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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//