KCNJ8_RAT
ID KCNJ8_RAT Reviewed; 424 AA.
AC Q63664; Q9JM49; Q9JM50;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=ATP-sensitive inward rectifier potassium channel 8;
DE AltName: Full=Inward rectifier K(+) channel Kir6.1;
DE AltName: Full=Potassium channel, inwardly rectifying subfamily J member 8;
DE AltName: Full=uKATP-1;
GN Name=Kcnj8;
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], FUNCTION, AND TISSUE SPECIFICITY.
RC STRAIN=Sprague-Dawley; TISSUE=Pancreatic islet;
RX PubMed=7890693; DOI=10.1074/jbc.270.11.5691;
RA Inagaki N., Tsuura Y., Namba N., Masuda K., Gonoi T., Horie M., Seino Y.,
RA Mizuta M., Seino S.;
RT "Cloning and functional characterization of a novel ATP-sensitive potassium
RT channel ubiquitously expressed in rat tissues, including pancreatic islets,
RT pituitary, skeletal muscle, and heart.";
RL J. Biol. Chem. 270:5691-5694(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS.
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 potassium channel is controlled by G proteins. Inward
CC rectifier potassium channels are characterized by a greater tendency to
CC allow potassium to flow into the cell rather than out of it. Their
CC voltage 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 external barium.
CC {ECO:0000269|PubMed:7890693}.
CC -!- INTERACTION:
CC Q63664; P08050: Gja1; NbExp=4; IntAct=EBI-6991142, EBI-476947;
CC Q63664; P23242: Gja1; Xeno; NbExp=4; IntAct=EBI-6991142, EBI-298630;
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein
CC {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Widely expressed, including in pancreatic islets,
CC pituitary, skeletal muscle and heart. {ECO:0000269|PubMed:7890693}.
CC -!- SIMILARITY: Belongs to the inward rectifier-type potassium channel (TC
CC 1.A.2.1) family. KCNJ8 subfamily. {ECO:0000305}.
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DR EMBL; D42145; BAA07716.1; -; mRNA.
DR EMBL; AB043636; BAA96237.1; -; mRNA.
DR EMBL; AB043637; BAA96238.1; -; mRNA.
DR PIR; I60373; I60373.
DR RefSeq; NP_058795.3; NM_017099.4.
DR PDB; 7MIT; EM; 3.40 A; A/B/C/D=1-424.
DR PDB; 7MJO; EM; 4.00 A; A/B/C/D=1-424.
DR PDB; 7MJP; EM; 4.20 A; A/B/C/D=1-424.
DR PDB; 7MJQ; EM; 4.20 A; A/B/C/D=1-424.
DR PDBsum; 7MIT; -.
DR PDBsum; 7MJO; -.
DR PDBsum; 7MJP; -.
DR PDBsum; 7MJQ; -.
DR AlphaFoldDB; Q63664; -.
DR SMR; Q63664; -.
DR CORUM; Q63664; -.
DR IntAct; Q63664; 3.
DR MINT; Q63664; -.
DR STRING; 10116.ENSRNOP00000018057; -.
DR ChEMBL; CHEMBL4524131; -.
DR iPTMnet; Q63664; -.
DR PhosphoSitePlus; Q63664; -.
DR PaxDb; Q63664; -.
DR ABCD; Q63664; 2 sequenced antibodies.
DR Ensembl; ENSRNOT00000018057; ENSRNOP00000018057; ENSRNOG00000013463.
DR GeneID; 25472; -.
DR KEGG; rno:25472; -.
DR UCSC; RGD:2960; rat.
DR CTD; 3764; -.
DR RGD; 2960; Kcnj8.
DR eggNOG; KOG3827; Eukaryota.
DR GeneTree; ENSGT00990000203615; -.
DR HOGENOM; CLU_022738_4_0_1; -.
DR InParanoid; Q63664; -.
DR OMA; NSMRKGG; -.
DR OrthoDB; 956263at2759; -.
DR PhylomeDB; Q63664; -.
DR TreeFam; TF313676; -.
DR Reactome; R-RNO-1296025; ATP sensitive Potassium channels.
DR PRO; PR:Q63664; -.
DR Proteomes; UP000002494; Chromosome 4.
DR Bgee; ENSRNOG00000013463; Expressed in heart and 19 other tissues.
DR Genevisible; Q63664; RN.
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:0016020; C:membrane; IDA:RGD.
DR GO; GO:0005739; C:mitochondrion; IDA:RGD.
DR GO; GO:0030016; C:myofibril; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0042383; C:sarcolemma; IDA:RGD.
DR GO; GO:0005524; F:ATP binding; IDA:ARUK-UCL.
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:0005242; F:inward rectifier potassium channel activity; IBA:GO_Central.
DR GO; GO:0017098; F:sulfonylurea receptor binding; IPI:RGD.
DR GO; GO:1902282; F:voltage-gated potassium channel activity involved in ventricular cardiac muscle cell action potential repolarization; ISO:RGD.
DR GO; GO:0051607; P:defense response to virus; ISO:RGD.
DR GO; GO:0007507; P:heart development; ISO:RGD.
DR GO; GO:0098662; P:inorganic cation transmembrane transport; IGI:ARUK-UCL.
DR GO; GO:0001822; P:kidney development; IEP:RGD.
DR GO; GO:0098915; P:membrane repolarization during ventricular cardiac muscle cell action potential; ISO:RGD.
DR GO; GO:1990573; P:potassium ion import across plasma membrane; IDA:RGD.
DR GO; GO:0006813; P:potassium ion transport; IDA:RGD.
DR GO; GO:0034765; P:regulation of ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0043330; P:response to exogenous dsRNA; ISO:RGD.
DR GO; GO:0032496; P:response to lipopolysaccharide; ISO: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; IPR003278; K_chnl_inward-rec_Kir6.1.
DR InterPro; IPR013518; K_chnl_inward-rec_Kir_cyto.
DR InterPro; IPR040445; Kir_TM.
DR PANTHER; PTHR11767; PTHR11767; 1.
DR PANTHER; PTHR11767:SF11; PTHR11767:SF11; 1.
DR Pfam; PF01007; IRK; 1.
DR Pfam; PF17655; IRK_C; 1.
DR PIRSF; PIRSF005465; GIRK_kir; 1.
DR PRINTS; PR01331; KIR61CHANNEL.
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..424
FT /note="ATP-sensitive inward rectifier potassium channel 8"
FT /id="PRO_0000154949"
FT TOPO_DOM 1..69
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 70..94
FT /note="Helical; Name=M1"
FT /evidence="ECO:0000250"
FT TOPO_DOM 95..126
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT INTRAMEM 127..138
FT /note="Helical; Pore-forming; Name=H5"
FT /evidence="ECO:0000250"
FT INTRAMEM 139..145
FT /note="Pore-forming"
FT /evidence="ECO:0000250"
FT TOPO_DOM 146..154
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 155..176
FT /note="Helical; Name=M2"
FT /evidence="ECO:0000250"
FT TOPO_DOM 177..424
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT REGION 374..424
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 140..145
FT /note="Selectivity filter"
FT /evidence="ECO:0000250"
FT COMPBIAS 390..424
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 170
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 6
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P97794"
FT VARIANT 23
FT /note="R -> H"
FT VARIANT 48
FT /note="K -> Q"
FT VARIANT 150
FT /note="E -> G"
FT VARIANT 170
FT /note="N -> D"
FT VARIANT 241
FT /note="V -> A"
FT VARIANT 379
FT /note="S -> F"
FT HELIX 17..20
FT /evidence="ECO:0007829|PDB:7MIT"
FT HELIX 58..65
FT /evidence="ECO:0007829|PDB:7MIT"
FT HELIX 69..97
FT /evidence="ECO:0007829|PDB:7MIT"
FT HELIX 100..109
FT /evidence="ECO:0007829|PDB:7MIT"
FT TURN 110..112
FT /evidence="ECO:0007829|PDB:7MIT"
FT HELIX 127..138
FT /evidence="ECO:0007829|PDB:7MIT"
FT STRAND 144..146
FT /evidence="ECO:0007829|PDB:7MIT"
FT HELIX 153..182
FT /evidence="ECO:0007829|PDB:7MIT"
FT STRAND 183..185
FT /evidence="ECO:0007829|PDB:7MIT"
FT STRAND 191..193
FT /evidence="ECO:0007829|PDB:7MIT"
FT STRAND 209..214
FT /evidence="ECO:0007829|PDB:7MIT"
FT STRAND 216..218
FT /evidence="ECO:0007829|PDB:7MIT"
FT STRAND 220..234
FT /evidence="ECO:0007829|PDB:7MIT"
FT STRAND 240..247
FT /evidence="ECO:0007829|PDB:7MIT"
FT STRAND 265..268
FT /evidence="ECO:0007829|PDB:7MIT"
FT HELIX 276..279
FT /evidence="ECO:0007829|PDB:7MIT"
FT TURN 282..286
FT /evidence="ECO:0007829|PDB:7MIT"
FT STRAND 291..300
FT /evidence="ECO:0007829|PDB:7MIT"
FT TURN 301..303
FT /evidence="ECO:0007829|PDB:7MIT"
FT STRAND 306..314
FT /evidence="ECO:0007829|PDB:7MIT"
FT TURN 315..317
FT /evidence="ECO:0007829|PDB:7MIT"
FT STRAND 322..324
FT /evidence="ECO:0007829|PDB:7MIT"
FT STRAND 328..330
FT /evidence="ECO:0007829|PDB:7MIT"
FT STRAND 332..338
FT /evidence="ECO:0007829|PDB:7MIT"
FT HELIX 339..341
FT /evidence="ECO:0007829|PDB:7MIT"
FT STRAND 345..347
FT /evidence="ECO:0007829|PDB:7MIT"
FT HELIX 355..358
FT /evidence="ECO:0007829|PDB:7MIT"
SQ SEQUENCE 424 AA; 47963 MW; 22548313B92FE095 CRC64;
MLARKSIIPE EYVLARIAAE NLRKPRIRDR LPKARFIAKS GACNLAHKNI REQGRFLQDI
FTTLVDLKWR HTLVIFTMSF LCSWLLFAIM WWLVAFAHGD IYAYMEKGIT EKSGLESAVC
VTNVRSFTSA FLFSIEVQVT IGFGGRMMTE ECPLAITVLI LQNIVGLIIN AVMLGCIFMK
TAQAHRRAET LIFSRHAVIA VRNGKLCFMF RVGDLRKSMI ISASVRIQVV KKTTTPEGEV
VPIHQQDIPV DNPIESNNIF LVAPLIICHV IDKRSPLYDI SATDLVNQDL EVIVILEGVV
ETTGITTQAR TSYIAEEIQW GHRFVSIVTE EEGVYSVDYS KFGNTVRVAA PRCSARELDE
KPSILIQTLQ KSELSHQNSL RKRNSMRRNN SMRRSNSIRR NNSSLMVPKV QFMTPEGNQC
PSES
