KCNJ6_PONAB
ID KCNJ6_PONAB Reviewed; 423 AA.
AC Q5NVJ6;
DT 11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 25-MAY-2022, entry version 81.
DE RecName: Full=G protein-activated inward rectifier potassium channel 2;
DE Short=GIRK-2;
DE AltName: Full=Potassium channel, inwardly rectifying subfamily J member 6;
GN Name=KCNJ6;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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 (By similarity).
CC {ECO:0000250}.
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. Interacts (via PDZ-binding motif) with SNX27 (via PDZ domain);
CC the interaction is required when endocytosed to prevent degradation in
CC lysosomes and promote recycling to the plasma membrane (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
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; CR926032; CAI29667.1; -; mRNA.
DR RefSeq; NP_001127100.1; NM_001133628.1.
DR AlphaFoldDB; Q5NVJ6; -.
DR SMR; Q5NVJ6; -.
DR STRING; 9601.ENSPPYP00000012893; -.
DR GeneID; 100174134; -.
DR KEGG; pon:100174134; -.
DR CTD; 3763; -.
DR eggNOG; KOG3827; Eukaryota.
DR InParanoid; Q5NVJ6; -.
DR OrthoDB; 956263at2759; -.
DR Proteomes; UP000001595; 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..423
FT /note="G protein-activated inward rectifier potassium
FT channel 2"
FT /id="PRO_0000154945"
FT TOPO_DOM 1..89
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 90..114
FT /note="Helical; Name=M1"
FT /evidence="ECO:0000250"
FT TOPO_DOM 115..138
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT INTRAMEM 139..150
FT /note="Helical; Pore-forming; Name=H5"
FT /evidence="ECO:0000250"
FT INTRAMEM 151..157
FT /note="Pore-forming"
FT /evidence="ECO:0000250"
FT TOPO_DOM 158..166
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 167..188
FT /note="Helical; Name=M2"
FT /evidence="ECO:0000250"
FT TOPO_DOM 189..423
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT REGION 390..423
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 152..157
FT /note="Selectivity filter"
FT /evidence="ECO:0000250"
FT MOTIF 420..423
FT /note="PDZ-binding"
FT COMPBIAS 392..423
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 182
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 16
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P48542"
FT MOD_RES 23
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P48542"
SQ SEQUENCE 423 AA; 48391 MW; 0D88D7F5FBECE69E CRC64;
MAKLTESMTN VLEGDSMDQD VESPVAIHQP KLPKQARDDL PRHISRDRTK RKIQRYVRKD
GKCNVHHGNV RETYRYLTDI FTTLVDLKWR FNLLIFVMVY TVTWLFFGMI WWLIAYIRGD
MDHIEDPSWT PCVTNLNGFV SAFLFSIETE TTIGYGYRVI TDKCPEGIIL LLIQSVLGSI
VNAFMVGCMF VKISQPKKRA ETLVFSTHAV ISMRDGKLCL MFRVGDLRNS HIVEASIRAK
LIKSKQTSEG EFIPLNQTDI NVGYYTGDDR LSLVSPLIIS HEINQQSPFW EISKAQLPKE
ELEIVVILEG MVEATGMTCQ ARSSYITSEI LWGYRFTPVL TLEDGFYEVD YNSFHETYET
STPSLSAKEL AELASRAELP LSWSVSSKLN QHAELETEEE EKNLEEQTER NGDVANLENE
SKV
