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Database: UniProt
Entry: A0A091GUJ8_BUCRH
LinkDB: A0A091GUJ8_BUCRH
Original site: A0A091GUJ8_BUCRH 
ID   A0A091GUJ8_BUCRH        Unreviewed;       377 AA.
AC   A0A091GUJ8;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   08-MAY-2019, entry version 22.
DE   SubName: Full=ATP-sensitive inward rectifier potassium channel 15 {ECO:0000313|EMBL:KFO86187.1};
GN   ORFNames=N320_06523 {ECO:0000313|EMBL:KFO86187.1};
OS   Buceros rhinoceros silvestris.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Bucerotiformes; Bucerotidae; Buceros.
OX   NCBI_TaxID=175836 {ECO:0000313|EMBL:KFO86187.1};
RN   [1] {ECO:0000313|EMBL:KFO86187.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N320 {ECO:0000313|EMBL:KFO86187.1};
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|RuleBase:RU003822};
CC       Multi-pass membrane protein {ECO:0000256|RuleBase:RU003822}.
CC   -!- SIMILARITY: Belongs to the inward rectifier-type potassium channel
CC       (TC 1.A.2.1) family. {ECO:0000256|RuleBase:RU003822,
CC       ECO:0000256|SAAS:SAAS00549381}.
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DR   EMBL; KL510203; KFO86187.1; -; Genomic_DNA.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005242; F:inward rectifier potassium channel activity; IEA:InterPro.
DR   GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.40.1400; -; 1.
DR   InterPro; IPR014756; Ig_E-set.
DR   InterPro; IPR041647; IRK_C.
DR   InterPro; IPR016449; K_chnl_inward-rec_Kir.
DR   InterPro; IPR003270; K_chnl_inward-rec_Kir1.3.
DR   InterPro; IPR013518; K_chnl_inward-rec_Kir_cyto.
DR   InterPro; IPR040445; Kir_TM.
DR   PANTHER; PTHR11767; PTHR11767; 1.
DR   PANTHER; PTHR11767:SF20; PTHR11767:SF20; 1.
DR   Pfam; PF01007; IRK; 1.
DR   Pfam; PF17655; IRK_C; 1.
DR   PIRSF; PIRSF005465; GIRK_kir; 1.
DR   PRINTS; PR01323; KIR13CHANNEL.
DR   PRINTS; PR01320; KIRCHANNEL.
DR   SUPFAM; SSF81296; SSF81296; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Ion channel {ECO:0000256|RuleBase:RU003822,
KW   ECO:0000256|SAAS:SAAS00434609, ECO:0000313|EMBL:KFO86187.1};
KW   Ion transport {ECO:0000256|RuleBase:RU003822,
KW   ECO:0000256|SAAS:SAAS00434639};
KW   Membrane {ECO:0000256|SAAS:SAAS00434581, ECO:0000256|SAM:Phobius};
KW   Potassium {ECO:0000256|RuleBase:RU003822,
KW   ECO:0000256|SAAS:SAAS00434575};
KW   Potassium transport {ECO:0000256|RuleBase:RU003822,
KW   ECO:0000256|SAAS:SAAS00434641};
KW   Transmembrane {ECO:0000256|RuleBase:RU003822,
KW   ECO:0000256|SAAS:SAAS00434543, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAAS:SAAS00036756,
KW   ECO:0000256|SAM:Phobius};
KW   Transport {ECO:0000256|RuleBase:RU003822,
KW   ECO:0000256|SAAS:SAAS00036755};
KW   Voltage-gated channel {ECO:0000256|RuleBase:RU003822,
KW   ECO:0000256|SAAS:SAAS00048561}.
FT   TRANSMEM     68     89       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    143    167       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN       31    172       IRK. {ECO:0000259|Pfam:PF01007}.
FT   DOMAIN      179    338       IRK_C. {ECO:0000259|Pfam:PF17655}.
FT   COILED      346    370       {ECO:0000256|SAM:Coils}.
FT   SITE        158    158       Role in the control of polyamine-mediated
FT                                channel gating and in the blocking by
FT                                intracellular magnesium.
FT                                {ECO:0000256|PIRSR:PIRSR005465-1}.
SQ   SEQUENCE   377 AA;  43271 MW;  54BAE227D14BFF2E CRC64;
     METTKINMSH VPLVNGGIDA AMLKAHKPRV MSKSGHSNVR IDKVDGIYLL YLQDLWTTVI
     DMKWRYKLTL FAATFVMTWF LFGVIYYAIA FLHGDLEINH FTPKREPCVK NVDSLTGAFL
     FSLESQTTIG YGFRFITEEC PHAIFLLVAQ LVITTLIEIF ITGTFLAKIA RPKKRAETIK
     FSHCAVITKH NGELCLVIRV ANMRKSLLIQ CQLSGKLLQT YETKEGERIP LNHATSVKFN
     VDSSSESPFL ILPLTFYHIL DESSPLRDLT PQNLKEKDFE LVVLLNATVE STSAVCQSRT
     SYIPEEIHWG YEFVPVVSLS PNGKYVADFS QFEKIRRSTD SIFYSMDSEK QRLEEKYRQE
     DQRERELRTM LLQQSNV
//
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