ID A0A3B3CF94_ORYME Unreviewed; 439 AA.
AC A0A3B3CF94;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE SubName: Full=ATP-sensitive inward rectifier potassium channel 10-like {ECO:0000313|Ensembl:ENSOMEP00000015993.1};
GN Name=KCNJ10 {ECO:0000313|Ensembl:ENSOMEP00000015993.1};
OS Oryzias melastigma (Marine medaka).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; Oryziinae;
OC Oryzias.
OX NCBI_TaxID=30732 {ECO:0000313|Ensembl:ENSOMEP00000015993.1, ECO:0000313|Proteomes:UP000261560};
RN [1] {ECO:0000313|Ensembl:ENSOMEP00000015993.1}
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. {ECO:0000256|RuleBase:RU003822}.
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DR AlphaFoldDB; A0A3B3CF94; -.
DR STRING; 30732.ENSOMEP00000015993; -.
DR PaxDb; 30732-ENSOMEP00000015993; -.
DR Ensembl; ENSOMET00000034225.1; ENSOMEP00000015993.1; ENSOMEG00000017634.1.
DR GeneTree; ENSGT00990000203615; -.
DR OMA; QVNVAFQ; -.
DR OrthoDB; 4126787at2759; -.
DR Proteomes; UP000261560; Unplaced.
DR GO; GO:0034702; C:monoatomic ion channel complex; IEA:UniProtKB-KW.
DR GO; GO:0005242; F:inward rectifier potassium channel activity; IEA:Ensembl.
DR GO; GO:0001822; P:kidney development; IEA:Ensembl.
DR GO; GO:0008345; P:larval locomotory behavior; IEA:Ensembl.
DR GO; GO:1990573; P:potassium ion import across plasma membrane; IEA:InterPro.
DR GO; GO:0034765; P:regulation of monoatomic ion transmembrane transport; IEA:InterPro.
DR GO; GO:0036268; P:swimming; IEA:Ensembl.
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; IPR003268; K_chnl_inward-rec_Kir1.1.
DR InterPro; IPR013518; K_chnl_inward-rec_Kir_cyto.
DR InterPro; IPR040445; Kir_TM.
DR PANTHER; PTHR11767:SF21; ATP-SENSITIVE INWARD RECTIFIER POTASSIUM CHANNEL 10; 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; PR01321; KIR11CHANNEL.
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 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 100..121
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 174..199
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 64..204
FT /note="Potassium channel inwardly rectifying transmembrane"
FT /evidence="ECO:0000259|Pfam:PF01007"
FT DOMAIN 211..378
FT /note="Inward rectifier potassium channel C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17655"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 375..439
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 376..393
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 394..430
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 190
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 439 AA; 48486 MW; 99023E8AF0CDBF6D CRC64;
MTSATPPSSE GSSPQKVCHS QTQTDITKPL LASTGGNGST VAGGGAAAGA GGPIALRRRR
RVLSKDGRSN VRIEHVSGRG ALYLRDLWTT FLDMQWRYKF FLFSATFAGT WFLFGVLWYL
VALVHGDLIE FDPPSNHTPC VMEVKTLTGA FLFSLESQTT IGYGFRCITE ECPVAIVLLI
TQLVITMVME IFITGTFLAK VARPKKRGET VKFSQHAVVS SHEGQPCLMI RVANMRKSLL
LGCQVTGKLL QTSLTKEGET VRLDQRNVPF QVDMSTDSPF LIIPLTYYHV IDENSPLRAW
AAKGGGWADP ELADFELLVI LSATVEPTSA TCQVRTSYLP DEILWGYEFP PVVSISPSGK
YVADFAFFDK VTKSKSPPPF KQSLSPSKQS HGSQYHSVKE DGKNLEKMRL EESYRGEERG
RDKGRIRDKS PRSVCISNV
//
