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Database: UniProt
Entry: A0A087R5T1_APTFO
LinkDB: A0A087R5T1_APTFO
Original site: A0A087R5T1_APTFO 
ID   A0A087R5T1_APTFO        Unreviewed;       352 AA.
AC   A0A087R5T1;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   SubName: Full=ATP-sensitive inward rectifier potassium channel 10 {ECO:0000313|EMBL:KFM08835.1};
DE   Flags: Fragment;
GN   ORFNames=AS27_07639 {ECO:0000313|EMBL:KFM08835.1};
OS   Aptenodytes forsteri (Emperor penguin).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Sphenisciformes; Spheniscidae;
OC   Aptenodytes.
OX   NCBI_TaxID=9233 {ECO:0000313|EMBL:KFM08835.1, ECO:0000313|Proteomes:UP000053286};
RN   [1] {ECO:0000313|EMBL:KFM08835.1, ECO:0000313|Proteomes:UP000053286}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_AS27 {ECO:0000313|EMBL:KFM08835.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: 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   EMBL; KL226132; KFM08835.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A087R5T1; -.
DR   STRING; 9233.A0A087R5T1; -.
DR   Proteomes; UP000053286; Unassembled WGS sequence.
DR   GO; GO:0034702; C:monoatomic ion channel complex; IEA:UniProtKB-KW.
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; IPR003269; K_chnl_inward-rec_Kir1.2.
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; PR01322; KIR12CHANNEL.
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   Reference proteome {ECO:0000313|Proteomes:UP000053286};
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        40..61
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        114..139
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          3..144
FT                   /note="Potassium channel inwardly rectifying transmembrane"
FT                   /evidence="ECO:0000259|Pfam:PF01007"
FT   DOMAIN          151..316
FT                   /note="Inward rectifier potassium channel C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17655"
FT   SITE            130
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:KFM08835.1"
FT   NON_TER         352
FT                   /evidence="ECO:0000313|EMBL:KFM08835.1"
SQ   SEQUENCE   352 AA;  39614 MW;  7B42498930477C9A CRC64;
     RVMTKDGRSN VRMEHIADKR FLYLKDLWTT FIDMQWRYKL VLFSATFAGT WFAFGVIWYL
     VAVVHGDLLE FDPPANHTPC VMQVHTLTGA FLFSLESQTT IGYGFRYISE ECPLAIVLLI
     TQLVLTTIME IFITGTFLAK IARPKKRAET IKFSQNAVVA QHNGKTCLMI RVANMRKSLL
     IGCQVTGKLL QTHLTKEGES VRLNQVNVDF QVDTSSDSPF LILPLTFYHV VDDASPFRDM
     ALRTGEGDFE LVVILSGTVE STSATCQVRT SYLPEEILWG YEFTPAISLS ASGKYVADFS
     LFDQVVKVTA PCCLHETVRF GDPEKVKLEE SLREAAERER EGAPLSVRIS NV
//
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