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Entry: A0A093C3A7_9AVES
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ID   A0A093C3A7_9AVES        Unreviewed;       427 AA.
AC   A0A093C3A7;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 39.
DE   RecName: Full=Inward rectifier potassium channel 2 {ECO:0000256|ARBA:ARBA00013754};
DE   AltName: Full=Inward rectifier K(+) channel Kir2.1 {ECO:0000256|ARBA:ARBA00032763};
DE   AltName: Full=Potassium channel, inwardly rectifying subfamily J member 2 {ECO:0000256|ARBA:ARBA00031391};
GN   ORFNames=N339_06730 {ECO:0000313|EMBL:KFV08918.1};
OS   Pterocles gutturalis (yellow-throated sandgrouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Ciconiiformes; Pteroclidae; Pterocles.
OX   NCBI_TaxID=240206 {ECO:0000313|EMBL:KFV08918.1, ECO:0000313|Proteomes:UP000053149};
RN   [1] {ECO:0000313|EMBL:KFV08918.1, ECO:0000313|Proteomes:UP000053149}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N339 {ECO:0000313|EMBL:KFV08918.1};
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:ARBA00004635}; Lipid-
CC       anchor {ECO:0000256|ARBA:ARBA00004635}. 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. KCNJ2 subfamily. {ECO:0000256|ARBA:ARBA00008162}.
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DR   EMBL; KL236122; KFV08918.1; -; Genomic_DNA.
DR   RefSeq; XP_010074221.1; XM_010075919.1.
DR   AlphaFoldDB; A0A093C3A7; -.
DR   GeneID; 104463543; -.
DR   KEGG; pguu:104463543; -.
DR   CTD; 3759; -.
DR   OrthoDB; 4126787at2759; -.
DR   Proteomes; UP000053149; 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; IPR003271; K_chnl_inward-rec_Kir2.1.
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; INWARD RECTIFIER POTASSIUM CHANNEL; 1.
DR   PANTHER; PTHR11767:SF43; INWARD RECTIFIER POTASSIUM CHANNEL 2; 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; PR01324; KIR21CHANNEL.
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   Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Myristate {ECO:0000256|ARBA:ARBA00022707};
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:UP000053149};
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        83..107
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        156..181
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          1..47
FT                   /note="Potassium channel inwardly rectifying Kir N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08466"
FT   DOMAIN          48..186
FT                   /note="Potassium channel inwardly rectifying transmembrane"
FT                   /evidence="ECO:0000259|Pfam:PF01007"
FT   DOMAIN          193..365
FT                   /note="Inward rectifier potassium channel C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17655"
FT   REGION          386..427
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            172
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   427 AA;  48548 MW;  3371E79776C20056 CRC64;
     MGSVRTNRYS IVSSEEDGMK LATMAVANGF GNGKSKVHTR QQCRSRFVKK DGHCNVQFIN
     VGEKGQRYLA DIFTTCVDIR WRWMLVIFCL TFILSWLFFG CVFWLIALLH GDLENQENNK
     PCVSQVSSFT AAFLFSIETQ TTIGYGFRCV TDECPIAVFM VVFQSIVGCI IDAFIIGAVM
     AKMAKPKKRN ETLVFSHNAV VAMRDGKLCL MWRVGNLRKS HLVEAHVRAQ LLKSRITSEG
     EYIPLDQIDI NVGFDSGIDR IFLVSPITIV HEIDEDSPLY DLSKQDMDNA DFEIVVILEG
     MVEATAMTTQ CRSSYLANEI LWGHRYEPVL FEEKNYYKVD YSRFHKTYEV PNTPICSARD
     LAEKKYILSN ANSFCYENEV ALTSKEEDEI DTGVPESMST DTHPDMDHHN QAGVPLEPRP
     LRRESEI
//
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