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Database: UniProt
Entry: Q61743
LinkDB: Q61743
Original site: Q61743 
ID   KCJ11_MOUSE             Reviewed;         390 AA.
AC   Q61743; Q9QX21;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   13-NOV-2019, entry version 163.
DE   RecName: Full=ATP-sensitive inward rectifier potassium channel 11;
DE   AltName: Full=Inward rectifier K(+) channel Kir6.2;
DE   AltName: Full=Potassium channel, inwardly rectifying subfamily J member 11;
GN   Name=Kcnj11;
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=C57BL/6J; TISSUE=Pancreatic islet;
RX   PubMed=7502040; DOI=10.1126/science.270.5239.1166;
RA   Inagaki N., Gonoi T., Clement J.P. IV, Namba N., Inazawa J.,
RA   Gonzalez G., Aguilar-Bryan L., Seino S., Bryan J.;
RT   "Reconstitution of IKATP: an inward rectifier subunit plus the
RT   sulfonylurea receptor.";
RL   Science 270:1166-1170(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Pancreatic islet;
RX   PubMed=8549751; DOI=10.1016/0014-5793(95)01369-5;
RA   Sakura H., Aemmaelae C., Smith P.A., Gribble F.M., Ashcroft F.M.;
RT   "Cloning and functional expression of the cDNA encoding a novel ATP-
RT   sensitive potassium channel subunit expressed in pancreatic beta-
RT   cells, brain, heart and skeletal muscle.";
RL   FEBS Lett. 377:338-344(1995).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=129/Ola;
RA   Kooptiwut S., Shelton K.D., Magnuson M.A.;
RT   "Structural characterization of the mouse sulfonylurea receptor-1 and
RT   potassium inward rectifier 6.2 genes.";
RL   Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Brain;
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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: This receptor is controlled by G proteins. 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. Can form cardiac and smooth muscle-type KATP
CC       channels with ABCC9. KCNJ11 forms the channel pore while ABCC9 is
CC       required for activation and regulation (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with ABCC9/SUR2 (By similarity). Interacts with
CC       ABCC8/SUR. {ECO:0000250}.
CC   -!- INTERACTION:
CC       Q8C8R3:Ank2; NbExp=2; IntAct=EBI-8603527, EBI-774322;
CC       O94973:AP2A2 (xeno); NbExp=2; IntAct=EBI-8603527, EBI-1642835;
CC       G3I1T3:I79_017352 (xeno); NbExp=3; IntAct=EBI-8603527, EBI-10953250;
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC   -!- PTM: Phosphorylation by MAPK1 results in changes in channel gating
CC       that destabilize the closed states and reduce the ATP sensitivity.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the inward rectifier-type potassium channel
CC       (TC 1.A.2.1) family. KCNJ11 subfamily. {ECO:0000305}.
DR   EMBL; D50581; BAA09130.1; -; mRNA.
DR   EMBL; U73626; AAB17355.1; -; mRNA.
DR   EMBL; AF037313; AAD02096.1; -; Genomic_DNA.
DR   EMBL; BC052731; AAH52731.1; -; mRNA.
DR   EMBL; BC057006; AAH57006.1; -; mRNA.
DR   CCDS; CCDS21274.1; -.
DR   PIR; S68403; S68403.
DR   RefSeq; NP_034732.1; NM_010602.3.
DR   PDB; 5WUA; EM; 5.60 A; A/B/C/D=1-390.
DR   PDB; 5YKE; EM; 4.11 A; A/C/E/G=1-390.
DR   PDB; 5YKF; EM; 4.33 A; A/C/E/G=1-390.
DR   PDB; 5YKG; EM; 4.57 A; A/C/E/G=1-390.
DR   PDB; 5YW8; EM; 4.40 A; A/C/E/G=1-390.
DR   PDB; 5YW9; EM; 5.00 A; A/C/E/G=1-390.
DR   PDB; 5YWA; EM; 6.10 A; A/C/E/G=1-390.
DR   PDB; 5YWB; EM; 5.20 A; A/C/E/G=1-390.
DR   PDB; 5YWC; EM; 4.30 A; A/C/E/G=1-390.
DR   PDB; 6JB1; EM; 3.30 A; A/C/E/G=1-390.
DR   PDBsum; 5WUA; -.
DR   PDBsum; 5YKE; -.
DR   PDBsum; 5YKF; -.
DR   PDBsum; 5YKG; -.
DR   PDBsum; 5YW8; -.
DR   PDBsum; 5YW9; -.
DR   PDBsum; 5YWA; -.
DR   PDBsum; 5YWB; -.
DR   PDBsum; 5YWC; -.
DR   PDBsum; 6JB1; -.
DR   SMR; Q61743; -.
DR   BioGrid; 200896; 1.
DR   ComplexPortal; CPX-194; Inward rectifying potassium channel complex, Kir6.2-SUR1.
DR   ComplexPortal; CPX-196; Inward rectifying potassium channel complex, Kir6.2-SUR2A.
DR   ComplexPortal; CPX-198; Inward rectifying potassium channel complex, Kir6.2-SUR2B.
DR   CORUM; Q61743; -.
DR   DIP; DIP-42790N; -.
DR   IntAct; Q61743; 5.
DR   MINT; Q61743; -.
DR   STRING; 10090.ENSMUSP00000136002; -.
DR   DrugCentral; Q61743; -.
DR   GuidetoPHARMACOLOGY; 442; -.
DR   iPTMnet; Q61743; -.
DR   PhosphoSitePlus; Q61743; -.
DR   PaxDb; Q61743; -.
DR   PRIDE; Q61743; -.
DR   Ensembl; ENSMUST00000211674; ENSMUSP00000147439; ENSMUSG00000096146.
DR   GeneID; 16514; -.
DR   KEGG; mmu:16514; -.
DR   UCSC; uc009gyc.2; mouse.
DR   CTD; 3767; -.
DR   MGI; MGI:107501; Kcnj11.
DR   eggNOG; KOG3827; Eukaryota.
DR   eggNOG; ENOG410XQ62; LUCA.
DR   GeneTree; ENSGT00970000193347; -.
DR   HOGENOM; HOG000237325; -.
DR   InParanoid; Q61743; -.
DR   KO; K05004; -.
DR   OMA; GMYAVDY; -.
DR   OrthoDB; 956263at2759; -.
DR   PhylomeDB; Q61743; -.
DR   TreeFam; TF313676; -.
DR   Reactome; R-MMU-1296025; ATP sensitive Potassium channels.
DR   Reactome; R-MMU-382556; ABC-family proteins mediated transport.
DR   Reactome; R-MMU-422356; Regulation of insulin secretion.
DR   Reactome; R-MMU-5578775; Ion homeostasis.
DR   PRO; PR:Q61743; -.
DR   Proteomes; UP000000589; Chromosome 7.
DR   Bgee; ENSMUSG00000096146; Expressed in 206 organ(s), highest expression level in thymus.
DR   ExpressionAtlas; Q61743; baseline and differential.
DR   Genevisible; Q61743; MM.
DR   GO; GO:0001669; C:acrosomal vesicle; ISO:MGI.
DR   GO; GO:0030673; C:axolemma; ISO:MGI.
DR   GO; GO:0005623; C:cell; IEA:GOC.
DR   GO; GO:0070852; C:cell body fiber; ISO:MGI.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR   GO; GO:0005768; C:endosome; ISO:MGI.
DR   GO; GO:0014704; C:intercalated disc; ISO:MGI.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR   GO; GO:0008282; C:inward rectifying potassium channel; IDA:BHF-UCL.
DR   GO; GO:0005739; C:mitochondrion; ISO:MGI.
DR   GO; GO:0043209; C:myelin sheath; ISO:MGI.
DR   GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR   GO; GO:0005635; C:nuclear envelope; ISO:MGI.
DR   GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR   GO; GO:0042383; C:sarcolemma; ISO:MGI.
DR   GO; GO:0030315; C:T-tubule; IDA:BHF-UCL.
DR   GO; GO:0030506; F:ankyrin binding; IPI:BHF-UCL.
DR   GO; GO:0005524; F:ATP binding; IDA:BHF-UCL.
DR   GO; GO:0015272; F:ATP-activated inward rectifier potassium channel activity; IDA:BHF-UCL.
DR   GO; GO:0031072; F:heat shock protein binding; ISO:MGI.
DR   GO; GO:0005242; F:inward rectifier potassium channel activity; IBA:GO_Central.
DR   GO; GO:0044325; F:ion channel binding; ISO:MGI.
DR   GO; GO:0030955; F:potassium ion binding; IC:BHF-UCL.
DR   GO; GO:0008022; F:protein C-terminus binding; ISO:MGI.
DR   GO; GO:0005249; F:voltage-gated potassium channel activity; ISO:MGI.
DR   GO; GO:0071333; P:cellular response to glucose stimulus; IEA:Ensembl.
DR   GO; GO:0071316; P:cellular response to nicotine; IEA:Ensembl.
DR   GO; GO:0071356; P:cellular response to tumor necrosis factor; IEA:Ensembl.
DR   GO; GO:0006006; P:glucose metabolic process; ISO:MGI.
DR   GO; GO:0046676; P:negative regulation of insulin secretion; ISO:MGI.
DR   GO; GO:0050877; P:nervous system process; ISO:MGI.
DR   GO; GO:2001259; P:positive regulation of cation channel activity; ISO:MGI.
DR   GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; ISO:MGI.
DR   GO; GO:1990573; P:potassium ion import across plasma membrane; IDA:BHF-UCL.
DR   GO; GO:0071805; P:potassium ion transmembrane transport; ISO:MGI.
DR   GO; GO:0006813; P:potassium ion transport; ISO:MGI.
DR   GO; GO:0050796; P:regulation of insulin secretion; ISO:MGI.
DR   GO; GO:0042391; P:regulation of membrane potential; ISO:MGI.
DR   GO; GO:0033198; P:response to ATP; ISO:MGI.
DR   GO; GO:0042493; P:response to drug; ISO:MGI.
DR   GO; GO:0032355; P:response to estradiol; IEA:Ensembl.
DR   GO; GO:0002931; P:response to ischemia; IEA:Ensembl.
DR   GO; GO:0033574; P:response to testosterone; IEA:Ensembl.
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; IPR003279; K_chnl_inward-rec_Kir6.2.
DR   InterPro; IPR013518; K_chnl_inward-rec_Kir_cyto.
DR   InterPro; IPR040445; Kir_TM.
DR   PANTHER; PTHR11767; PTHR11767; 1.
DR   PANTHER; PTHR11767:SF44; PTHR11767:SF44; 1.
DR   Pfam; PF01007; IRK; 1.
DR   Pfam; PF17655; IRK_C; 1.
DR   PIRSF; PIRSF005465; GIRK_kir; 1.
DR   PRINTS; PR01332; KIR62CHANNEL.
DR   PRINTS; PR01320; KIRCHANNEL.
DR   SUPFAM; SSF81296; SSF81296; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Complete proteome; Ion channel; Ion transport; Membrane;
KW   Phosphoprotein; Potassium; Potassium transport; Reference proteome;
KW   Transmembrane; Transmembrane helix; Transport; Voltage-gated channel.
FT   CHAIN         1    390       ATP-sensitive inward rectifier potassium
FT                                channel 11.
FT                                /FTId=PRO_0000154958.
FT   TOPO_DOM      1     68       Cytoplasmic. {ECO:0000250}.
FT   TRANSMEM     69     93       Helical; Name=M1. {ECO:0000250}.
FT   TOPO_DOM     94    116       Extracellular. {ECO:0000250}.
FT   INTRAMEM    117    128       Helical; Pore-forming; Name=H5.
FT                                {ECO:0000250}.
FT   INTRAMEM    129    135       Pore-forming. {ECO:0000250}.
FT   TOPO_DOM    136    144       Extracellular. {ECO:0000250}.
FT   TRANSMEM    145    166       Helical; Name=M2. {ECO:0000250}.
FT   TOPO_DOM    167    390       Cytoplasmic. {ECO:0000250}.
FT   MOTIF       130    135       Selectivity filter. {ECO:0000250}.
FT   SITE        160    160       Role in the control of polyamine-mediated
FT                                channel gating and in the blocking by
FT                                intracellular magnesium. {ECO:0000250}.
FT   MOD_RES     341    341       Phosphothreonine; by MAPK1.
FT                                {ECO:0000250|UniProtKB:Q14654}.
FT   MOD_RES     385    385       Phosphoserine; by MAPK1.
FT                                {ECO:0000250|UniProtKB:Q14654}.
FT   CONFLICT    248    248       G -> S (in Ref. 3; AAD02096).
FT                                {ECO:0000305}.
FT   STRAND       44     47       {ECO:0000244|PDB:6JB1}.
FT   HELIX        54     57       {ECO:0000244|PDB:6JB1}.
FT   HELIX        59     65       {ECO:0000244|PDB:6JB1}.
FT   HELIX        68     96       {ECO:0000244|PDB:6JB1}.
FT   STRAND      100    102       {ECO:0000244|PDB:6JB1}.
FT   HELIX       117    128       {ECO:0000244|PDB:6JB1}.
FT   STRAND      134    136       {ECO:0000244|PDB:6JB1}.
FT   HELIX       143    171       {ECO:0000244|PDB:6JB1}.
FT   TURN        175    179       {ECO:0000244|PDB:6JB1}.
FT   STRAND      180    183       {ECO:0000244|PDB:6JB1}.
FT   STRAND      188    192       {ECO:0000244|PDB:6JB1}.
FT   STRAND      195    204       {ECO:0000244|PDB:6JB1}.
FT   STRAND      206    208       {ECO:0000244|PDB:6JB1}.
FT   STRAND      211    220       {ECO:0000244|PDB:6JB1}.
FT   STRAND      235    238       {ECO:0000244|PDB:6JB1}.
FT   STRAND      243    247       {ECO:0000244|PDB:6JB1}.
FT   STRAND      255    260       {ECO:0000244|PDB:6JB1}.
FT   STRAND      262    265       {ECO:0000244|PDB:6JB1}.
FT   TURN        266    269       {ECO:0000244|PDB:6JB1}.
FT   STRAND      282    290       {ECO:0000244|PDB:6JB1}.
FT   TURN        292    294       {ECO:0000244|PDB:6JB1}.
FT   STRAND      297    305       {ECO:0000244|PDB:6JB1}.
FT   TURN        306    308       {ECO:0000244|PDB:6JB1}.
FT   STRAND      309    314       {ECO:0000244|PDB:6JB1}.
FT   STRAND      319    321       {ECO:0000244|PDB:6JB1}.
FT   STRAND      323    329       {ECO:0000244|PDB:6JB1}.
FT   HELIX       330    332       {ECO:0000244|PDB:6JB1}.
FT   HELIX       346    357       {ECO:0000244|PDB:6JB1}.
SQ   SEQUENCE   390 AA;  43562 MW;  6AFBFFD284C92C3A CRC64;
     MLSRKGIIPE EYVLTRLAED PAEPRYRTRE RRARFVSKKG NCNVAHKNIR EQGRFLQDVF
     TTLVDLKWPH TLLIFTMSFL CSWLLFAMVW WLIAFAHGDL APGEGTNVPC VTSIHSFSSA
     FLFSIEVQVT IGFGGRMVTE ECPLAILILI VQNIVGLMIN AIMLGCIFMK TAQAHRRAET
     LIFSKHAVIT LRHGRLCFML RVGDLRKSMI ISATIHMQVV RKTTSPEGEV VPLHQVDIPM
     ENGVGGNGIF LVAPLIIYHV IDSNSPLYDL APSDLHHHQD LEIIVILEGV VETTGITTQA
     RTSYLADEIL WGQRFVPIVA EEDGRYSVDY SKFGNTIKVP TPLCTARQLD EDRSLLDALT
     LASSRGPLRK RSVAVAKAKP KFSISPDSLS
//
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