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Database: UniProt
Entry: A0A2I3GSH9_NOMLE
LinkDB: A0A2I3GSH9_NOMLE
Original site: A0A2I3GSH9_NOMLE 
ID   A0A2I3GSH9_NOMLE        Unreviewed;       420 AA.
AC   A0A2I3GSH9;
DT   28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT   28-FEB-2018, sequence version 1.
DT   18-SEP-2019, entry version 12.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSNLEP00000034293};
GN   Name=KCNJ1 {ECO:0000313|Ensembl:ENSNLEP00000034293};
OS   Nomascus leucogenys (Northern white-cheeked gibbon) (Hylobates
OS   leucogenys).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hylobatidae; Nomascus.
OX   NCBI_TaxID=61853 {ECO:0000313|Ensembl:ENSNLEP00000034293, ECO:0000313|Proteomes:UP000001073};
RN   [1] {ECO:0000313|Ensembl:ENSNLEP00000034293, ECO:0000313|Proteomes:UP000001073}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   Gibbon Genome Sequencing Consortium;
RL   Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSNLEP00000034293}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (JAN-2018) to UniProtKB.
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; ADFV01057717; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ADFV01057718; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ADFV01057719; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ADFV01057720; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ADFV01057721; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ADFV01057722; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   Ensembl; ENSNLET00000050678; ENSNLEP00000034293; ENSNLEG00000007480.
DR   GeneTree; ENSGT00970000193347; -.
DR   Proteomes; UP000001073; Chromosome 15.
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:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IEA:Ensembl.
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; IPR003268; K_chnl_inward-rec_Kir1.1.
DR   InterPro; IPR013518; K_chnl_inward-rec_Kir_cyto.
DR   InterPro; IPR040445; Kir_TM.
DR   PANTHER; PTHR11767; PTHR11767; 1.
DR   PANTHER; PTHR11767:SF6; PTHR11767:SF6; 1.
DR   Pfam; PF01007; IRK; 1.
DR   Pfam; PF17655; IRK_C; 1.
DR   PIRSF; PIRSF005465; GIRK_kir; 1.
DR   PRINTS; PR01320; KIRCHANNEL.
DR   SUPFAM; SSF81296; SSF81296; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000001073};
KW   Ion channel {ECO:0000256|RuleBase:RU003822,
KW   ECO:0000256|SAAS:SAAS00434609};
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:UP000001073};
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    112    134       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    185    209       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN       72    214       IRK. {ECO:0000259|Pfam:PF01007}.
FT   DOMAIN      221    392       IRK_C. {ECO:0000259|Pfam:PF17655}.
FT   SITE        200    200       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   420 AA;  48264 MW;  D2FA5D7ED04CC4C0 CRC64;
     MLMRLVLRAH LSSTTSLPWT HAAISWELDN VLMPRPRIWP QIRVLTESML KHLRKWVVTR
     FFGHSRQRAR LVSKDGRCNI EFGNVEAQSR FIFFVDIWTT VLDLKWRYKM TIFITAFLGS
     WFFFGLLWYT VAYIHKDLPE FHPSANHTPC VENINGLTSA FLFSLETQVT IGYGFRCVTE
     QCATAIFLLI FQSILGVIIN SFMCGAILAK ISRPKKRAKT ITFSKNAVIS KRGGKLCLLI
     RVANLRKSLL IGSHIYGKLL KTTVTPEGET IILDQININF VVDTGNENLF FISPLTIYHV
     IDHNSPFFHM AAETLLQQDF ELVVFLDGTV ESTSATCQVR TSYVPEEVLW GYRFAPIVSK
     TKEGKYRVDF HNFSKTVEVE TPHCAMCLYN EKDARARMKR GYDNPNFILS EVNETDDTKM
//
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