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Database: UniProt
Entry: A0A218UTL0_9PASE
LinkDB: A0A218UTL0_9PASE
Original site: A0A218UTL0_9PASE 
ID   A0A218UTL0_9PASE        Unreviewed;       401 AA.
AC   A0A218UTL0;
DT   27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT   27-SEP-2017, sequence version 1.
DT   16-OCT-2019, entry version 13.
DE   SubName: Full=ATP-sensitive inward rectifier potassium channel 11 {ECO:0000313|EMBL:OWK57103.1};
GN   Name=KCNJ11 {ECO:0000313|EMBL:OWK57103.1};
GN   ORFNames=RLOC_00013473 {ECO:0000313|EMBL:OWK57103.1};
OS   Lonchura striata domestica (Bengalese finch).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea;
OC   Estrildidae; Estrildinae; Lonchura.
OX   NCBI_TaxID=299123 {ECO:0000313|EMBL:OWK57103.1, ECO:0000313|Proteomes:UP000197619};
RN   [1] {ECO:0000313|EMBL:OWK57103.1, ECO:0000313|Proteomes:UP000197619}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=White83orange57 {ECO:0000313|EMBL:OWK57103.1};
RA   Colquitt B.M., Brainard M.S.;
RT   "Genome of assembly of the Bengalese finch, Lonchura striata
RT   domestica.";
RL   Submitted (MAY-2017) 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:OWK57103.1}.
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DR   EMBL; MUZQ01000133; OWK57103.1; -; Genomic_DNA.
DR   Ensembl; ENSLSDT00000011812; ENSLSDP00000010266; ENSLSDG00000007570.
DR   Proteomes; UP000197619; Unassembled WGS sequence.
DR   GO; GO:0008282; C:inward rectifying potassium channel; IEA:Ensembl.
DR   GO; GO:0030315; C:T-tubule; IEA:Ensembl.
DR   GO; GO:0030506; F:ankyrin binding; IEA:Ensembl.
DR   GO; GO:0005524; F:ATP binding; IEA:Ensembl.
DR   GO; GO:0015272; F:ATP-activated inward rectifier potassium channel activity; IEA:Ensembl.
DR   GO; GO:0044325; F:ion channel binding; IEA:Ensembl.
DR   GO; GO:0006006; P:glucose metabolic process; IEA:Ensembl.
DR   GO; GO:0046676; P:negative regulation of insulin secretion; IEA:Ensembl.
DR   GO; GO:0050877; P:nervous system process; IEA:Ensembl.
DR   GO; GO:1990573; P:potassium ion import across plasma membrane; IEA:Ensembl.
DR   GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
DR   GO; GO:0042391; P:regulation of membrane potential; IEA:Ensembl.
DR   GO; GO:0033198; P:response to ATP; IEA:Ensembl.
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; IPR003279; K_chnl_inward-rec_Kir6.2.
DR   InterPro; IPR013518; K_chnl_inward-rec_Kir_cyto.
DR   InterPro; IPR040445; Kir_TM.
DR   PANTHER; PTHR11767; PTHR11767; 1.
DR   PANTHER; PTHR11767:SF44; PTHR11767:SF44; 1.
DR   Pfam; PF01007; IRK; 1.
DR   Pfam; PF17655; IRK_C; 1.
DR   PIRSF; PIRSF005465; GIRK_kir; 1.
DR   PRINTS; PR01332; KIR62CHANNEL.
DR   PRINTS; PR01320; KIRCHANNEL.
DR   SUPFAM; SSF81296; SSF81296; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000197619};
KW   Ion channel {ECO:0000256|RuleBase:RU003822,
KW   ECO:0000256|SAAS:SAAS00434609, ECO:0000313|EMBL:OWK57103.1};
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:UP000197619};
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    161    184       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN       37    189       IRK. {ECO:0000259|Pfam:PF01007}.
FT   DOMAIN      197    369       IRK_C. {ECO:0000259|Pfam:PF17655}.
FT   SITE        176    176       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   401 AA;  44881 MW;  E3AA878E5CEBB28E CRC64;
     MLSRKGIIPE EYVLTRLAED VPDHARYRAR ERRARFVGKN GACNVAHKNI REQGRFLQDV
     FTTLVDLKWP HTLLIFTMSF LCSWLLFGMV WWLIAFAHGD LDHSTRLQRD PAEGAAAGSA
     AAFVPCVTSI HSFTSAFLFS IEVQVTIGFG GRMVTEECPA AILVLIVQNI VGLVINAIML
     GCIFMKTSQA HRRAETLIFS KHAVIALREG RLCFMLRVGD LRKSMIISAT IRMQVVKKTA
     SLEGEVVPLN QIDIQMENPV GGNSIFLVSP LIIYHVIDKN SPLYDISPMN LHHHEDLEII
     VILEGVVETT GITTQARTSY LADEILWGQR FVPIVAEEDG RYSVDYSKFG NTVKVPTPSC
     TARQLEEDKS IMDTMPLSPK GTIRKRSVKL KPKFTISEEP S
//
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