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Database: UniProt
Entry: A0A1V4JEL6_PATFA
LinkDB: A0A1V4JEL6_PATFA
Original site: A0A1V4JEL6_PATFA 
ID   A0A1V4JEL6_PATFA        Unreviewed;       421 AA.
AC   A0A1V4JEL6;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   31-JUL-2019, entry version 13.
DE   SubName: Full=ATP-sensitive inward rectifier potassium channel 8 {ECO:0000313|EMBL:OPJ70631.1};
GN   Name=KCNJ8 {ECO:0000313|EMBL:OPJ70631.1};
GN   ORFNames=AV530_008888 {ECO:0000313|EMBL:OPJ70631.1};
OS   Patagioenas fasciata monilis.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Columbiformes; Columbidae;
OC   Patagioenas.
OX   NCBI_TaxID=372326 {ECO:0000313|EMBL:OPJ70631.1, ECO:0000313|Proteomes:UP000190648};
RN   [1] {ECO:0000313|EMBL:OPJ70631.1, ECO:0000313|Proteomes:UP000190648}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BTP2013 {ECO:0000313|EMBL:OPJ70631.1};
RC   TISSUE=Blood {ECO:0000313|EMBL:OPJ70631.1};
RA   Soares A.E., Novak B.J., Rice E.S., O'Connell B., Chang D., Weber S.,
RA   Shapiro B.;
RT   "Band-tailed pigeon sequencing and assembly.";
RL   Submitted (FEB-2016) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:OPJ70631.1}.
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DR   EMBL; LSYS01007836; OPJ70631.1; -; Genomic_DNA.
DR   Proteomes; UP000190648; Unassembled WGS sequence.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0015272; F:ATP-activated 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; IPR003278; K_chnl_inward-rec_Kir6.1.
DR   InterPro; IPR013518; K_chnl_inward-rec_Kir_cyto.
DR   InterPro; IPR040445; Kir_TM.
DR   PANTHER; PTHR11767; PTHR11767; 1.
DR   PANTHER; PTHR11767:SF11; PTHR11767:SF11; 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; SSF81296; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000190648};
KW   Ion channel {ECO:0000256|RuleBase:RU003822,
KW   ECO:0000256|SAAS:SAAS00434609, ECO:0000313|EMBL:OPJ70631.1};
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   Reference proteome {ECO:0000313|Proteomes:UP000190648};
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     73     94       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    151    175       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN       37    180       IRK. {ECO:0000259|Pfam:PF01007}.
FT   DOMAIN      188    358       IRK_C. {ECO:0000259|Pfam:PF17655}.
FT   REGION      372    402       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   COMPBIAS    387    402       Polar. {ECO:0000256|SAM:MobiDB-lite}.
FT   SITE        167    167       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   421 AA;  47598 MW;  5AA7B9559220D8BB 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 PLIICHIIDK RSPLYDISAA DLALQDLELI VILEGVVETT
     GITTQARTSY IAEEILWGHR FVPIVTEEEG VYSVDYSKFG NTVKVAAPRC SARELDEKPS
     ILIQTLQKSE LSHQNSLRKR NSMRRNNSIR RSNSMRRTNP SLIVPKVQFM TPEGSQSASE
     T
//
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