KCNJ6_RAT
ID KCNJ6_RAT Reviewed; 425 AA.
AC P48550;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=G protein-activated inward rectifier potassium channel 2;
DE Short=GIRK-2;
DE AltName: Full=BIR1;
DE AltName: Full=Inward rectifier K(+) channel Kir3.2;
DE AltName: Full=KATP-2;
DE AltName: Full=Potassium channel, inwardly rectifying subfamily J member 6;
GN Name=Kcnj6; Synonyms=Girk2, Kcnj7;
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].
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RX PubMed=7601286; DOI=10.1016/0014-5793(95)00497-w;
RA Bond C.T., Aemmaelae C., Ashfield R., Blair T.A., Gribble F., Khan R.N.,
RA Lee K., Proks P., Rowe I.C.M., Sakura H., Ashford M.J., Adelman J.P.,
RA Ashcroft F.M.;
RT "Cloning and functional expression of the cDNA encoding an inwardly-
RT rectifying potassium channel expressed in pancreatic beta-cells and in the
RT brain.";
RL FEBS Lett. 367:61-66(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7626127; DOI=10.1006/bbrc.1995.2053;
RA Stoffel M., Tokuyama Y., Trabb J.B., German M.S., Tsaar M.L., Jan L.Y.,
RA Polonsky K.S., Bell G.I.;
RT "Cloning of rat KATP-2 channel and decreased expression in pancreatic
RT islets of male Zucker diabetic fatty rats.";
RL Biochem. Biophys. Res. Commun. 212:894-899(1995).
RN [3]
RP INTERACTION WITH SNX27.
RX PubMed=17828261; DOI=10.1038/nn1953;
RA Lunn M.L., Nassirpour R., Arrabit C., Tan J., McLeod I., Arias C.M.,
RA Sawchenko P.E., Yates J.R. III, Slesinger P.A.;
RT "A unique sorting nexin regulates trafficking of potassium channels via a
RT PDZ domain interaction.";
RL Nat. Neurosci. 10:1249-1259(2007).
CC -!- FUNCTION: This potassium channel is controlled by G proteins. It may be
CC involved in the regulation of insulin secretion by glucose and/or
CC neurotransmitters. Inward rectifier potassium channels are
CC characterized by a greater tendency to allow potassium to flow into the
CC cell rather than out of it. Their voltage dependence is regulated by
CC the concentration of extracellular potassium; as external potassium is
CC raised, the voltage range of the channel opening shifts to more
CC positive voltages. The inward rectification is mainly due to the
CC blockage of outward current by internal magnesium. Can be blocked by
CC external barium or cesium.
CC -!- SUBUNIT: Associates with GIRK1 or GIRK4 to form a G-protein-activated
CC heteromultimer pore-forming unit. The resulting inward current is much
CC larger (By similarity). Interacts (via PDZ-binding motif) with SNX27
CC (via PDZ domain); the interaction is required for recycling to the
CC plasma membrane when endocytosed and prevent degradation in lysosomes.
CC {ECO:0000250, ECO:0000269|PubMed:17828261}.
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Pancreatic beta cells and brain.
CC -!- SIMILARITY: Belongs to the inward rectifier-type potassium channel (TC
CC 1.A.2.1) family. KCNJ6 subfamily. {ECO:0000305}.
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DR EMBL; X83583; CAA58566.1; -; mRNA.
DR EMBL; U21087; AAA87002.1; -; mRNA.
DR PIR; S66266; S52852.
DR RefSeq; NP_037324.1; NM_013192.2.
DR AlphaFoldDB; P48550; -.
DR SMR; P48550; -.
DR STRING; 10116.ENSRNOP00000059308; -.
DR iPTMnet; P48550; -.
DR PhosphoSitePlus; P48550; -.
DR PaxDb; P48550; -.
DR PRIDE; P48550; -.
DR GeneID; 25743; -.
DR KEGG; rno:25743; -.
DR UCSC; RGD:2959; rat.
DR CTD; 3763; -.
DR RGD; 2959; Kcnj6.
DR eggNOG; KOG3827; Eukaryota.
DR InParanoid; P48550; -.
DR OrthoDB; 956263at2759; -.
DR PhylomeDB; P48550; -.
DR Reactome; R-RNO-1296041; Activation of G protein gated Potassium channels.
DR Reactome; R-RNO-997272; Inhibition of voltage gated Ca2+ channels via Gbeta/gamma subunits.
DR PRO; PR:P48550; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0030424; C:axon; IDA:RGD.
DR GO; GO:0009986; C:cell surface; IDA:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0030425; C:dendrite; IDA:RGD.
DR GO; GO:0099056; C:integral component of presynaptic membrane; ISO:RGD.
DR GO; GO:0032809; C:neuronal cell body membrane; IDA:RGD.
DR GO; GO:0098688; C:parallel fiber to Purkinje cell synapse; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0015467; F:G-protein activated inward rectifier potassium channel activity; ISO:RGD.
DR GO; GO:0001965; F:G-protein alpha-subunit binding; IDA:RGD.
DR GO; GO:0005242; F:inward rectifier potassium channel activity; IBA:GO_Central.
DR GO; GO:0071315; P:cellular response to morphine; IEP:RGD.
DR GO; GO:1990573; P:potassium ion import across plasma membrane; IBA:GO_Central.
DR GO; GO:0034765; P:regulation of ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0051602; P:response to electrical stimulus; IEP:RGD.
DR GO; GO:0042403; P:thyroid hormone metabolic process; 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; IPR003275; K_chnl_inward-rec_Kir3.2.
DR InterPro; IPR013518; K_chnl_inward-rec_Kir_cyto.
DR InterPro; IPR040445; Kir_TM.
DR PANTHER; PTHR11767; PTHR11767; 1.
DR PANTHER; PTHR11767:SF19; PTHR11767:SF19; 1.
DR Pfam; PF01007; IRK; 1.
DR Pfam; PF17655; IRK_C; 1.
DR PIRSF; PIRSF005465; GIRK_kir; 1.
DR PRINTS; PR01328; KIR32CHANNEL.
DR PRINTS; PR01320; KIRCHANNEL.
DR SUPFAM; SSF81296; SSF81296; 1.
PE 1: Evidence at protein 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..425
FT /note="G protein-activated inward rectifier potassium
FT channel 2"
FT /id="PRO_0000154946"
FT TOPO_DOM 1..91
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 92..116
FT /note="Helical; Name=M1"
FT /evidence="ECO:0000250"
FT TOPO_DOM 117..140
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT INTRAMEM 141..152
FT /note="Helical; Pore-forming; Name=H5"
FT /evidence="ECO:0000250"
FT INTRAMEM 153..159
FT /note="Pore-forming"
FT /evidence="ECO:0000250"
FT TOPO_DOM 160..168
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 169..190
FT /note="Helical; Name=M2"
FT /evidence="ECO:0000250"
FT TOPO_DOM 191..425
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT REGION 392..425
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 154..159
FT /note="Selectivity filter"
FT /evidence="ECO:0000250"
FT MOTIF 422..425
FT /note="PDZ-binding"
FT COMPBIAS 394..425
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 184
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 18
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P48542"
FT MOD_RES 25
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P48542"
FT CONFLICT 328
FT /note="V -> I (in Ref. 2; AAA87002)"
FT /evidence="ECO:0000305"
FT CONFLICT 360
FT /note="H -> Y (in Ref. 2; AAA87002)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 425 AA; 48640 MW; 66CE9599A4AE38D3 CRC64;
MTMAKLTESM TNVLEGDSMD QDVESPVAIH QPKLPKQARD DLPRHISRDR TKRKIQRYVR
KDGKCNVHHG NVRETYRYLT DIFTTLVDLK WRFNLLIFVM VYTVTWLFFG MIWWLIAYIR
GDMDHIEDPS WTPCVTNLNG FVSAFLFSIE TETTIGYGYR VITDKCPEGI ILLLIQSVLG
SIVNAFMVGC MFVKISQPKK RAETLVFSTH AVISMRDGKL CLMFRVGDLR NSHIVEASIR
AKLIKSKQTS EGEFIPLNQT DINVGYYTGD DRLFLVSPLI ISHEINQQSP FWEISKAQLP
KEELEIVVIL EGMVEATGMT CQARSSYVTS EILWGYRFTP VLTLEDGFYE VDYNSFHETH
ETSTPSLSAK ELAELANRAE LPLSWSVSSK LNQHAELETE EEEKNPEELT ERNGDVANLE
NESKV
