KCJ11_RAT
ID KCJ11_RAT Reviewed; 390 AA.
AC P70673; Q62906; Q9JM48;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=ATP-sensitive inward rectifier potassium channel 11;
DE AltName: Full=BIR;
DE AltName: Full=Inward rectifier K(+) channel Kir6.2;
DE AltName: Full=Potassium channel, inwardly rectifying subfamily J member 11;
GN Name=Kcnj11;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8798681; DOI=10.1074/jbc.271.40.24321;
RA Isomoto S., Kondo C., Yamada M., Matsumoto S., Higashiguchi O., Horio Y.,
RA Matsuzawa Y., Kurachi Y.;
RT "A novel sulfonylurea receptor forms with BIR (Kir6.2) a smooth muscle type
RT ATP-sensitive K+ channel.";
RL J. Biol. Chem. 271:24321-24324(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Pancreatic islet;
RA Faure C., Partiseti M., Gouhier C., Graham D.;
RL Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Wistar; TISSUE=Pancreatic islet;
RX PubMed=8607800; DOI=10.1006/bbrc.1996.0439;
RA Tokuyama Y., Fan Z., Furuta H., Makielski J.C., Polonsky K.S., Bell G.I.,
RA Yano H.;
RT "Rat inwardly rectifying potassium channel Kir6.2: cloning
RT electrophysiological characterization, and decreased expression in
RT pancreatic islets of male Zucker diabetic fatty rats.";
RL Biochem. Biophys. Res. Commun. 220:532-538(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Wistar; TISSUE=Heart ventricle;
RA Wada Y., Takao K., Nishi M., Takeshima H., Imai K., Yamashita T.,
RA Kokubun S., Yoshii M., Nukada T.;
RL Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Vascular smooth muscle;
RA Cao K., Wang R.;
RL Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
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 -!- 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; D86039; BAA12971.1; -; mRNA.
DR EMBL; X97041; CAA65754.1; -; mRNA.
DR EMBL; U44897; AAB01810.1; -; mRNA.
DR EMBL; D61687; BAA23630.1; -; mRNA.
DR EMBL; AB043638; BAA96239.1; -; mRNA.
DR PIR; JC4689; JC4689.
DR RefSeq; NP_112648.2; NM_031358.3.
DR PDB; 5TWV; EM; 6.30 A; A/C/E/G=1-390.
DR PDB; 6BAA; EM; 3.63 A; A/B/C/D=1-390.
DR PDB; 6PZ9; EM; 3.65 A; D=1-390.
DR PDB; 6PZA; EM; 3.74 A; D=1-390.
DR PDBsum; 5TWV; -.
DR PDBsum; 6BAA; -.
DR PDBsum; 6PZ9; -.
DR PDBsum; 6PZA; -.
DR AlphaFoldDB; P70673; -.
DR SMR; P70673; -.
DR ComplexPortal; CPX-181; Inward rectifying potassium channel complex, Kir6.2-SUR2A.
DR ComplexPortal; CPX-185; Inward rectifying potassium channel complex, Kir6.2-SUR2B.
DR ComplexPortal; CPX-186; Inward rectifying potassium channel complex, Kir6.2-SUR1.
DR CORUM; P70673; -.
DR DIP; DIP-58641N; -.
DR IntAct; P70673; 2.
DR STRING; 10116.ENSRNOP00000028685; -.
DR ChEMBL; CHEMBL3038487; -.
DR TCDB; 1.A.2.1.7; the inward rectifier k(+) channel (irk-c) family.
DR iPTMnet; P70673; -.
DR PhosphoSitePlus; P70673; -.
DR PaxDb; P70673; -.
DR ABCD; P70673; 1 sequenced antibody.
DR Ensembl; ENSRNOT00000028685; ENSRNOP00000028685; ENSRNOG00000021128.
DR GeneID; 83535; -.
DR KEGG; rno:83535; -.
DR UCSC; RGD:69247; rat.
DR CTD; 3767; -.
DR RGD; 69247; Kcnj11.
DR eggNOG; KOG3827; Eukaryota.
DR GeneTree; ENSGT00990000203615; -.
DR HOGENOM; CLU_022738_4_0_1; -.
DR InParanoid; P70673; -.
DR OMA; FGMVWWL; -.
DR OrthoDB; 956263at2759; -.
DR PhylomeDB; P70673; -.
DR TreeFam; TF313676; -.
DR Reactome; R-RNO-1296025; ATP sensitive Potassium channels.
DR Reactome; R-RNO-382556; ABC-family proteins mediated transport.
DR Reactome; R-RNO-422356; Regulation of insulin secretion.
DR Reactome; R-RNO-5578775; Ion homeostasis.
DR PRO; PR:P70673; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000021128; Expressed in skeletal muscle tissue and 11 other tissues.
DR Genevisible; P70673; RN.
DR GO; GO:0001669; C:acrosomal vesicle; IDA:RGD.
DR GO; GO:0030673; C:axolemma; IDA:RGD.
DR GO; GO:0070852; C:cell body fiber; IDA:RGD.
DR GO; GO:0005829; C:cytosol; IDA:RGD.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:RGD.
DR GO; GO:0005768; C:endosome; IDA:RGD.
DR GO; GO:0014704; C:intercalated disc; IDA:RGD.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:RGD.
DR GO; GO:0008282; C:inward rectifying potassium channel; IDA:RGD.
DR GO; GO:0005739; C:mitochondrion; IDA:RGD.
DR GO; GO:0043209; C:myelin sheath; IDA:RGD.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0005635; C:nuclear envelope; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0042383; C:sarcolemma; IDA:RGD.
DR GO; GO:0030315; C:T-tubule; IDA:RGD.
DR GO; GO:0030506; F:ankyrin binding; IPI:BHF-UCL.
DR GO; GO:0005524; F:ATP binding; ISO:RGD.
DR GO; GO:0015272; F:ATP-activated inward rectifier potassium channel activity; IDA:RGD.
DR GO; GO:0019829; F:ATPase-coupled cation transmembrane transporter activity; IGI:ARUK-UCL.
DR GO; GO:0031072; F:heat shock protein binding; IPI:RGD.
DR GO; GO:0005242; F:inward rectifier potassium channel activity; IBA:GO_Central.
DR GO; GO:0008022; F:protein C-terminus binding; IPI:RGD.
DR GO; GO:0044325; F:transmembrane transporter binding; ISO:RGD.
DR GO; GO:0005249; F:voltage-gated potassium channel activity; ISO:RGD.
DR GO; GO:0071333; P:cellular response to glucose stimulus; IEP:RGD.
DR GO; GO:0071316; P:cellular response to nicotine; IEP:RGD.
DR GO; GO:0071356; P:cellular response to tumor necrosis factor; IEP:RGD.
DR GO; GO:0006006; P:glucose metabolic process; ISO:RGD.
DR GO; GO:0098662; P:inorganic cation transmembrane transport; IGI:ARUK-UCL.
DR GO; GO:0046676; P:negative regulation of insulin secretion; ISO:RGD.
DR GO; GO:0050877; P:nervous system process; ISO:RGD.
DR GO; GO:2001259; P:positive regulation of cation channel activity; IMP:RGD.
DR GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; IMP:RGD.
DR GO; GO:1990573; P:potassium ion import across plasma membrane; IDA:ComplexPortal.
DR GO; GO:0071805; P:potassium ion transmembrane transport; ISO:RGD.
DR GO; GO:0006813; P:potassium ion transport; IDA:RGD.
DR GO; GO:0050796; P:regulation of insulin secretion; ISO:RGD.
DR GO; GO:0034765; P:regulation of ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0042391; P:regulation of membrane potential; ISO:RGD.
DR GO; GO:0033198; P:response to ATP; IGI:ARUK-UCL.
DR GO; GO:0032355; P:response to estradiol; IEP:RGD.
DR GO; GO:0002931; P:response to ischemia; IEP:RGD.
DR GO; GO:0033574; P:response to testosterone; IEP:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
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_0000154960"
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 191
FT /note="L -> P (in Ref. 5; BAA96239)"
FT /evidence="ECO:0000305"
FT CONFLICT 365
FT /note="R -> Q (in Ref. 3; AAB01810)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 390 AA; 43608 MW; C8E59AD298DE4F13 CRC64;
MLSRKGIIPE EYVLTRLAED PTEPRYRTRE RRARFVSKKG NCNVAHKNIR EQGRFLQDVF
TTLVDLKWPH TLLIFTMSFL CSWLLFAMVW WLIAFAHGDL APGEGTNVPC VTSIHSFSSA
FLFSIEVQVT IGFGGRMVTE ECPLAILILI VQNIVGLMIN AIMLGCIFMK TAQAHRRAET
LIFSKHAVIT LRHGRLCFML RVGDLRKSMI ISATIHMQVV RKTTSPEGEV VPLHQVDIPM
ENGVGGNSIF LVAPLIIYHV IDSNSPLYDL APSDLHHHQD LEIIVILEGV VETTGITTQA
RTSYLADEIL WGQRFVPIVA EEDGRYSVDY SKFGNTVKVP TPLCTARQLD EDRSLLDALT
LASSRGPLRK RSVAVAKAKP KFSISPDSLS
