ID Q32PR9_DANRE Unreviewed; 513 AA. AC Q32PR9; DT 06-DEC-2005, integrated into UniProtKB/TrEMBL. DT 06-DEC-2005, sequence version 1. DT 27-MAR-2024, entry version 113. DE SubName: Full=Potassium channel subfamily K member 5 {ECO:0000313|RefSeq:NP_001032478.1}; DE SubName: Full=Zgc:123271 {ECO:0000313|EMBL:AAI08009.1}; GN Name=kcnk5a {ECO:0000313|ZFIN:ZDB-GENE-051113-112}; GN Synonyms=zgc:123271 {ECO:0000313|RefSeq:NP_001032478.1}; 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:AAI08009.1}; RN [1] {ECO:0000313|EMBL:AAI08009.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Testis {ECO:0000313|EMBL:AAI08009.1}; RG NIH - Zebrafish Gene Collection (ZGC) project; RL Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|RefSeq:NP_001032478.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=18202183; RA Asakawa K., Suster M.L., Mizusawa K., Nagayoshi S., Kotani T., Urasaki A., RA Kishimoto Y., Hibi M., Kawakami K.; RT "Genetic dissection of neural circuits by Tol2 transposon-mediated Gal4 RT gene and enhancer trapping in zebrafish."; RL Proc. Natl. Acad. Sci. U.S.A. 105:1255-1260(2008). RN [3] {ECO:0000313|RefSeq:NP_001032478.1} 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 [4] {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 [5] {ECO:0000313|RefSeq:NP_001032478.1} 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 [6] {ECO:0000313|RefSeq:NP_001032478.1} 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 [7] {ECO:0000313|RefSeq:NP_001032478.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=30324621; RA Samarut E., Swaminathan A., Riche R., Liao M., Hassan-Abdi R., Renault S., RA Allard M., Dufour L., Cossette P., Soussi-Yanicostas N., Drapeau P.; RT "gamma-Aminobutyric acid receptor alpha 1 subunit loss of function causes RT genetic generalized epilepsy by impairing inhibitory network RT neurodevelopment."; RL Epilepsia 59:2061-2074(2018). RN [8] {ECO:0000313|RefSeq:NP_001032478.1} 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; BC108008; AAI08009.1; -; mRNA. DR RefSeq; NP_001032478.1; NM_001037401.1. DR GeneID; 570159; -. DR KEGG; dre:570159; -. DR AGR; ZFIN:ZDB-GENE-051113-112; -. DR CTD; 570159; -. DR ZFIN; ZDB-GENE-051113-112; kcnk5a. DR OrthoDB; 600333at2759; -. DR PhylomeDB; Q32PR9; -. DR Proteomes; UP000000437; Alternate scaffold 17. DR Proteomes; UP000000437; Chromosome 17. DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell. DR GO; GO:0015271; F:outward rectifier potassium channel activity; IBA:GO_Central. DR GO; GO:0005267; F:potassium channel activity; IDA:ZFIN. DR GO; GO:0022841; F:potassium ion leak channel activity; IBA:GO_Central. DR GO; GO:0071805; P:potassium ion transmembrane transport; IBA:GO_Central. 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:SF241; POTASSIUM CHANNEL SUBFAMILY K MEMBER 5; 1. DR PANTHER; PTHR11003; POTASSIUM CHANNEL, SUBFAMILY K; 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, KW ECO:0000313|RefSeq:NP_001032478.1}; 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 85..104 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 116..138 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 158..182 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 194..213 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 225..244 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 79..137 FT /note="Potassium channel" FT /evidence="ECO:0000259|Pfam:PF07885" FT DOMAIN 170..247 FT /note="Potassium channel" FT /evidence="ECO:0000259|Pfam:PF07885" FT REGION 457..513 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 457..483 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 497..513 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 513 AA; 58012 MW; A88E5630AB9FFE0E CRC64; MVDKGPLLTS AIIFYLSIGA AIFQVIEEPN WEIAVRKYRA DKESILKQYP CLTKADLDYI LEVVSDAAGQ GITITGDKTF NNWNWPNAVI FAATVITTIG YGNIAPKTPS GRVFCIFYGL FGVPLCFTWI SELGKFFGGR AKHLGWYLTK KGVTLRKTQL TCTAVFLLWG VLIHLVIPPF VFMTQEGWTY IEGLYFSFVT LTTIGFGDLV AGVDPNAEYP TLYRYFVEVW IYLGLAWLSL FFNWKVRMVV EAHKALKKHR KRRRLSLDEL QLKESHKTLH LPPTPNDVNI FSFLSKKKEG YNDLIKQIGA DKGENQCVST MNSRKNAAAK RSKSCSDALS INGNTIVSLD GSPRLKRHYS FSDRVAVALS KSKGYLFSQE ECLLMTEKLE EGDTDSQCMG MSENQLDKEA GESHKALISE GCRNSQITWD SKGHQTNMFP NANITFIDED NFVNNNREDE NDFMPSFKSD EPDFRKEEDS ESETSVFTGC GSDHGQSYER LVEEYSKEDN TDI //