ATP-sensitive inward rectifier potassium channel 11

Details

Name
ATP-sensitive inward rectifier potassium channel 11
Synonyms
  • IKATP
  • Inward rectifier K(+) channel Kir6.2
  • Potassium channel, inwardly rectifying subfamily J member 11
Gene Name
KCNJ11
Organism
Humans
Amino acid sequence
>lcl|BSEQ0001412|ATP-sensitive inward rectifier potassium channel 11
MLSRKGIIPEEYVLTRLAEDPAEPRYRARQRRARFVSKKGNCNVAHKNIREQGRFLQDVF
TTLVDLKWPHTLLIFTMSFLCSWLLFAMAWWLIAFAHGDLAPSEGTAEPCVTSIHSFSSA
FLFSIEVQVTIGFGGRMVTEECPLAILILIVQNIVGLMINAIMLGCIFMKTAQAHRRAET
LIFSKHAVIALRHGRLCFMLRVGDLRKSMIISATIHMQVVRKTTSPEGEVVPLHQVDIPM
ENGVGGNSIFLVAPLIIYHVIDANSPLYDLAPSDLHHHQDLEIIVILEGVVETTGITTQA
RTSYLADEILWGQRFVPIVAEEDGRYSVDYSKFGNTIKVPTPLCTARQLDEDHSLLEALT
LASARGPLRKRSVPMAKAKPKFSISPDSLS
Number of residues
390
Molecular Weight
43540.375
Theoretical pI
8.1
GO Classification
Functions
ankyrin binding / ATP binding / ATP-activated inward rectifier potassium channel activity / ion channel binding / potassium ion binding / voltage-gated potassium channel activity
Processes
cellular response to glucose stimulus / cellular response to nicotine / cellular response to tumor necrosis factor / energy reserve metabolic process / glucose metabolic process / negative regulation of insulin secretion / neurological system process / positive regulation of cation channel activity / potassium ion import / potassium ion transmembrane transport / regulation of insulin secretion / regulation of ion transmembrane transport / regulation of membrane potential / response to ATP / response to drug / response to estradiol / response to ischemia / response to testosterone / small molecule metabolic process / synaptic transmission / transmembrane transport
Components
ATP-sensitive potassium channel complex / axolemma / cell body fiber / cytosol / endoplasmic reticulum / endosome / integral component of plasma membrane / intercalated disc / mitochondrion / myelin sheath / neuronal cell body / nuclear envelope / plasma membrane / T-tubule / voltage-gated potassium channel complex
General Function
Voltage-gated potassium channel activity
Specific Function
This receptor is controlled by G proteins. Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. Their voltage dependence is regulated by the concentration of extracellular potassium; as external potassium is raised, the voltage range of the channel opening shifts to more positive voltages. The inward rectification is mainly due to the blockage of outward current by internal magnesium. Can be blocked by extracellular barium (By similarity). Subunit of ATP-sensitive potassium channels (KATP). Can form cardiac and smooth muscle-type KATP channels with ABCC9. KCNJ11 forms the channel pore while ABCC9 is required for activation and regulation.
Pfam Domain Function
Transmembrane Regions
69-93 145-166
Cellular Location
Membrane
Gene sequence
>lcl|BSEQ0001411|1173 bp
ATGCTGTCCCGCAAGGGCATCATCCCCGAGGAATACGTGCTGACACGCCTGGCAGAGGAC
CCTGCCGAGCCCAGGTACCGTGCCCGCCAGCGGAGGGCCCGCTTTGTGTCCAAGAAAGGC
AACTGCAACGTGGCCCACAAGAACATCCGGGAGCAGGGCCGCTTCCTGCAGGACGTGTTC
ACCACGCTGGTGGACCTCAAGTGGCCACACACATTGCTCATCTTCACCATGTCCTTCCTG
TGCAGCTGGCTGCTCTTCGCCATGGCCTGGTGGCTCATCGCCTTCGCCCACGGTGACCTG
GCCCCCAGCGAGGGCACTGCTGAGCCCTGTGTCACCAGCATCCACTCCTTCTCGTCTGCC
TTCCTTTTCTCCATTGAGGTCCAAGTGACTATTGGCTTTGGGGGGCGCATGGTGACTGAG
GAGTGCCCACTGGCCATCCTGAGCCTCATCGTGCAGAACATCGTGGGGCTCATGATCAAC
GCCATCATGCTTGGCTGCATCTTCATGAAGACTGCCCAAGCCCACCGCAGGGCTGAGACC
CTCATCTTCAGCAAGCATGCGGTGATCGCTCTGCGCCACGGCCGCCTCTGCTTCATGCTA
CGTGTGGGTGACCTCCGCAAGAGCATGATCATCAGCGCCACCATCCACATGCAGGTGGTA
CGCAAGACCACCAGCCCCGAGGGCGAGGTGGTGCCCCTCCACCAGGTGGACATCCCCATG
GAGAACGGCGTGGGTGGCAACAGCATCTTCCTGGTGGCCCCGCTGATCATCTACCATGTC
ATTGATGCCAACAGCCCACTCTACGACCTGGCACCCAGCGACCTGCACCACCACCAGGAC
CTCGAGATCATCGTCATCCTGGAAGGCGTGGTGGAAACCACGGGCATCACCACCCAGGCC
CGCACCTCCTACCTGGCCGATGAGATCCTGTGGGGCCAGCGCTTTGTGCCCATTGTAGCT
GAGGAGGACGGACGTTACTCTGTGGACTACTCCAAGTTTGGCAACACCATCAAAGTGCCC
ACACCACTCTGCACGGCCCGCCAGCTTGATGAGGACCACAGCCTACTGGAAGCTCTGACC
CTCGCCTCAGCCCGCGGGCCCCTGCGCAAGCGCAGCGTGCCCATGGCCAAGGCCAAGCCC
AAGTTCAGCATCTCTCCAGATTCCCTGTCCTGA
Chromosome Location
Not Available
Locus
11p15.1
External Identifiers
ResourceLink
UniProtKB IDQ14654
UniProtKB Entry NameKCJ11_HUMAN
GenBank Protein ID1088445
GenBank Gene IDD50582
GenAtlas IDKCNJ11
HGNC IDHGNC:6257
General References
  1. Inagaki N, Gonoi T, Clement JP 4th, Namba N, Inazawa J, Gonzalez G, Aguilar-Bryan L, Seino S, Bryan J: Reconstitution of IKATP: an inward rectifier subunit plus the sulfonylurea receptor. Science. 1995 Nov 17;270(5239):1166-70. [PubMed:7502040]
  2. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed:14702039]
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  5. Babenko AP, Gonzalez G, Aguilar-Bryan L, Bryan J: Reconstituted human cardiac KATP channels: functional identity with the native channels from the sarcolemma of human ventricular cells. Circ Res. 1998 Nov 30;83(11):1132-43. [PubMed:9831708]
  6. Ribalet B, John SA, Weiss JN: Molecular basis for Kir6.2 channel inhibition by adenine nucleotides. Biophys J. 2003 Jan;84(1):266-76. [PubMed:12524280]
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  8. Pinney SE, MacMullen C, Becker S, Lin YW, Hanna C, Thornton P, Ganguly A, Shyng SL, Stanley CA: Clinical characteristics and biochemical mechanisms of congenital hyperinsulinism associated with dominant KATP channel mutations. J Clin Invest. 2008 Aug;118(8):2877-86. doi: 10.1172/JCI35414. [PubMed:18596924]
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  10. Mannikko R, Jefferies C, Flanagan SE, Hattersley A, Ellard S, Ashcroft FM: Interaction between mutations in the slide helix of Kir6.2 associated with neonatal diabetes and neurological symptoms. Hum Mol Genet. 2010 Mar 15;19(6):963-72. doi: 10.1093/hmg/ddp554. Epub 2009 Dec 18. [PubMed:20022885]
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  12. Tammaro P, Ashcroft FM: A mutation in the ATP-binding site of the Kir6.2 subunit of the KATP channel alters coupling with the SUR2A subunit. J Physiol. 2007 Nov 1;584(Pt 3):743-53. Epub 2007 Sep 13. [PubMed:17855752]
  13. Lin YF, Chai Y: Functional modulation of the ATP-sensitive potassium channel by extracellular signal-regulated kinase-mediated phosphorylation. Neuroscience. 2008 Mar 18;152(2):371-80. doi: 10.1016/j.neuroscience.2008.01.003. Epub 2008 Jan 9. [PubMed:18280666]
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  16. Thomas P, Ye Y, Lightner E: Mutation of the pancreatic islet inward rectifier Kir6.2 also leads to familial persistent hyperinsulinemic hypoglycemia of infancy. Hum Mol Genet. 1996 Nov;5(11):1809-12. [PubMed:8923010]
  17. Sakura H, Wat N, Horton V, Millns H, Turner RC, Ashcroft FM: Sequence variations in the human Kir6.2 gene, a subunit of the beta-cell ATP-sensitive K-channel: no association with NIDDM in while Caucasian subjects or evidence of abnormal function when expressed in vitro. Diabetologia. 1996 Oct;39(10):1233-6. [PubMed:8897013]
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  24. Gloyn AL, Cummings EA, Edghill EL, Harries LW, Scott R, Costa T, Temple IK, Hattersley AT, Ellard S: Permanent neonatal diabetes due to paternal germline mosaicism for an activating mutation of the KCNJ11 Gene encoding the Kir6.2 subunit of the beta-cell potassium adenosine triphosphate channel. J Clin Endocrinol Metab. 2004 Aug;89(8):3932-5. [PubMed:15292329]
  25. Tornovsky S, Crane A, Cosgrove KE, Hussain K, Lavie J, Heyman M, Nesher Y, Kuchinski N, Ben-Shushan E, Shatz O, Nahari E, Potikha T, Zangen D, Tenenbaum-Rakover Y, de Vries L, Argente J, Gracia R, Landau H, Eliakim A, Lindley K, Dunne MJ, Aguilar-Bryan L, Glaser B: Hyperinsulinism of infancy: novel ABCC8 and KCNJ11 mutations and evidence for additional locus heterogeneity. J Clin Endocrinol Metab. 2004 Dec;89(12):6224-34. [PubMed:15579781]
  26. Gloyn AL, Pearson ER, Antcliff JF, Proks P, Bruining GJ, Slingerland AS, Howard N, Srinivasan S, Silva JM, Molnes J, Edghill EL, Frayling TM, Temple IK, Mackay D, Shield JP, Sumnik Z, van Rhijn A, Wales JK, Clark P, Gorman S, Aisenberg J, Ellard S, Njolstad PR, Ashcroft FM, Hattersley AT: Activating mutations in the gene encoding the ATP-sensitive potassium-channel subunit Kir6.2 and permanent neonatal diabetes. N Engl J Med. 2004 Apr 29;350(18):1838-49. [PubMed:15115830]
  27. Proks P, Antcliff JF, Lippiat J, Gloyn AL, Hattersley AT, Ashcroft FM: Molecular basis of Kir6.2 mutations associated with neonatal diabetes or neonatal diabetes plus neurological features. Proc Natl Acad Sci U S A. 2004 Dec 14;101(50):17539-44. Epub 2004 Dec 6. [PubMed:15583126]
  28. Ohkubo K, Nagashima M, Naito Y, Taguchi T, Suita S, Okamoto N, Fujinaga H, Tsumura K, Kikuchi K, Ono J: Genotypes of the pancreatic beta-cell K-ATP channel and clinical phenotypes of Japanese patients with persistent hyperinsulinaemic hypoglycaemia of infancy. Clin Endocrinol (Oxf). 2005 Apr;62(4):458-65. [PubMed:15807877]
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  30. Massa O, Iafusco D, D'Amato E, Gloyn AL, Hattersley AT, Pasquino B, Tonini G, Dammacco F, Zanette G, Meschi F, Porzio O, Bottazzo G, Crino A, Lorini R, Cerutti F, Vanelli M, Barbetti F: KCNJ11 activating mutations in Italian patients with permanent neonatal diabetes. Hum Mutat. 2005 Jan;25(1):22-7. [PubMed:15580558]
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  32. Yorifuji T, Nagashima K, Kurokawa K, Kawai M, Oishi M, Akazawa Y, Hosokawa M, Yamada Y, Inagaki N, Nakahata T: The C42R mutation in the Kir6.2 (KCNJ11) gene as a cause of transient neonatal diabetes, childhood diabetes, or later-onset, apparently type 2 diabetes mellitus. J Clin Endocrinol Metab. 2005 Jun;90(6):3174-8. Epub 2005 Mar 22. [PubMed:15784703]
  33. Marthinet E, Bloc A, Oka Y, Tanizawa Y, Wehrle-Haller B, Bancila V, Dubuis JM, Philippe J, Schwitzgebel VM: Severe congenital hyperinsulinism caused by a mutation in the Kir6.2 subunit of the adenosine triphosphate-sensitive potassium channel impairing trafficking and function. J Clin Endocrinol Metab. 2005 Sep;90(9):5401-6. Epub 2005 Jul 5. [PubMed:15998776]
  34. Shimomura K, Girard CA, Proks P, Nazim J, Lippiat JD, Cerutti F, Lorini R, Ellard S, Hattersley AT, Barbetti F, Ashcroft FM: Mutations at the same residue (R50) of Kir6.2 (KCNJ11) that cause neonatal diabetes produce different functional effects. Diabetes. 2006 Jun;55(6):1705-12. [PubMed:16731833]
  35. Flanagan SE, Edghill EL, Gloyn AL, Ellard S, Hattersley AT: Mutations in KCNJ11, which encodes Kir6.2, are a common cause of diabetes diagnosed in the first 6 months of life, with the phenotype determined by genotype. Diabetologia. 2006 Jun;49(6):1190-7. Epub 2006 Apr 12. [PubMed:16609879]
  36. Fernandez-Marmiesse A, Salas A, Vega A, Fernandez-Lorenzo JR, Barreiro J, Carracedo A: Mutation spectra of ABCC8 gene in Spanish patients with Hyperinsulinism of Infancy (HI). Hum Mutat. 2006 Feb;27(2):214. [PubMed:16429405]
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  39. Stanik J, Gasperikova D, Paskova M, Barak L, Javorkova J, Jancova E, Ciljakova M, Hlava P, Michalek J, Flanagan SE, Pearson E, Hattersley AT, Ellard S, Klimes I: Prevalence of permanent neonatal diabetes in Slovakia and successful replacement of insulin with sulfonylurea therapy in KCNJ11 and ABCC8 mutation carriers. J Clin Endocrinol Metab. 2007 Apr;92(4):1276-82. Epub 2007 Jan 9. [PubMed:17213273]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB00308IbutilideapprovedunknowninhibitorDetails
DB00222GlimepirideapprovedyesinhibitorDetails
DB01119DiazoxideapprovedyesinducerDetails
DB00661VerapamilapprovedunknowninhibitorDetails
DB00922Levosimendanapproved, investigationalyesinducerDetails
DB01154Thiamylalapproved, vet_approvedyesinhibitorDetails
DB11633Isavuconazoleapproved, investigationalnoinhibitorDetails
DB01392Yohimbineapproved, investigational, vet_approvedunknowninhibitorDetails
DB11148Butambenapproved, withdrawnyesantagonistDetails
DB01016GlyburideapprovedunknowninhibitorDetails
DB00839Tolazamideapproved, investigationalyesblockerDetails
DB01016GlyburideapprovedyesblockerDetails