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Database: UniProt
Entry: Q5RH88_DANRE
LinkDB: Q5RH88_DANRE
Original site: Q5RH88_DANRE 
ID   Q5RH88_DANRE            Unreviewed;       416 AA.
AC   Q5RH88;
DT   21-DEC-2004, integrated into UniProtKB/TrEMBL.
DT   21-DEC-2004, sequence version 1.
DT   16-OCT-2019, entry version 123.
DE   SubName: Full=Kir6.1 like {ECO:0000313|EMBL:BAE79476.1};
DE   SubName: Full=Potassium inwardly rectifying channel subfamily J member 8 {ECO:0000313|Ensembl:ENSDARP00000067030};
DE   SubName: Full=Potassium inwardly-rectifying channel, subfamily J, member 8 {ECO:0000313|EMBL:AAI63413.1};
GN   Name=kcnj8 {ECO:0000313|EMBL:AAI63413.1,
GN   ECO:0000313|Ensembl:ENSDARP00000067030,
GN   ECO:0000313|ZFIN:ZDB-GENE-060308-1};
GN   Synonyms=zKir6.1 {ECO:0000313|EMBL:BAE79476.1};
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Cyprinidae; Danio.
OX   NCBI_TaxID=7955 {ECO:0000313|Ensembl:ENSDARP00000067030, ECO:0000313|Proteomes:UP000000437};
RN   [1] {ECO:0000313|EMBL:BAE79476.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=16317080; DOI=10.1152/physiolgenomics.00228.2005;
RA   Zhang C., Miki T., Shibasaki T., Yokokura M., Saraya A., Seino S.;
RT   "Identification and characterization of a novel member of the ATP-
RT   sensitive K+ channel subunit family, Kir6.3, in zebrafish.";
RL   Physiol. Genomics 24:290-297(2006).
RN   [2] {ECO:0000313|EMBL:AAI63413.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|Ensembl:ENSDARP00000067030, ECO:0000313|Proteomes:UP000000437}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000067030,
RC   ECO:0000313|Proteomes:UP000000437};
RX   PubMed=23594743; DOI=10.1038/nature12111;
RA   Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C.,
RA   Muffato M., Collins J.E., Humphray S., McLaren K., Matthews L.,
RA   McLaren S., Sealy I., Caccamo M., Churcher C., Scott C., Barrett J.C.,
RA   Koch R., Rauch G.J., White S., Chow W., Kilian B., Quintais L.T.,
RA   Guerra-Assuncao J.A., Zhou Y., Gu Y., Yen J., Vogel J.H., Eyre T.,
RA   Redmond S., Banerjee R., Chi J., Fu B., Langley E., Maguire S.F.,
RA   Laird G.K., Lloyd D., Kenyon E., Donaldson S., Sehra H.,
RA   Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA   Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA   Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA   Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA   Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J.,
RA   Clark S., Pelan S., Griffiths G., Smith M., Glithero R., Howden P.,
RA   Barker N., Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G.,
RA   Lovell J., Beasley H., Henderson C., Gordon D., Auger K., Wright D.,
RA   Collins J., Raisen C., Dyer L., Leung K., Robertson L., Ambridge K.,
RA   Leongamornlert D., McGuire S., Gilderthorp R., Griffiths C.,
RA   Manthravadi D., Nichol S., Barker G., Whitehead S., Kay M., Brown J.,
RA   Murnane C., Gray E., Humphries M., Sycamore N., Barker D.,
RA   Saunders D., Wallis J., Babbage A., Hammond S.,
RA   Mashreghi-Mohammadi M., Barr L., Martin S., Wray P., Ellington A.,
RA   Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA   Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA   Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D.,
RA   Bird C., Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z.,
RA   Eser C., Geiger H., Geisler M., Karotki L., Kirn A., Konantz J.,
RA   Konantz M., Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C.,
RA   Raddatz G., Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C.,
RA   Yang F., Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J.,
RA   Searle S.M., Enright A., Geisler R., Plasterk R.H., Lee C.,
RA   Westerfield M., de Jong P.J., Zon L.I., Postlethwait J.H.,
RA   Nusslein-Volhard C., Hubbard T.J., Roest Crollius H., Rogers J.,
RA   Stemple D.L.;
RT   "The zebrafish reference genome sequence and its relationship to the
RT   human genome.";
RL   Nature 496:498-503(2013).
RN   [4] {ECO:0000313|Ensembl:ENSDARP00000067030}
RP   IDENTIFICATION.
RC   STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000067030};
RG   Ensembl;
RL   Submitted (AUG-2013) 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; BX571719; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC163413; AAI63413.1; -; mRNA.
DR   EMBL; BC163434; AAI63434.1; -; mRNA.
DR   EMBL; AB231936; BAE79476.1; -; mRNA.
DR   RefSeq; NP_001025324.1; NM_001030153.1.
DR   STRING; 7955.ENSDARP00000067030; -.
DR   Ensembl; ENSDART00000067031; ENSDARP00000067030; ENSDARG00000045589.
DR   GeneID; 561090; -.
DR   KEGG; dre:561090; -.
DR   CTD; 3764; -.
DR   ZFIN; ZDB-GENE-060308-1; kcnj8.
DR   eggNOG; KOG3827; Eukaryota.
DR   eggNOG; ENOG410XQ62; LUCA.
DR   GeneTree; ENSGT00970000193347; -.
DR   HOGENOM; HOG000237325; -.
DR   KO; K05001; -.
DR   OMA; CPTAITV; -.
DR   OrthoDB; 956263at2759; -.
DR   TreeFam; TF313676; -.
DR   Reactome; R-DRE-1296025; ATP sensitive Potassium channels.
DR   Proteomes; UP000000437; Chromosome 4.
DR   Bgee; ENSDARG00000045589; Expressed in 11 organ(s), highest expression level in liver.
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:0005242; F:inward rectifier potassium channel activity; IBA:GO_Central.
DR   GO; GO:1990573; P:potassium ion import across plasma membrane; IBA:GO_Central.
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   2: Evidence at transcript level;
KW   Complete proteome {ECO:0000313|Proteomes:UP000000437};
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:UP000000437};
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     71     94       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    146    170       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN       37    175       IRK. {ECO:0000259|Pfam:PF01007}.
FT   DOMAIN      183    353       IRK_C. {ECO:0000259|Pfam:PF17655}.
FT   REGION      366    392       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   SITE        162    162       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   416 AA;  46831 MW;  762BCF8E3368363A CRC64;
     MLPRKSIIPE EFALPALVSR VPRKPVFRDR VNKARFIAKS GACNLAHKNI REQGRFLQDV
     FTTLVDLKWR FTLVIFTMTF LCSWLLFAMS WWLVAFGHGD LDTDRKPAVE QCVTNVNSFT
     SAFLFSIEVQ VTIGFGGRMI TERCPIAIAF LILQNIIGLI INAVMLGCIF MKTAQSHRRA
     ETLIFSRHAV IAVRNNRLCF MIRVGDLRKS MIINAVVRLQ VVRKTMTPEG EVIPIQQIDV
     QTESAVAGNS IFLLAPLIIC HVIDKDSPLY DLSAMELQCS DLEVIVILEG VVETTGITTQ
     ARTSYVTEEI QWGHRFVPIV TEEEGVYSVD YSKFGNTVKV ATPRCSAREL DEKPSILIQT
     LQKSELSHQN SLRKRNSMRR NNSMRKGNSM RRNNSALAVP KVQFLTPEGG ANLAVT
//
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