:0000244|PDB:2GIX}.
FT   TURN        278    281       {ECO:0000244|PDB:2GIX}.
FT   HELIX       284    288       {ECO:0000244|PDB:2GIX}.
FT   STRAND      293    302       {ECO:0000244|PDB:2GIX}.
FT   TURN        303    305       {ECO:0000244|PDB:2GIX}.
FT   STRAND      308    316       {ECO:0000244|PDB:2GIX}.
FT   HELIX       317    319       {ECO:0000244|PDB:2GIX}.
FT   STRAND      320    322       {ECO:0000244|PDB:2GIX}.
FT   STRAND      324    326       {ECO:0000244|PDB:2GIX}.
FT   STRAND      330    332       {ECO:0000244|PDB:2GIX}.
FT   STRAND      334    340       {ECO:0000244|PDB:2GIX}.
FT   HELIX       341    343       {ECO:0000244|PDB:2GIX}.
FT   STRAND      347    349       {ECO:0000244|PDB:2GIX}.
FT   HELIX       358    369       {ECO:0000244|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
//
DBGET integrated database retrieval system