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Database: UniProt
Entry: A0A093PMC1_PYGAD
LinkDB: A0A093PMC1_PYGAD
Original site: A0A093PMC1_PYGAD 
ID   A0A093PMC1_PYGAD        Unreviewed;       421 AA.
AC   A0A093PMC1;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 37.
DE   SubName: Full=ATP-sensitive inward rectifier potassium channel 8 {ECO:0000313|EMBL:KFW73327.1};
GN   ORFNames=AS28_09023 {ECO:0000313|EMBL:KFW73327.1};
OS   Pygoscelis adeliae (Adelie penguin).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Sphenisciformes; Spheniscidae; Pygoscelis.
OX   NCBI_TaxID=9238 {ECO:0000313|EMBL:KFW73327.1, ECO:0000313|Proteomes:UP000054081};
RN   [1] {ECO:0000313|EMBL:KFW73327.1, ECO:0000313|Proteomes:UP000054081}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_AS28 {ECO:0000313|EMBL:KFW73327.1};
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; KL225530; KFW73327.1; -; Genomic_DNA.
DR   RefSeq; XP_009331099.1; XM_009332824.1.
DR   AlphaFoldDB; A0A093PMC1; -.
DR   STRING; 9238.A0A093PMC1; -.
DR   GeneID; 103924328; -.
DR   KEGG; padl:103924328; -.
DR   CTD; 3764; -.
DR   OrthoDB; 4126787at2759; -.
DR   Proteomes; UP000054081; Unassembled WGS sequence.
DR   GO; GO:0034702; C:monoatomic ion channel complex; IEA:UniProtKB-KW.
DR   GO; GO:0015272; F:ATP-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; IPR003278; K_chnl_inward-rec_Kir6.1.
DR   InterPro; IPR013518; K_chnl_inward-rec_Kir_cyto.
DR   InterPro; IPR040445; Kir_TM.
DR   PANTHER; PTHR11767:SF11; ATP-SENSITIVE INWARD RECTIFIER POTASSIUM CHANNEL 8; 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; PR01331; KIR61CHANNEL.
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:UP000054081};
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        73..94
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        151..175
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          37..180
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          372..403
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        387..403
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   421 AA;  47591 MW;  B6EBE614AE520CF0 CRC64;
     MLARKSIIPE EYVLARIAAE NLRKPRIRDR PRKARFIAKN GACNLAHKNI REQGRFLQDI
     FTTLVDLKWR HTLVIFTMSF LCSWLLFAMM WWLVAFAHGD MDPSTESTTN STKWTPCVTC
     VRSFTSAFLF SIEVQVTIGF GGRMMTEECP LAITVLILQN IVGLIINAVM LGCIFMKTAQ
     AHRRAETLIF SRQAVIAVRN GKLCFMFRVG DLRKSMIISA SVRIQVVRKT TTPEGEVIPI
     HQVDIPVDNP IESNNIFLVA PLIICHVIDK RSPLYDISAA DLALQDLELI VILEGVVETT
     GITTQARTSY IAEEILWGHR FVPIVTEEEG VYAVDYSKFG NTIKVAAPRC SARELDEKPS
     ILIQTLQKSE LSHQNSLRKR NSMRRNNSIR RSNSMRRTNP SLIVPKVQFI TPEGNQSASE
     T
//
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