KCNJ6_MESAU
ID KCNJ6_MESAU Reviewed; 425 AA.
AC P49658;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 25-MAY-2022, entry version 109.
DE RecName: Full=G protein-activated inward rectifier potassium channel 2;
DE Short=GIRK-2;
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, KATP2, KCNJ7;
OS Mesocricetus auratus (Golden hamster).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Mesocricetus.
OX NCBI_TaxID=10036;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Insulinoma;
RX PubMed=7729621; DOI=10.2337/diab.44.5.592;
RA Tsaur M.-L., Menzel S., Lai F.-P., Espinosa R. III, Concannon P.,
RA Spielman R.S., Hanis C.L., Cox N.J., le Beau M.M., German M.S., Jan L.Y.,
RA Bell G.I., Stoffel M.;
RT "Isolation of a cDNA clone encoding a KATP channel-like protein expressed
RT in insulin-secreting cells, localization of the human gene to chromosome
RT band 21q22.1, and linkage studies with NIDDM.";
RL Diabetes 44:592-596(1995).
CC -!- FUNCTION: This potassium channel may be involved in the regulation of
CC insulin secretion by glucose and/or neurotransmitters acting through G-
CC protein-coupled receptors. 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.
CC -!- SUBUNIT: May associate with GIRK1 or GIRK4 to form a G-protein-
CC activated heteromultimer pore-forming unit. The resulting inward
CC current is much larger. Interacts (via PDZ-binding motif) with SNX27
CC (via PDZ domain); the interaction is required when endocytosed to
CC prevent degradation in lysosomes and promote recycling to the plasma
CC membrane (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Expressed in insulin-secreting 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; U21937; AAA79983.1; -; mRNA.
DR PIR; I48202; I48202.
DR RefSeq; NP_001268770.1; NM_001281841.1.
DR AlphaFoldDB; P49658; -.
DR SMR; P49658; -.
DR GeneID; 101823647; -.
DR CTD; 3763; -.
DR eggNOG; KOG3827; Eukaryota.
DR OrthoDB; 956263at2759; -.
DR PRO; PR:P49658; -.
DR Proteomes; UP000189706; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0015467; F:G-protein 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; 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 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..425
FT /note="G protein-activated inward rectifier potassium
FT channel 2"
FT /id="PRO_0000154943"
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"
SQ SEQUENCE 425 AA; 48647 MW; E49A16495FB1CEED CRC64;
MTMAKLTESM TNVLEGDSMD QDVESPVAIH QPKLPKQARD DLPRHISRDR TKRKIQRYVR
KDGKCNVHHG NVRETYRYLT DILTTLVDLK WRFNLLIFVM VYTVTWLFFG MIWWLIAYIR
GDMDHVEDPS WTPCVTNLNG FVSAFLFSIE TETTIGYGYR VITDKCPEGI ILLLIQSVLG
SIVNAFMVGC MFVKISQPKK RAETLVFSTH AVISMRDGKL CLMFRVGDLR NSHIVEASIR
AKLIKSKQTS EGEFIPLNQT DINVGYYTGD DRLFLVSPLI ISHEINQQSP FWEISKAQLP
KEELEIVVIL EGMVEATGMT CQARSSYITS EILWGYRFTP VLTLEDGFYE VDYNSFHETY
ETSTPSLSAK ELAELANRAE LPLSWSVSSK LNQHAELETE EEEKNPEEQT ERNGDVANLE
NESKV
