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 24-JAN-2024, entry version 183. 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; 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=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., Gonzalez G., RA Aguilar-Bryan L., Seino S., Bryan J.; RT "Reconstitution of IKATP: an inward rectifier subunit plus the sulfonylurea RT 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-cells, RT 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 project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- FUNCTION: This receptor is controlled by G proteins. 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. Can be blocked by extracellular barium. Can form CC cardiac and smooth muscle-type KATP channels with ABCC9. KCNJ11 forms CC the channel pore while ABCC9 is required for activation and regulation CC (By similarity). {ECO:0000250}. CC -!- SUBUNIT: Interacts with ABCC9/SUR2 (By similarity). Interacts with CC ABCC8/SUR. {ECO:0000250}. CC -!- INTERACTION: CC Q61743; Q8C8R3: Ank2; NbExp=2; IntAct=EBI-8603527, EBI-774322; CC Q61743; O94973: AP2A2; Xeno; NbExp=2; IntAct=EBI-8603527, EBI-1642835; CC Q61743; 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 that CC 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 PDB; 7W4O; EM; 2.96 A; A/C/E/G=1-390. DR PDB; 7W4P; EM; 3.19 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 PDBsum; 7W4O; -. DR PDBsum; 7W4P; -. DR AlphaFoldDB; Q61743; -. DR EMDB; EMD-32310; -. DR EMDB; EMD-32311; -. DR EMDB; EMD-3265; -. DR EMDB; EMD-6689; -. DR EMDB; EMD-6831; -. DR EMDB; EMD-6832; -. DR EMDB; EMD-6833; -. DR EMDB; EMD-6848; -. DR EMDB; EMD-6849; -. DR EMDB; EMD-6850; -. DR EMDB; EMD-6851; -. DR EMDB; EMD-6852; -. DR EMDB; EMD-9787; -. 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.ENSMUSP00000147439; -. DR DrugCentral; Q61743; -. DR GuidetoPHARMACOLOGY; 442; -. DR iPTMnet; Q61743; -. DR PhosphoSitePlus; Q61743; -. DR PaxDb; 10090-ENSMUSP00000136002; -. DR ProteomicsDB; 263589; -. DR ABCD; Q61743; 1 sequenced antibody. DR Antibodypedia; 24845; 540 antibodies from 38 providers. DR DNASU; 16514; -. DR Ensembl; ENSMUST00000211674.2; ENSMUSP00000147439.2; ENSMUSG00000096146.3. DR GeneID; 16514; -. DR KEGG; mmu:16514; -. DR UCSC; uc009gyc.2; mouse. DR AGR; MGI:107501; -. DR CTD; 3767; -. DR MGI; MGI:107501; Kcnj11. DR VEuPathDB; HostDB:ENSMUSG00000096146; -. DR eggNOG; KOG3827; Eukaryota. DR GeneTree; ENSGT00990000203615; -. DR HOGENOM; CLU_022738_4_0_1; -. DR InParanoid; Q61743; -. DR OMA; FGMVWWL; -. DR OrthoDB; 4126787at2759; -. 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 BioGRID-ORCS; 16514; 2 hits in 46 CRISPR screens. DR PRO; PR:Q61743; -. DR Proteomes; UP000000589; Chromosome 7. DR RNAct; Q61743; Protein. DR Bgee; ENSMUSG00000096146; Expressed in gastrula and 180 other cell types or tissues. DR ExpressionAtlas; Q61743; baseline and differential. DR GO; GO:0001669; C:acrosomal vesicle; ISO:MGI. DR GO; GO:0030673; C:axolemma; ISO:MGI. DR GO; GO:0070852; C:cell body fiber; ISO:MGI. DR GO; GO:0005768; C:endosome; ISO:MGI. DR GO; GO:0098978; C:glutamatergic synapse; ISO:MGI. DR GO; GO:0014704; C:intercalated disc; ISO:MGI. DR GO; GO:0008282; C:inward rectifying potassium channel; IDA:BHF-UCL. 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:0042734; C:presynaptic membrane; ISO: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:0019829; F:ATPase-coupled monoatomic cation transmembrane transporter activity; ISO:MGI. DR GO; GO:0031072; F:heat shock protein binding; ISO:MGI. DR GO; GO:0005242; F:inward rectifier potassium channel activity; IDA:MGI. DR GO; GO:0030955; F:potassium ion binding; IC:BHF-UCL. DR GO; GO:0044325; F:transmembrane transporter binding; ISO:MGI. DR GO; GO:0099508; F:voltage-gated monoatomic ion channel activity involved in regulation of presynaptic membrane potential; ISO:MGI. DR GO; GO:0005249; F:voltage-gated potassium channel activity; ISO:MGI. DR GO; GO:0001508; P:action potential; IGI:MGI. DR GO; GO:0006915; P:apoptotic process; IMP:MGI. DR GO; GO:0061762; P:CAMKK-AMPK signaling cascade; IMP: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:0008340; P:determination of adult lifespan; IGI:MGI. DR GO; GO:0006006; P:glucose metabolic process; ISO:MGI. DR GO; GO:0098662; P:inorganic cation transmembrane transport; ISO:MGI. DR GO; GO:0046676; P:negative regulation of insulin secretion; IMP:MGI. DR GO; GO:0050877; P:nervous system process; 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:0034765; P:regulation of monoatomic ion transmembrane transport; IBA:GO_Central. DR GO; GO:0033198; P:response to ATP; ISO:MGI. DR GO; GO:0032355; P:response to estradiol; IEA:Ensembl. DR GO; GO:0001666; P:response to hypoxia; IMP:MGI. DR GO; GO:0002931; P:response to ischemia; IMP:MGI. DR GO; GO:1904638; P:response to resveratrol; IMP:MGI. DR GO; GO:0033574; P:response to testosterone; IEA:Ensembl. DR GO; GO:0009410; P:response to xenobiotic stimulus; ISO:MGI. DR GO; GO:0003229; P:ventricular cardiac muscle tissue development; IGI:MGI. DR Gene3D; 1.10.287.70; -; 1. DR Gene3D; 2.60.40.1400; G protein-activated inward rectifier potassium channel 1; 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:SF44; ATP-SENSITIVE INWARD RECTIFIER POTASSIUM CHANNEL 11; 1. DR PANTHER; PTHR11767; INWARD RECTIFIER POTASSIUM CHANNEL; 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; E set domains; 1. DR SUPFAM; SSF81324; Voltage-gated potassium channels; 1. DR Genevisible; Q61743; MM. PE 1: Evidence at protein level; KW 3D-structure; Ion channel; Ion transport; Membrane; Phosphoprotein; KW Potassium; Potassium transport; Reference proteome; Transmembrane; KW Transmembrane helix; Transport; Voltage-gated channel. FT CHAIN 1..390 FT /note="ATP-sensitive inward rectifier potassium channel 11" FT /id="PRO_0000154958" FT TOPO_DOM 1..68 FT /note="Cytoplasmic" FT /evidence="ECO:0000250" FT TRANSMEM 69..93 FT /note="Helical; Name=M1" FT /evidence="ECO:0000250" FT TOPO_DOM 94..116 FT /note="Extracellular" FT /evidence="ECO:0000250" FT INTRAMEM 117..128 FT /note="Helical; Pore-forming; Name=H5" FT /evidence="ECO:0000250" FT INTRAMEM 129..135 FT /note="Pore-forming" FT /evidence="ECO:0000250" FT TOPO_DOM 136..144 FT /note="Extracellular" FT /evidence="ECO:0000250" FT TRANSMEM 145..166 FT /note="Helical; Name=M2" FT /evidence="ECO:0000250" FT TOPO_DOM 167..390 FT /note="Cytoplasmic" FT /evidence="ECO:0000250" FT MOTIF 130..135 FT /note="Selectivity filter" FT /evidence="ECO:0000250" FT SITE 160 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 341 FT /note="Phosphothreonine; by MAPK1" FT /evidence="ECO:0000250|UniProtKB:Q14654" FT MOD_RES 385 FT /note="Phosphoserine; by MAPK1" FT /evidence="ECO:0000250|UniProtKB:Q14654" FT CONFLICT 248 FT /note="G -> S (in Ref. 3; AAD02096)" FT /evidence="ECO:0000305" FT STRAND 38..40 FT /evidence="ECO:0007829|PDB:7W4P" FT STRAND 44..47 FT /evidence="ECO:0007829|PDB:7W4O" FT HELIX 53..57 FT /evidence="ECO:0007829|PDB:7W4O" FT HELIX 59..64 FT /evidence="ECO:0007829|PDB:7W4O" FT HELIX 68..96 FT /evidence="ECO:0007829|PDB:7W4O" FT TURN 97..100 FT /evidence="ECO:0007829|PDB:7W4O" FT HELIX 117..128 FT /evidence="ECO:0007829|PDB:7W4O" FT STRAND 134..136 FT /evidence="ECO:0007829|PDB:7W4O" FT HELIX 143..171 FT /evidence="ECO:0007829|PDB:7W4O" FT TURN 174..176 FT /evidence="ECO:0007829|PDB:7W4O" FT HELIX 177..180 FT /evidence="ECO:0007829|PDB:7W4O" FT STRAND 181..183 FT /evidence="ECO:0007829|PDB:7W4O" FT STRAND 185..189 FT /evidence="ECO:0007829|PDB:7W4O" FT STRAND 192..195 FT /evidence="ECO:0007829|PDB:7W4P" FT STRAND 197..199 FT /evidence="ECO:0007829|PDB:7W4O" FT STRAND 202..204 FT /evidence="ECO:0007829|PDB:7W4O" FT STRAND 206..208 FT /evidence="ECO:0007829|PDB:7W4P" FT STRAND 210..221 FT /evidence="ECO:0007829|PDB:7W4O" FT STRAND 226..228 FT /evidence="ECO:0007829|PDB:7W4O" FT STRAND 234..238 FT /evidence="ECO:0007829|PDB:7W4O" FT STRAND 243..246 FT /evidence="ECO:0007829|PDB:7W4O" FT STRAND 258..260 FT /evidence="ECO:0007829|PDB:7W4O" FT STRAND 262..265 FT /evidence="ECO:0007829|PDB:6JB1" FT HELIX 266..269 FT /evidence="ECO:0007829|PDB:7W4O" FT STRAND 276..278 FT /evidence="ECO:0007829|PDB:7W4O" FT STRAND 282..291 FT /evidence="ECO:0007829|PDB:7W4O" FT TURN 292..294 FT /evidence="ECO:0007829|PDB:7W4O" FT STRAND 297..306 FT /evidence="ECO:0007829|PDB:7W4O" FT STRAND 309..311 FT /evidence="ECO:0007829|PDB:7W4O" FT STRAND 313..315 FT /evidence="ECO:0007829|PDB:7W4O" FT STRAND 319..321 FT /evidence="ECO:0007829|PDB:7W4O" FT STRAND 323..329 FT /evidence="ECO:0007829|PDB:7W4O" FT HELIX 330..332 FT /evidence="ECO:0007829|PDB:7W4O" FT STRAND 336..338 FT /evidence="ECO:0007829|PDB:7W4O" FT HELIX 346..355 FT /evidence="ECO:0007829|PDB:7W4O" 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 //