ID A0A091N518_9PASS Unreviewed; 353 AA.
AC A0A091N518;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE SubName: Full=ATP-sensitive inward rectifier potassium channel 12 {ECO:0000313|EMBL:KFP84506.1};
DE Flags: Fragment;
GN ORFNames=N310_01045 {ECO:0000313|EMBL:KFP84506.1};
OS Acanthisitta chloris (rifleman).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Acanthisittidae;
OC Acanthisitta.
OX NCBI_TaxID=57068 {ECO:0000313|EMBL:KFP84506.1, ECO:0000313|Proteomes:UP000053537};
RN [1] {ECO:0000313|EMBL:KFP84506.1, ECO:0000313|Proteomes:UP000053537}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N310 {ECO:0000313|EMBL:KFP84506.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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 EMBL; KK842240; KFP84506.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091N518; -.
DR Proteomes; UP000053537; Unassembled WGS sequence.
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: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; 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:UP000053537};
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 79..103
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 153..178
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..41
FT /note="Potassium channel inwardly rectifying Kir N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF08466"
FT DOMAIN 42..183
FT /note="Potassium channel inwardly rectifying transmembrane"
FT /evidence="ECO:0000259|Pfam:PF01007"
FT DOMAIN 190..353
FT /note="Inward rectifier potassium channel C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17655"
FT SITE 169
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"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFP84506.1"
FT NON_TER 353
FT /evidence="ECO:0000313|EMBL:KFP84506.1"
SQ SEQUENCE 353 AA; 40264 MW; 185319F54138DCE9 CRC64;
RVNPYSIVSS EEDGLRLTTM PGINGFGNGK IHTRRKCRNR FVKKNGQCNV EFANMDDKPQ
RYIADMFTTC VDIRWRYMLL LFSLAFLVSW LLFGLIFWLI ALIHGDLENP GGDDNFKPCV
LQVNGFVAAF LFSIETQTTI GYGFRCVTEE CPLAVFMVVV QSIVGCIIDS FMIGAIMAKM
ARPKKRAQTL LFSHNAVVAM RDGKLCLMWR VGNLRKSHIV EAHVRAQLIK PRITEEGEYI
PLDQIDIDVG FDKGLDRIFL VSPITILHEI NEDSPLFGIS RQDLETDDFE IVVILEGMVE
ATAMTTQARS SYLASEILWG HRFEPVLFEE KNQYKVDYSH FHKTYEVPST PRC
//
