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Database: UniProt
Entry: A0A087VQ27_BALRE
LinkDB: A0A087VQ27_BALRE
Original site: A0A087VQ27_BALRE 
ID   A0A087VQ27_BALRE        Unreviewed;       425 AA.
AC   A0A087VQ27;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   11-DEC-2019, entry version 27.
DE   SubName: Full=ATP-sensitive inward rectifier potassium channel 12 {ECO:0000313|EMBL:KFO14719.1};
DE   Flags: Fragment;
GN   ORFNames=N312_05438 {ECO:0000313|EMBL:KFO14719.1};
OS   Balearica regulorum gibbericeps (East African grey crowned-crane).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Gruiformes; Gruidae; Balearica.
OX   NCBI_TaxID=100784 {ECO:0000313|EMBL:KFO14719.1, ECO:0000313|Proteomes:UP000053309};
RN   [1] {ECO:0000313|EMBL:KFO14719.1, ECO:0000313|Proteomes:UP000053309}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N312 {ECO:0000313|EMBL:KFO14719.1};
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}; Multi-
CC       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}.
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DR   EMBL; KL501440; KFO14719.1; -; Genomic_DNA.
DR   Proteomes; UP000053309; Unassembled WGS sequence.
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; IPR003272; K_chnl_inward-rec_Kir2.2.
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; PTHR11767; 1.
DR   PANTHER; PTHR11767:SF14; PTHR11767:SF14; 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; PR01325; KIR22CHANNEL.
DR   PRINTS; PR01320; KIRCHANNEL.
DR   SUPFAM; SSF81296; SSF81296; 1.
PE   3: Inferred from homology;
KW   Ion channel {ECO:0000256|RuleBase:RU003822, ECO:0000256|SAAS:SAAS00434609,
KW   ECO:0000313|EMBL:KFO14719.1};
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, 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, ECO:0000256|SAAS:SAAS00036755};
KW   Voltage-gated channel {ECO:0000256|RuleBase:RU003822,
KW   ECO:0000256|SAAS:SAAS00048561}.
FT   TRANSMEM        79..103
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        153..178
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          1..41
FT                   /note="IRK_N"
FT                   /evidence="ECO:0000259|Pfam:PF08466"
FT   DOMAIN          42..183
FT                   /note="IRK"
FT                   /evidence="ECO:0000259|Pfam:PF01007"
FT   DOMAIN          190..361
FT                   /note="IRK_C"
FT                   /evidence="ECO:0000259|Pfam:PF17655"
FT   REGION          382..404
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            169
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:KFO14719.1"
FT   NON_TER         425
FT                   /evidence="ECO:0000313|EMBL:KFO14719.1"
SQ   SEQUENCE   425 AA;  48751 MW;  976293EC3B52F48F CRC64;
     RVNPYSIVSS EEDGLRLTTM PGINGFGNGK IHTRRKCRNR FVKKNGQCNV EFTNMDDKPQ
     RYIADMFTTC VDIRWRYMLL LFSLAFLVSW LLFGLIFWLI ALIHGDLENP GGDDTFKPCV
     LQVNGFVAAF LFSIETQTTI GYGFRCVTEE CPLAVFMVVV QSIVGCIIDS FMIGAIMAKM
     ARPKKRAQTL LFSHNAVVAM RDGKLCLMWR VGNLRKSHIV EAHVRAQLIK PRITEEGEYI
     PLDQIDIDVG FDKGLDRIFL VSPITILHEI NEDSPLFGIS RQDLETDDFE IVVILEGMVE
     ATAMTTQARS SYLASEILWG HRFEPVLFEE KNQYKVDYSH FHKTYEVPST PRCSAKDLVE
     NKFLLPSTNS FCYENELAFM SRDEEEEDDD SRGLEDLSPD NRHEFDRLQA TIALDQRSYR
     RESEI
//
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