ID A0A3Q3GE49_9LABR Unreviewed; 428 AA.
AC A0A3Q3GE49;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=ATP-sensitive inward rectifier potassium channel 12-like {ECO:0000313|Ensembl:ENSLBEP00000031497.1};
OS Labrus bergylta (ballan wrasse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Labriformes; Labridae; Labrus.
OX NCBI_TaxID=56723 {ECO:0000313|Ensembl:ENSLBEP00000031497.1, ECO:0000313|Proteomes:UP000261660};
RN [1] {ECO:0000313|Ensembl:ENSLBEP00000031497.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU003822}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141,
CC 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; A0A3Q3GE49; -.
DR STRING; 56723.ENSLBEP00000031497; -.
DR Ensembl; ENSLBET00000032923.1; ENSLBEP00000031497.1; ENSLBEG00000023771.1.
DR GeneTree; ENSGT01030000234586; -.
DR InParanoid; A0A3Q3GE49; -.
DR OrthoDB; 4126787at2759; -.
DR Proteomes; UP000261660; Unplaced.
DR GO; GO:0034702; C:monoatomic ion channel complex; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005242; F:inward rectifier potassium channel activity; 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; IPR003272; K_chnl_inward-rec_Kir2.2.
DR InterPro; IPR013518; K_chnl_inward-rec_Kir_cyto.
DR InterPro; IPR013673; K_chnl_inward-rec_Kir_N.
DR InterPro; IPR040445; Kir_TM.
DR PANTHER; PTHR11767:SF14; ATP-SENSITIVE INWARD RECTIFIER POTASSIUM CHANNEL 12-RELATED; 1.
DR PANTHER; PTHR11767; INWARD RECTIFIER POTASSIUM CHANNEL; 1.
DR Pfam; PF01007; IRK; 1.
DR Pfam; PF17655; IRK_C; 1.
DR Pfam; PF08466; IRK_N; 1.
DR PIRSF; PIRSF005465; GIRK_kir; 1.
DR PRINTS; PR01325; KIR22CHANNEL.
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 Cell membrane {ECO:0000256|ARBA:ARBA00022475};
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 Reference proteome {ECO:0000313|Proteomes:UP000261660};
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 84..107
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 160..183
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..48
FT /note="Potassium channel inwardly rectifying Kir N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF08466"
FT DOMAIN 49..190
FT /note="Potassium channel inwardly rectifying transmembrane"
FT /evidence="ECO:0000259|Pfam:PF01007"
FT DOMAIN 197..369
FT /note="Inward rectifier potassium channel C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17655"
FT REGION 390..428
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 393..407
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 176
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 428 AA; 48476 MW; F98381F3E8BD294D CRC64;
MSVGRAHHHH HHSFPSCEEE GLRLSAMPAV GSFGNGKIHT RRKYHSRFVG KTGQCNVHFS
NMDEKSQRYI SDIFTTCVDI RWRYMFLLFS LAFVVSWLTF GLAYWVIGLL HGDMDHPAGD
DGFVPCVTEV RTFVAAFLFS IETQTTIGYG ARCVTEECPA AVFMVVFQSI MGCIIDAFMI
GAIMAKMARP KKRAETLLFS HNAVIALRDG KLCLMFRVAN LRKSHIVEAH VRAQLVKPRF
TEEGEYIPLD QMDMNVGYDK GTDRLFLVAP LTVIHEIDEE SPLFGISKQD LETSDFEIVI
ILEGLVEATA MTTQARSSYL ASEILWGHRF EPVIFEEKSQ YRIDYAYFHK TFEVPSTPRC
SAKDMEERKF LTSGANSFCY ENELAFISRD EEEEEGEAGK DRKCSSDLVN EQATSGRDPK
SSPKESEI
//
