ID   KCJ11_RABIT             Reviewed;         390 AA.
AC   O02822;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   25-MAY-2022, entry version 104.
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; Synonyms=KIR62;
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Heart;
RA   Janecki M., O'Rourke B., Marban E.;
RT   "Rabbit cardiac ATP-sensitive potassium channel Kir6.2.";
RL   Submitted (MAY-1997) 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 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; AF006262; AAB61473.1; -; mRNA.
DR   RefSeq; NP_001075486.1; NM_001082017.1.
DR   AlphaFoldDB; O02822; -.
DR   SMR; O02822; -.
DR   GeneID; 100008648; -.
DR   KEGG; ocu:100008648; -.
DR   CTD; 3767; -.
DR   InParanoid; O02822; -.
DR   OrthoDB; 956263at2759; -.
DR   Proteomes; UP000001811; Unplaced.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0015272; F:ATP-activated inward rectifier potassium channel activity; IEA:InterPro.
DR   GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
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_0000154959"
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;  43438 MW;  17D5C39E0025EAE3 CRC64;
     MLSRKGIIPE EYVLTRLAED PAEPRYRARE RRARFVSKKG NCNVAHKNIR EQGRFLQDVF
     TTLVDLKWTH TLLIFTMSFL CSWLLFAMVW WLIAFAHGDL APGEGAAVPC VTSIHSFSSA
     FLFSIEVQVT IGFGGRMVTE ECPLAILILI VQNIVGLMIN AIMLGCIFMK TAQAHRRAET
     LIFSKHAVIA LRQGRLCFML RVGDLRKSMI ISATIHMQVV RKTTSPEGEV VPLHQVDIPM
     ENGVGGNSIF LVAPLIIHHV IDANSPLYDL APSDLHHHQD LEIIVILEGV VETTGITTQA
     RTSYLADEIL WGQRFVPIVA EEDGRYSVDY SKFGNTVKVP TPLCTARQLD EDRSLLDALT
     LTSARGPLRK RSVPVAKAKP KFSISPDSLS