ID A0A3B3SY83_9TELE Unreviewed; 409 AA.
AC A0A3B3SY83;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=G protein-activated inward rectifier potassium channel 2 {ECO:0000256|ARBA:ARBA00015884};
DE AltName: Full=Potassium channel, inwardly rectifying subfamily J member 6 {ECO:0000256|ARBA:ARBA00031384};
GN Name=KCNJ6 {ECO:0000313|Ensembl:ENSPKIP00000035208.1};
OS Paramormyrops kingsleyae.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Osteoglossocephala;
OC Osteoglossomorpha; Osteoglossiformes; Mormyridae; Paramormyrops.
OX NCBI_TaxID=1676925 {ECO:0000313|Ensembl:ENSPKIP00000035208.1, ECO:0000313|Proteomes:UP000261540};
RN [1] {ECO:0000313|Ensembl:ENSPKIP00000035208.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141,
CC ECO:0000256|RuleBase:RU003822}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU003822}.
CC -!- SIMILARITY: Belongs to the inward rectifier-type potassium channel (TC
CC 1.A.2.1) family. KCNJ6 subfamily. {ECO:0000256|ARBA:ARBA00007670}.
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DR AlphaFoldDB; A0A3B3SY83; -.
DR STRING; 1676925.ENSPKIP00000035208; -.
DR Ensembl; ENSPKIT00000016136.1; ENSPKIP00000035208.1; ENSPKIG00000014251.1.
DR GeneTree; ENSGT01080000257365; -.
DR Proteomes; UP000261540; Unplaced.
DR GO; GO:0034702; C:monoatomic ion channel complex; IEA:UniProtKB-KW.
DR GO; GO:0015467; F:G-protein activated inward rectifier potassium channel activity; IEA:InterPro.
DR Gene3D; 1.10.287.70; -; 1.
DR Gene3D; 2.60.40.1400; G protein-activated inward rectifier potassium channel 1; 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:SF19; G PROTEIN-ACTIVATED INWARD RECTIFIER POTASSIUM CHANNEL 2; 1.
DR PANTHER; PTHR11767; INWARD RECTIFIER POTASSIUM CHANNEL; 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; E set domains; 1.
DR SUPFAM; SSF81324; Voltage-gated potassium channels; 1.
PE 3: Inferred from homology;
KW Ion channel {ECO:0000256|ARBA:ARBA00023303, ECO:0000256|RuleBase:RU003822};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065,
KW ECO:0000256|RuleBase:RU003822};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Potassium {ECO:0000256|ARBA:ARBA00022958, ECO:0000256|RuleBase:RU003822};
KW Potassium transport {ECO:0000256|ARBA:ARBA00022538,
KW ECO:0000256|RuleBase:RU003822};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU003822};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU003822};
KW Voltage-gated channel {ECO:0000256|ARBA:ARBA00022882,
KW ECO:0000256|RuleBase:RU003822}.
FT TRANSMEM 78..99
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 153..176
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 42..181
FT /note="Potassium channel inwardly rectifying transmembrane"
FT /evidence="ECO:0000259|Pfam:PF01007"
FT DOMAIN 188..358
FT /note="Inward rectifier potassium channel C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17655"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 381..409
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 381..402
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 167
FT /note="Role in the control of polyamine-mediated channel
FT gating and in the blocking by intracellular magnesium"
FT /evidence="ECO:0000256|PIRSR:PIRSR005465-1"
SQ SEQUENCE 409 AA; 46759 MW; 5FE03EE7C450B574 CRC64;
MEQDVESPVT IRQPKLPKQA REDLPKQLVD KEQGKRKIQR YVRKDGKCNV HHGNVRETYR
YLTDIFTTLV DLKWRFNLFI FVLVYTVTWL FFGFMWWLIA YIRGDLEHIG DNQWTPCVNN
LNGFVSAFLF SIETETTIGY GYRVITDKCP EGIVLLLVQS VLGSIVNAFM VGCMFVKISQ
PKKRAETLVF STNAVISMRD GRLCLMFRVG DLRNSHIVEA SIRAKLIKSK QTKEGEFIPL
NQTDMNVGYD TGDDRLFLVS PLIICHEINQ HSPFWEISKA HLAKEELEIV VILEGMVEAT
GMTCQARSSY VTSEIKWGYR FTPVLTLEDG FYEVDYNSFH EVYETNTPTC SARELSEMTA
RASLPLTWSV ASKLNQQAAL DEQTERNGDI TAVTQGTSGF SGRLEKHVQ
//
