ID Q9JK62_MOUSE Unreviewed; 502 AA.
AC Q9JK62;
DT 01-OCT-2000, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2000, sequence version 1.
DT 27-MAR-2024, entry version 163.
DE SubName: Full=Potassium channel TASK2 {ECO:0000313|EMBL:AAF68668.1};
DE SubName: Full=Potassium channel, subfamily K, member 5 {ECO:0000313|EMBL:AAH34012.1, ECO:0000313|Ensembl:ENSMUSP00000024011.9};
DE SubName: Full=TASK2 potassium channel {ECO:0000313|EMBL:AAG35065.1};
GN Name=Kcnk5 {ECO:0000313|EMBL:AAH34012.1,
GN ECO:0000313|Ensembl:ENSMUSP00000024011.9,
GN ECO:0000313|MGI:MGI:1336175};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090 {ECO:0000313|EMBL:AAF68668.1};
RN [1] {ECO:0000313|EMBL:BAC39423.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAC39423.1};
RC TISSUE=Head {ECO:0000313|EMBL:BAE21010.1}, and Kidney
RC {ECO:0000313|EMBL:BAC39423.1};
RX PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA Carninci P., Hayashizaki Y.;
RT "High-efficiency full-length cDNA cloning.";
RL Methods Enzymol. 303:19-44(1999).
RN [2] {ECO:0000313|EMBL:BAC39423.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAC39423.1};
RC TISSUE=Head {ECO:0000313|EMBL:BAE21010.1}, and Kidney
RC {ECO:0000313|EMBL:BAC39423.1};
RX PubMed=11042159; DOI=10.1101/gr.145100;
RA Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT "Normalization and subtraction of cap-trapper-selected cDNAs to prepare
RT full-length cDNA libraries for rapid discovery of new genes.";
RL Genome Res. 10:1617-1630(2000).
RN [3] {ECO:0000313|EMBL:BAC39423.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAC39423.1};
RC TISSUE=Head {ECO:0000313|EMBL:BAE21010.1}, and Kidney
RC {ECO:0000313|EMBL:BAC39423.1};
RX PubMed=11076861; DOI=10.1101/gr.152600;
RA Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M., Sumi N.,
RA Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A., Yamamoto R.,
RA Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K., Fujiwake S.,
RA Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M., Yoneda Y.,
RA Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J., Okazaki Y.,
RA Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT "RIKEN integrated sequence analysis (RISA) system--384-format sequencing
RT pipeline with 384 multicapillary sequencer.";
RL Genome Res. 10:1757-1771(2000).
RN [4] {ECO:0000313|EMBL:AAF68668.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=129 SvJ {ECO:0000313|EMBL:AAF68668.1};
RC TISSUE=Kidney {ECO:0000313|EMBL:AAF68668.1};
RA Roux J., Barhanin J.;
RT "Mouse two P domain potassium channel TASK2.";
RL Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000313|EMBL:AAG35065.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Kidney {ECO:0000313|EMBL:AAG35065.1};
RX PubMed=11560934; DOI=10.1074/jbc.M107192200;
RA Niemeyer M.I., Cid L.P., Barros L.F., Sepulveda F.V.;
RT "Modulation of the two-pore domain acid-sensitive K+ channel TASK-2 (KCNK5)
RT by changes in cell volume.";
RL J. Biol. Chem. 276:43166-43174(2001).
RN [6] {ECO:0000313|EMBL:BAC39423.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAC39423.1};
RC TISSUE=Head {ECO:0000313|EMBL:BAE21010.1}, and Kidney
RC {ECO:0000313|EMBL:BAC39423.1};
RX PubMed=11217851; DOI=10.1038/35055500;
RG The RIKEN Genome Exploration Research Group Phase II Team and the FANTOM Consortium;
RT "Functional annotation of a full-length mouse cDNA collection.";
RL Nature 409:685-690(2001).
RN [7] {ECO:0000313|EMBL:BAC39423.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAC39423.1};
RC TISSUE=Head {ECO:0000313|EMBL:BAE21010.1}, and Kidney
RC {ECO:0000313|EMBL:BAC39423.1};
RX PubMed=12466851; DOI=10.1038/nature01266;
RG The FANTOM Consortium and the RIKEN Genome Exploration Research Group Phase I and II Team;
RT "Analysis of the mouse transcriptome based on functional annotation of
RT 60,770 full-length cDNAs.";
RL Nature 420:563-573(2002).
RN [8] {ECO:0000313|EMBL:BAC39423.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAC39423.1};
RC TISSUE=Kidney {ECO:0000313|EMBL:BAC39423.1};
RA Adachi J., Aizawa K., Akimura T., Arakawa T., Bono H., Carninci P.,
RA Fukuda S., Furuno M., Hanagaki T., Hara A., Hashizume W., Hayashida K.,
RA Hayatsu N., Hiramoto K., Hiraoka T., Hirozane T., Hori F., Imotani K.,
RA Ishii Y., Itoh M., Kagawa I., Kasukawa T., Katoh H., Kawai J., Kojima Y.,
RA Kondo S., Konno H., Kouda M., Koya S., Kurihara C., Matsuyama T.,
RA Miyazaki A., Murata M., Nakamura M., Nishi K., Nomura K., Numazaki R.,
RA Ohno M., Ohsato N., Okazaki Y., Saito R., Saitoh H., Sakai C., Sakai K.,
RA Sakazume N., Sano H., Sasaki D., Shibata K., Shinagawa A., Shiraki T.,
RA Sogabe Y., Tagami M., Tagawa A., Takahashi F., Takaku-Akahira S.,
RA Takeda Y., Tanaka T., Tomaru A., Toya T., Yasunishi A., Muramatsu M.,
RA Hayashizaki Y.;
RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
RN [9] {ECO:0000313|EMBL:AAH34012.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N {ECO:0000313|EMBL:AAH34012.1};
RC TISSUE=Kidney {ECO:0000313|EMBL:AAH34012.1}, and Mammary tumor. C3
RC {ECO:0000313|EMBL:AAH58164.1};
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RA Gerhard D.S., Wagner L., Feingold E.A., Shenmen C.M., Grouse L.H.,
RA Schuler G., Klein S.L., Old S., Rasooly R., Good P., Guyer M., Peck A.M.,
RA Derge J.G., Lipman D., Collins F.S., Jang W., Sherry S., Feolo M.,
RA Misquitta L., Lee E., Rotmistrovsky K., Greenhut S.F., Schaefer C.F.,
RA Buetow K., Bonner T.I., Haussler D., Kent J., Kiekhaus M., Furey T.,
RA Brent M., Prange C., Schreiber K., Shapiro N., Bhat N.K., Hopkins R.F.,
RA Hsie F., Driscoll T., Soares M.B., Casavant T.L., Scheetz T.E.,
RA Brown-stein M.J., Usdin T.B., Toshiyuki S., Carninci P., Piao Y.,
RA Dudekula D.B., Ko M.S., Kawakami K., Suzuki Y., Sugano S., Gruber C.E.,
RA Smith M.R., Simmons B., Moore T., Waterman R., Johnson S.L., Ruan Y.,
RA Wei C.L., Mathavan S., Gunaratne P.H., Wu J., Garcia A.M., Hulyk S.W.,
RA Fuh E., Yuan Y., Sneed A., Kowis C., Hodgson A., Muzny D.M., McPherson J.,
RA Gibbs R.A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S.,
RA Sanchez A., Whiting M., Madari A., Young A.C., Wetherby K.D., Granite S.J.,
RA Kwong P.N., Brinkley C.P., Pearson R.L., Bouffard G.G., Blakesly R.W.,
RA Green E.D., Dickson M.C., Rodriguez A.C., Grimwood J., Schmutz J.,
RA Myers R.M., Butterfield Y.S., Griffith M., Griffith O.L., Krzywinski M.I.,
RA Liao N., Morin R., Morrin R., Palmquist D., Petrescu A.S., Skalska U.,
RA Smailus D.E., Stott J.M., Schnerch A., Schein J.E., Jones S.J., Holt R.A.,
RA Baross A., Marra M.A., Clifton S., Makowski K.A., Bosak S., Malek J.;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [10] {ECO:0000313|EMBL:BAE21010.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE21010.1};
RC TISSUE=Head {ECO:0000313|EMBL:BAE21010.1};
RA Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K., Hori F.,
RA Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S., Kawai J., Kojima M.,
RA Konno H., Murata M., Nakamura M., Ninomiya N., Nishiyori H., Nomura K.,
RA Ohno M., Sakazume N., Sano H., Sasaki D., Shibata K., Shiraki T.,
RA Tagami M., Tagami Y., Waki K., Watahiki A., Muramatsu M., Hayashizaki Y.;
RL Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
RN [11] {ECO:0000313|EMBL:BAC39423.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAC39423.1};
RC TISSUE=Head {ECO:0000313|EMBL:BAE21010.1}, and Kidney
RC {ECO:0000313|EMBL:BAC39423.1};
RG The FANTOM Consortium;
RG Riken Genome Exploration Research Group and Genome Science Group (Genome Network Project Core Group);
RT "The Transcriptional Landscape of the Mammalian Genome.";
RL Science 309:1559-1563(2005).
RN [12] {ECO:0000313|EMBL:BAC39423.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAC39423.1};
RC TISSUE=Head {ECO:0000313|EMBL:BAE21010.1}, and Kidney
RC {ECO:0000313|EMBL:BAC39423.1};
RX PubMed=16141073; DOI=10.1126/science.1112009;
RG RIKEN Genome Exploration Research Group and Genome Science Group (Genome Network Project Core Group) and the FANTOM Consortium;
RT "Antisense Transcription in the Mammalian Transcriptome.";
RL Science 309:1564-1566(2005).
RN [13] {ECO:0000313|Ensembl:ENSMUSP00000024011.9, ECO:0000313|Proteomes:UP000000589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000024011.9,
RC ECO:0000313|Proteomes:UP000000589};
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [14] {ECO:0007829|PDB:6WLV, ECO:0007829|PDB:6WM0}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.45 ANGSTROMS) OF 1-335, AND DISULFIDE
RP BONDS.
RX PubMed=32999458; DOI=10.1038/s41586-020-2770-2;
RA Li B., Rietmeijer R.A., Brohawn S.G.;
RT "Structural basis for pH gating of the two-pore domain K<sup>+</sup>
RT channel TASK2.";
RL Nature 586:457-462(2020).
RN [15] {ECO:0000313|Ensembl:ENSMUSP00000024011.9}
RP IDENTIFICATION.
RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000024011.9};
RG Ensembl;
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; AF259395; AAF68668.1; -; mRNA.
DR EMBL; AF319542; AAG35065.1; -; mRNA.
DR EMBL; BC034012; AAH34012.1; -; mRNA.
DR EMBL; BC058164; AAH58164.1; -; mRNA.
DR EMBL; AK085330; BAC39423.1; -; mRNA.
DR EMBL; AK132172; BAE21010.1; -; mRNA.
DR RefSeq; NP_067517.1; NM_021542.4.
DR PDB; 6WLV; EM; 3.45 A; A/B=1-335.
DR PDB; 6WM0; EM; 3.52 A; A/B=1-335.
DR EMDB; EMD-21843; -.
DR EMDB; EMD-21846; -.
DR STRING; 10090.ENSMUSP00000024011; -.
DR PaxDb; 10090-ENSMUSP00000024011; -.
DR ProteomicsDB; 334805; -.
DR Antibodypedia; 15697; 132 antibodies from 29 providers.
DR DNASU; 16529; -.
DR Ensembl; ENSMUST00000024011.10; ENSMUSP00000024011.9; ENSMUSG00000023243.10.
DR GeneID; 16529; -.
DR KEGG; mmu:16529; -.
DR UCSC; uc007siz.1; mouse.
DR AGR; MGI:1336175; -.
DR CTD; 8645; -.
DR MGI; MGI:1336175; Kcnk5.
DR VEuPathDB; HostDB:ENSMUSG00000023243; -.
DR eggNOG; KOG1418; Eukaryota.
DR GeneTree; ENSGT00940000156775; -.
DR HOGENOM; CLU_040658_0_0_1; -.
DR OMA; TEEWNYI; -.
DR OrthoDB; 600333at2759; -.
DR TreeFam; TF313947; -.
DR Reactome; R-MMU-5576886; Phase 4 - resting membrane potential.
DR BioGRID-ORCS; 16529; 5 hits in 77 CRISPR screens.
DR Proteomes; UP000000589; Chromosome 14.
DR Bgee; ENSMUSG00000023243; Expressed in right kidney and 155 other cell types or tissues.
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:ARUK-UCL.
DR GO; GO:0022841; F:potassium ion leak channel activity; IBA:GO_Central.
DR GO; GO:0005249; F:voltage-gated potassium channel activity; IDA:MGI.
DR GO; GO:0097623; P:potassium ion export across plasma membrane; IDA:ARUK-UCL.
DR GO; GO:1990573; P:potassium ion import across plasma membrane; IDA:MGI.
DR GO; GO:0071805; P:potassium ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0006813; P:potassium ion transport; ISO:MGI.
DR GO; GO:0060075; P:regulation of resting membrane potential; IDA:ARUK-UCL.
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 1: Evidence at protein level;
KW 3D-structure {ECO:0007829|PDB:6WLV, ECO:0007829|PDB:6WM0};
KW Ion channel {ECO:0000256|RuleBase:RU003857, ECO:0000313|EMBL:AAF68668.1};
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 Proteomics identification {ECO:0007829|EPD:Q9JK62,
KW ECO:0007829|ProteomicsDB:Q9JK62};
KW Reference proteome {ECO:0000313|Proteomes:UP000000589};
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 6..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..137
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 172..245
FT /note="Potassium channel"
FT /evidence="ECO:0000259|Pfam:PF07885"
FT REGION 365..386
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 428..502
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 463..487
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 51
FT /note="Interchain"
FT /evidence="ECO:0007829|PDB:6WLV, ECO:0007829|PDB:6WM0"
SQ SEQUENCE 502 AA; 55977 MW; E4C7E7CC71B44D95 CRC64;
MVDRGPLLTS AIIFYLAIGA AIFEVLEEPH WKEAKKNYYT QKLHLLKEFP CLSQEGLDKI
LQVVSDAADQ GVAITGNQTF NNWNWPNAMI FAATVITTIG YGNVAPKTPA GRLFCVFYGL
FGVPLCLTWI SALGKFFGGR AKRLGQFLTR RGVSLRKAQI TCTAIFIVWG VLVHLVIPPF
VFMVTEEWNY IEGLYYSFIT ISTIGFGDFV AGVNPSANYH ALYRYFVELW IYLGLAWLSL
FVNWKVSMFV EVHKAIKKRR RRRKESFESS PHSRKALQMA GSTASKDVNI FSFLSKKEET
YNDLIKQIGK KAMKTSGGGE RVPGPGHGLG PQGDRLPTIP ASLAPLVVYS KNRVPSLEEV
SQTLKNKGHV SRPLGEEAGA QAPKDSYQTS EVFINQLDRI SEEGEPWEAL DYHPLIFQNA
NITFENEETG LSDEETSKSS VEDNLTSKEQ PEQGPMAEAP LSSTGEFPSS DESTFTSTES
ELSVPYEQLM NEYNKADNPR GT
//
