KCJ11_CAVPO
ID KCJ11_CAVPO Reviewed; 390 AA.
AC Q9JHJ9;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=ATP-sensitive inward rectifier potassium channel 11;
DE AltName: Full=IKATP;
DE AltName: Full=Inward rectifier K(+) channel Kir6.2;
DE AltName: Full=Potassium channel, inwardly rectifying subfamily J member 11;
GN Name=KCNJ11;
OS Cavia porcellus (Guinea pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC Cavia.
OX NCBI_TaxID=10141;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX PubMed=10835035; DOI=10.1111/j.1469-7793.2000.t01-1-00307.x;
RA Mederos y Schnitzler M., Derst C., Daut J., Preisig-Mueller R.;
RT "ATP-sensitive potassium channels in capillaries isolated from guinea-pig
RT heart.";
RL J. Physiol. (Lond.) 525:307-317(2000).
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 ABCC8/SUR. Interacts with ABCC9/SUR2 (By
CC similarity). {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; AF183920; AAF79058.1; -; Genomic_DNA.
DR EMBL; AF183919; AAF79057.1; -; mRNA.
DR RefSeq; NP_001166445.1; NM_001172974.1.
DR AlphaFoldDB; Q9JHJ9; -.
DR SMR; Q9JHJ9; -.
DR STRING; 10141.ENSCPOP00000019931; -.
DR Ensembl; ENSCPOT00000004187; ENSCPOP00000019931; ENSCPOG00000004142.
DR GeneID; 100135564; -.
DR KEGG; cpoc:100135564; -.
DR CTD; 3767; -.
DR eggNOG; KOG3827; Eukaryota.
DR GeneTree; ENSGT00990000203615; -.
DR HOGENOM; CLU_022738_4_0_1; -.
DR InParanoid; Q9JHJ9; -.
DR OMA; FGMVWWL; -.
DR OrthoDB; 956263at2759; -.
DR TreeFam; TF313676; -.
DR Proteomes; UP000005447; Unassembled WGS sequence.
DR Bgee; ENSCPOG00000004142; Expressed in heart left ventricle and 7 other tissues.
DR GO; GO:0008282; C:inward rectifying potassium channel; IEA:Ensembl.
DR GO; GO:0030315; C:T-tubule; IEA:Ensembl.
DR GO; GO:0030506; F:ankyrin binding; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:Ensembl.
DR GO; GO:0015272; F:ATP-activated inward rectifier potassium channel activity; IEA:Ensembl.
DR GO; GO:0044325; F:transmembrane transporter binding; IEA:Ensembl.
DR GO; GO:0006006; P:glucose metabolic process; IEA:Ensembl.
DR GO; GO:0046676; P:negative regulation of insulin secretion; IEA:Ensembl.
DR GO; GO:0050877; P:nervous system process; IEA:Ensembl.
DR GO; GO:1990573; P:potassium ion import across plasma membrane; IEA:Ensembl.
DR GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
DR GO; GO:0042391; P:regulation of membrane potential; IEA:Ensembl.
DR GO; GO:0033198; P:response to ATP; IEA:Ensembl.
DR GO; GO:0009410; P:response to xenobiotic stimulus; 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 2: Evidence at transcript level;
KW Ion channel; Ion transport; Membrane; Phosphoprotein; Potassium;
KW 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_0000154956"
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"
SQ SEQUENCE 390 AA; 43574 MW; 536D5A7809E1E78F CRC64;
MLSRKGIIPE EYVLTRLAED PTEPRYRARE RRARFVSKKG NCNVAHKNIR EQGRFLQDVF
TTLVDLKWPH TLLIFTMSFL CSWLLFAMVW WLIAFAHGDL APGEGTTVPC VTSIHSFSSA
FLFSIEVQVT IGFGGRMVTE ECPLAILILI VQNIVGLMIN AIMLGCIFMK TSQAHRRAET
LIFSKHAVIA LRHGRLCFML RVGDLRKSMI ISATIHMQVV RKTTSPEGEV VPLHQVDIPM
ENGVGGNSIF LVAPLIIYHV IDANSPLYDL GPSDLHHHQD LEIIVILEGV VETTGITTQA
RTSYLADEIL WGHRFVPIVA EEDGRYSVDY SKFGNTIKVP TPLCTAHQLD EDHSLLDALT
LASTRGPLRK RSVPVAKAKP RFSISPDSLS
