KCJ11_MOUSE
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 03-AUG-2022, entry version 175.
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 (TC
CC 1.A.2.1) family. KCNJ11 subfamily. {ECO:0000305}.
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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 AlphaFoldDB; Q61743; -.
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 ProteomicsDB; 263589; -.
DR ABCD; Q61743; 1 sequenced antibody.
DR Antibodypedia; 24845; 465 antibodies from 37 providers.
DR DNASU; 16514; -.
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 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; 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 BioGRID-ORCS; 16514; 1 hit in 41 CRISPR screens.
DR PRO; PR:Q61743; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q61743; protein.
DR Bgee; ENSMUSG00000096146; Expressed in gastrula and 178 other tissues.
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: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:0019829; F:ATPase-coupled 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; IBA:GO_Central.
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:0044325; F:transmembrane transporter 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:0098662; P:inorganic cation transmembrane transport; 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:0034765; P:regulation of ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0042391; P:regulation of membrane potential; ISO:MGI.
DR GO; GO:0033198; P:response to ATP; 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 GO; GO:0009410; P:response to xenobiotic stimulus; 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; 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; 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 44..47
FT /evidence="ECO:0007829|PDB:6JB1"
FT HELIX 54..57
FT /evidence="ECO:0007829|PDB:6JB1"
FT HELIX 59..65
FT /evidence="ECO:0007829|PDB:6JB1"
FT HELIX 68..96
FT /evidence="ECO:0007829|PDB:6JB1"
FT STRAND 100..102
FT /evidence="ECO:0007829|PDB:6JB1"
FT HELIX 117..128
FT /evidence="ECO:0007829|PDB:6JB1"
FT STRAND 134..136
FT /evidence="ECO:0007829|PDB:6JB1"
FT HELIX 143..171
FT /evidence="ECO:0007829|PDB:6JB1"
FT TURN 175..179
FT /evidence="ECO:0007829|PDB:6JB1"
FT STRAND 180..183
FT /evidence="ECO:0007829|PDB:6JB1"
FT STRAND 188..192
FT /evidence="ECO:0007829|PDB:6JB1"
FT STRAND 195..204
FT /evidence="ECO:0007829|PDB:6JB1"
FT STRAND 206..208
FT /evidence="ECO:0007829|PDB:6JB1"
FT STRAND 211..220
FT /evidence="ECO:0007829|PDB:6JB1"
FT STRAND 235..238
FT /evidence="ECO:0007829|PDB:6JB1"
FT STRAND 243..247
FT /evidence="ECO:0007829|PDB:6JB1"
FT STRAND 255..260
FT /evidence="ECO:0007829|PDB:6JB1"
FT STRAND 262..265
FT /evidence="ECO:0007829|PDB:6JB1"
FT TURN 266..269
FT /evidence="ECO:0007829|PDB:6JB1"
FT STRAND 282..290
FT /evidence="ECO:0007829|PDB:6JB1"
FT TURN 292..294
FT /evidence="ECO:0007829|PDB:6JB1"
FT STRAND 297..305
FT /evidence="ECO:0007829|PDB:6JB1"
FT TURN 306..308
FT /evidence="ECO:0007829|PDB:6JB1"
FT STRAND 309..314
FT /evidence="ECO:0007829|PDB:6JB1"
FT STRAND 319..321
FT /evidence="ECO:0007829|PDB:6JB1"
FT STRAND 323..329
FT /evidence="ECO:0007829|PDB:6JB1"
FT HELIX 330..332
FT /evidence="ECO:0007829|PDB:6JB1"
FT HELIX 346..357
FT /evidence="ECO:0007829|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
