ID Q6PFU3_DANRE Unreviewed; 448 AA.
AC Q6PFU3;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 113.
DE SubName: Full=Potassium channel subfamily K member 5 {ECO:0000313|RefSeq:NP_956927.1};
DE SubName: Full=Potassium channel, subfamily K, member 5 {ECO:0000313|EMBL:AAH57416.1};
GN Name=kcnk5b {ECO:0000313|RefSeq:NP_956927.1,
GN ECO:0000313|ZFIN:ZDB-GENE-040426-1297};
GN Synonyms=kcnk5 {ECO:0000313|EMBL:AAH57416.1}, zgc:63921
GN {ECO:0000313|RefSeq:NP_956927.1};
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955 {ECO:0000313|EMBL:AAH57416.1};
RN [1] {ECO:0000313|RefSeq:NP_956927.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=24173565;
RA Haffter P., Odenthal J., Mullins M.C., Lin S., Farrell M.J., Vogelsang E.,
RA Haas F., Brand M., van Eeden F.J., Furutani-Seiki M., Granato M.,
RA Hammerschmidt M., Heisenberg C.P., Jiang Y.J., Kane D.A., Kelsh R.N.,
RA Hopkins N., Nusslein-Volhard C.;
RT "Mutations affecting pigmentation and shape of the adult zebrafish.";
RL Dev. Genes Evol. 206:260-276(1996).
RN [2] {ECO:0000313|RefSeq:NP_956927.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=11748827;
RA Dickmeis T., Aanstad P., Clark M., Fischer N., Herwig R., Mourrain P.,
RA Blader P., Rosa F., Lehrach H., Strahle U.;
RT "Identification of nodal signaling targets by array analysis of induced
RT complex probes.";
RL Dev. Dyn. 222:571-580(2001).
RN [3] {ECO:0000313|EMBL:AAH57416.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney {ECO:0000313|EMBL:AAH57416.1};
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|RefSeq:NP_956927.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=21963410;
RA Gierten J., Hassel D., Schweizer P.A., Becker R., Katus H.A., Thomas D.;
RT "Identification and functional characterization of zebrafish K(2P)10.1
RT (TREK2) two-pore-domain K(+) channels.";
RL Biochim. Biophys. Acta 1818:33-41(2012).
RN [5] {ECO:0000313|Proteomes:UP000000437}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23594743; DOI=10.1038/nature12111;
RG Genome Reference Consortium Zebrafish;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., 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., Eliott D.,
RA Threadgold G., Harden G., Ware D., Begum S., Mortimore B., Mortimer B.,
RA Kerry G., Heath P., Phillimore B., Tracey A., Corby N., Dunn M.,
RA Johnson C., Wood J., Clark S., Pelan S., Griffiths G., Smith M.,
RA Glithero R., Howden P., Barker N., Lloyd C., Stevens C., Harley J.,
RA Holt K., Panagiotidis G., Lovell J., Beasley H., Henderson C., Gordon D.,
RA Auger K., Wright D., Collins J., Raisen C., Dyer L., Leung K.,
RA Robertson L., Ambridge K., Leongamornlert D., McGuire S., Gilderthorp R.,
RA Griffiths C., Manthravadi D., Nichol S., Barker G., Whitehead S., Kay M.,
RA Brown J., Murnane C., Gray E., Humphries M., Sycamore N., Barker D.,
RA Saunders D., Wallis J., Babbage A., Hammond S., Mashreghi-Mohammadi M.,
RA Barr L., Martin S., Wray P., Ellington A., Matthews N., Ellwood M.,
RA Woodmansey R., Clark G., Cooper J., Cooper J., Tromans A., Grafham D.,
RA Skuce C., Pandian R., Andrews R., Harrison E., Kimberley A., Garnett J.,
RA Fosker N., Hall R., Garner P., Kelly D., Bird C., Palmer S., Gehring I.,
RA Berger A., Dooley C.M., Ersan-Urun Z., Eser C., Geiger H., Geisler M.,
RA Karotki L., Kirn A., Konantz J., Konantz M., Oberlander M.,
RA Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G., Osoegawa K., Zhu B.,
RA Rapp A., Widaa S., Langford C., Yang F., Schuster S.C., Carter N.P.,
RA Harrow J., Ning Z., Herrero J., Searle S.M., Enright A., Geisler R.,
RA Plasterk R.H., Lee C., Westerfield M., de Jong P.J., Zon L.I.,
RA Postlethwait J.H., Nusslein-Volhard C., Hubbard T.J., Roest Crollius H.,
RA Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [6] {ECO:0000313|RefSeq:NP_956927.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=24081451;
RA Pena-Munzenmayer G., Niemeyer M.I., Sepulveda F.V., Cid L.P.;
RT "Zebrafish and mouse TASK-2 K(+) channels are inhibited by increased CO2
RT and intracellular acidification.";
RL Pflugers Arch. 466:1317-1327(2014).
RN [7] {ECO:0000313|RefSeq:NP_956927.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=24453984;
RA Perathoner S., Daane J.M., Henrion U., Seebohm G., Higdon C.W.,
RA Johnson S.L., Nusslein-Volhard C., Harris M.P.;
RT "Bioelectric signaling regulates size in zebrafish fins.";
RL PLoS Genet. 10:e1004080-e1004080(2014).
RN [8] {ECO:0000313|RefSeq:NP_956927.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=26469318;
RA Elkon R., Milon B., Morrison L., Shah M., Vijayakumar S., Racherla M.,
RA Leitch C.C., Silipino L., Hadi S., Weiss-Gayet M., Barras E., Schmid C.D.,
RA Ait-Lounis A., Barnes A., Song Y., Eisenman D.J., Eliyahu E.,
RA Frolenkov G.I., Strome S.E., Durand B., Zaghloul N.A., Jones S.M.,
RA Reith W., Hertzano R.;
RT "RFX transcription factors are essential for hearing in mice.";
RL Nat. Commun. 6:8549-8549(2015).
RN [9] {ECO:0000313|RefSeq:NP_956927.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=29991812;
RA Daane J.M., Lanni J., Rothenberg I., Seebohm G., Higdon C.W., Johnson S.L.,
RA Harris M.P.;
RT "Bioelectric-calcineurin signaling module regulates allometric growth and
RT size of the zebrafish fin.";
RL Sci. Rep. 8:10391-10391(2018).
RN [10] {ECO:0000313|RefSeq:NP_956927.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the two pore domain potassium channel (TC
CC 1.A.1.8) family. {ECO:0000256|ARBA:ARBA00006666,
CC ECO:0000256|RuleBase:RU003857}.
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DR EMBL; BC057416; AAH57416.1; -; mRNA.
DR RefSeq; NP_956927.1; NM_200633.1.
DR GeneID; 393606; -.
DR KEGG; dre:393606; -.
DR AGR; ZFIN:ZDB-GENE-040426-1297; -.
DR CTD; 393606; -.
DR ZFIN; ZDB-GENE-040426-1297; kcnk5b.
DR OrthoDB; 600333at2759; -.
DR PhylomeDB; Q6PFU3; -.
DR Proteomes; UP000000437; Chromosome 20.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015271; F:outward rectifier potassium channel activity; IDA:ZFIN.
DR GO; GO:0022841; F:potassium ion leak channel activity; IBA:GO_Central.
DR GO; GO:0033333; P:fin development; IMP:ZFIN.
DR GO; GO:0033334; P:fin morphogenesis; IMP:ZFIN.
DR GO; GO:0071805; P:potassium ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0042391; P:regulation of membrane potential; IDA:ZFIN.
DR GO; GO:0030322; P:stabilization of membrane potential; IBA:GO_Central.
DR Gene3D; 1.10.287.70; -; 1.
DR InterPro; IPR003280; 2pore_dom_K_chnl.
DR InterPro; IPR003092; 2pore_dom_K_chnl_TASK.
DR InterPro; IPR013099; K_chnl_dom.
DR PANTHER; PTHR11003; POTASSIUM CHANNEL, SUBFAMILY K; 1.
DR PANTHER; PTHR11003:SF295; POTASSIUM CHANNEL, SUBFAMILY K, MEMBER 5; 1.
DR Pfam; PF07885; Ion_trans_2; 2.
DR PRINTS; PR01333; 2POREKCHANEL.
DR PRINTS; PR01095; TASKCHANNEL.
DR SUPFAM; SSF81324; Voltage-gated potassium channels; 2.
PE 2: Evidence at transcript level;
KW Ion channel {ECO:0000256|RuleBase:RU003857, ECO:0000313|EMBL:AAH57416.1};
KW Ion transport {ECO:0000256|RuleBase:RU003857};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Potassium {ECO:0000256|ARBA:ARBA00022958};
KW Potassium channel {ECO:0000256|ARBA:ARBA00022826};
KW Potassium transport {ECO:0000256|ARBA:ARBA00022538};
KW Reference proteome {ECO:0000313|Proteomes:UP000000437};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU003857};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU003857}.
FT TRANSMEM 7..26
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 116..137
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 158..185
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 229..250
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 75..137
FT /note="Potassium channel"
FT /evidence="ECO:0000259|Pfam:PF07885"
FT DOMAIN 173..246
FT /note="Potassium channel"
FT /evidence="ECO:0000259|Pfam:PF07885"
FT REGION 382..448
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 382..402
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 409..431
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 432..448
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 448 AA; 50823 MW; A5437FAB7930A1B8 CRC64;
MADKGPILTS VIIFYLSIGA AIFQILEEPN LNSAVDDYKN KTNNLLKKYP CLSKEVLGEI
IEVVAEATGQ GVTVTKEAQF NNWNWENAVI FAATVITTIG YGNVAPKTTG GRLFCILYGL
CGIPLCLTWI SELGTFFGSR TKRLSQLLLH SGLNVRKVQF ICTIVFLLWG FLVHLIIPAF
VFMFFENWTY LEGLYFSFTT LTTVGFGDYV AGVDPSVNYP TLYRFFVQLW IYLGLAWLSL
FFSWNVHMVV EAHKVLKKRR MRRHRLPTDD VPEKKEVKKT PKPPPRSGVI DIFEFMSEKV
EDYSDVIRAI GADEKRRKKK QEEELARSKS CSDLLQGLVI PLDHSPRLQR RFSVSANMCM
AISDESVDGL NNNNCKQEDD TLTKVRHKDQ KVNRERAENP ARCAWDSRSS DPSIFQSSTV
TNSTNRGSRF SVSKVSEDRS LGKRKSFG
//
