Full text data of KCNK5
KCNK5
(TASK2)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Potassium channel subfamily K member 5 (Acid-sensitive potassium channel protein TASK-2; TWIK-related acid-sensitive K(+) channel 2)
Potassium channel subfamily K member 5 (Acid-sensitive potassium channel protein TASK-2; TWIK-related acid-sensitive K(+) channel 2)
hRBCD
IPI00029507
IPI00029507 Potassium channel subfamily K member 5 Potassium channel subfamily K member 5 membrane n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a 1 n/a n/a n/a n/a n/a integral membrane protein n/a found at its expected molecular weight found at molecular weight
IPI00029507 Potassium channel subfamily K member 5 Potassium channel subfamily K member 5 membrane n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a 1 n/a n/a n/a n/a n/a integral membrane protein n/a found at its expected molecular weight found at molecular weight
UniProt
O95279
ID KCNK5_HUMAN Reviewed; 499 AA.
AC O95279; B5TJL2; Q5VV76;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-MAY-1999, sequence version 1.
DT 22-JAN-2014, entry version 112.
DE RecName: Full=Potassium channel subfamily K member 5;
DE AltName: Full=Acid-sensitive potassium channel protein TASK-2;
DE AltName: Full=TWIK-related acid-sensitive K(+) channel 2;
GN Name=KCNK5; Synonyms=TASK2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Kidney;
RX PubMed=9812978; DOI=10.1074/jbc.273.47.30863;
RA Reyes R., Duprat F., Lesage F., Fink M., Salinas M., Farman N.,
RA Lazdunski M.;
RT "Cloning and expression of a novel pH-sensitive two pore domain K+
RT channel from human kidney.";
RL J. Biol. Chem. 273:30863-30869(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=18516069; DOI=10.1038/bjp.2008.213;
RA Gierten J., Ficker E., Bloehs R., Schlomer K., Kathofer S., Scholz E.,
RA Zitron E., Kiesecker C., Bauer A., Becker R., Katus H.A., Karle C.A.,
RA Thomas D.;
RT "Regulation of two-pore-domain (K2P) potassium leak channels by the
RT tyrosine kinase inhibitor genistein.";
RL Br. J. Pharmacol. 154:1680-1690(2008).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
RA Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
RA Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP INTERCHAIN DISULFIDE BOND.
RX PubMed=12851074; DOI=10.1080/0968768031000084181;
RA Niemeyer M.I., Cid L.P., Valenzuela X., Paeile V., Sepulveda F.V.;
RT "Extracellular conserved cysteine forms an intersubunit disulphide
RT bridge in the KCNK5 (TASK-2) K+ channel without having an essential
RT effect upon activity.";
RL Mol. Membr. Biol. 20:185-191(2003).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-371, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
CC -!- FUNCTION: pH-dependent, voltage insensitive, outwardly rectifying
CC potassium channel. Outward rectification is lost at high external
CC K(+) concentrations.
CC -!- SUBUNIT: Homodimer; disulfide-linked.
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein
CC (Potential).
CC -!- TISSUE SPECIFICITY: Abundant expression in kidney, also detected
CC in liver, placenta and small intestine. In the kidney, expression
CC is restricted to the distal tubules and collecting ducts. Not
CC expressed in proximal tubules or glomeruli.
CC -!- MISCELLANEOUS: Inhibited by quinine, quinidine and external
CC acidification.
CC -!- SIMILARITY: Belongs to the two pore domain potassium channel
CC (TC 1.A.1.8) family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AF084830; AAC79458.1; -; mRNA.
DR EMBL; EU978936; ACH86095.1; -; mRNA.
DR EMBL; AL451185; CAH70466.1; -; Genomic_DNA.
DR EMBL; CH471081; EAX03979.1; -; Genomic_DNA.
DR EMBL; BC060793; AAH60793.1; -; mRNA.
DR EMBL; BC069573; AAH69573.1; -; mRNA.
DR RefSeq; NP_003731.1; NM_003740.3.
DR UniGene; Hs.444448; -.
DR ProteinModelPortal; O95279; -.
DR SMR; O95279; 19-244.
DR IntAct; O95279; 1.
DR TCDB; 1.A.1.8.2; the voltage-gated ion channel (vic) superfamily.
DR PhosphoSite; O95279; -.
DR PaxDb; O95279; -.
DR PRIDE; O95279; -.
DR Ensembl; ENST00000359534; ENSP00000352527; ENSG00000164626.
DR GeneID; 8645; -.
DR KEGG; hsa:8645; -.
DR UCSC; uc003oon.3; human.
DR CTD; 8645; -.
DR GeneCards; GC06M039242; -.
DR HGNC; HGNC:6280; KCNK5.
DR MIM; 603493; gene.
DR neXtProt; NX_O95279; -.
DR PharmGKB; PA30062; -.
DR eggNOG; NOG323264; -.
DR HOGENOM; HOG000113211; -.
DR HOVERGEN; HBG052236; -.
DR InParanoid; O95279; -.
DR KO; K04916; -.
DR OMA; PYEQLMN; -.
DR OrthoDB; EOG7TTQ85; -.
DR PhylomeDB; O95279; -.
DR ChiTaRS; KCNK5; human.
DR GeneWiki; KCNK5; -.
DR GenomeRNAi; 8645; -.
DR NextBio; 32411; -.
DR PRO; PR:O95279; -.
DR Bgee; O95279; -.
DR CleanEx; HS_KCNK5; -.
DR Genevestigator; O95279; -.
DR GO; GO:0005887; C:integral to plasma membrane; TAS:ProtInc.
DR GO; GO:0005267; F:potassium channel activity; TAS:ProtInc.
DR GO; GO:0005244; F:voltage-gated ion channel activity; IEA:UniProtKB-KW.
DR GO; GO:0007588; P:excretion; TAS:ProtInc.
DR InterPro; IPR003280; 2pore_dom_K_chnl.
DR InterPro; IPR013099; 2pore_dom_K_chnl_dom.
DR InterPro; IPR003092; 2pore_dom_K_chnl_TASK.
DR Pfam; PF07885; Ion_trans_2; 2.
DR PRINTS; PR01333; 2POREKCHANEL.
DR PRINTS; PR01095; TASKCHANNEL.
PE 1: Evidence at protein level;
KW Complete proteome; Disulfide bond; Glycoprotein; Ion channel;
KW Ion transport; Membrane; Phosphoprotein; Polymorphism; Potassium;
KW Potassium channel; Potassium transport; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport; Voltage-gated channel.
FT CHAIN 1 499 Potassium channel subfamily K member 5.
FT /FTId=PRO_0000101749.
FT TOPO_DOM 1 7 Cytoplasmic (Potential).
FT TRANSMEM 8 26 Helical; (Potential).
FT INTRAMEM 85 112 Pore-forming; Name=Pore-forming 1;
FT (Potential).
FT TRANSMEM 113 133 Helical; (Potential).
FT TOPO_DOM 134 157 Cytoplasmic (Potential).
FT TRANSMEM 158 180 Helical; (Potential).
FT INTRAMEM 190 215 Pore-forming; Name=Pore-forming 2;
FT (Potential).
FT TRANSMEM 230 250 Helical; (Potential).
FT TOPO_DOM 251 325 Cytoplasmic (Potential).
FT MOD_RES 371 371 Phosphoserine.
FT CARBOHYD 77 77 N-linked (GlcNAc...) (Potential).
FT DISULFID 51 51 Interchain.
FT VARIANT 465 465 P -> T (in dbSNP:rs9462487).
FT /FTId=VAR_052425.
SQ SEQUENCE 499 AA; 55130 MW; E871A7A4823DDA00 CRC64;
MVDRGPLLTS AIIFYLAIGA AIFEVLEEPH WKEAKKNYYT QKLHLLKEFP CLGQEGLDKI
LEVVSDAAGQ GVAITGNQTF NNWNWPNAMI FAATVITTIG YGNVAPKTPA GRLFCVFYGL
FGVPLCLTWI SALGKFFGGR AKRLGQFLTK RGVSLRKAQI TCTVIFIVWG VLVHLVIPPF
VFMVTEGWNY IEGLYYSFIT ISTIGFGDFV AGVNPSANYH ALYRYFVELW IYLGLAWLSL
FVNWKVSMFV EVHKAIKKRR RRRKESFESS PHSRKALQVK GSTASKDVNI FSFLSKKEET
YNDLIKQIGK KAMKTSGGGE TGPGPGLGPQ GGGLPALPPS LVPLVVYSKN RVPTLEEVSQ
TLRSKGHVSR SPDEEAVARA PEDSSPAPEV FMNQLDRISE ECEPWDAQDY HPLIFQDASI
TFVNTEAGLS DEETSKSSLE DNLAGEESPQ QGAEAKAPLN MGEFPSSSES TFTSTESELS
VPYEQLMNEY NKANSPKGT
//
ID KCNK5_HUMAN Reviewed; 499 AA.
AC O95279; B5TJL2; Q5VV76;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-MAY-1999, sequence version 1.
DT 22-JAN-2014, entry version 112.
DE RecName: Full=Potassium channel subfamily K member 5;
DE AltName: Full=Acid-sensitive potassium channel protein TASK-2;
DE AltName: Full=TWIK-related acid-sensitive K(+) channel 2;
GN Name=KCNK5; Synonyms=TASK2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Kidney;
RX PubMed=9812978; DOI=10.1074/jbc.273.47.30863;
RA Reyes R., Duprat F., Lesage F., Fink M., Salinas M., Farman N.,
RA Lazdunski M.;
RT "Cloning and expression of a novel pH-sensitive two pore domain K+
RT channel from human kidney.";
RL J. Biol. Chem. 273:30863-30869(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=18516069; DOI=10.1038/bjp.2008.213;
RA Gierten J., Ficker E., Bloehs R., Schlomer K., Kathofer S., Scholz E.,
RA Zitron E., Kiesecker C., Bauer A., Becker R., Katus H.A., Karle C.A.,
RA Thomas D.;
RT "Regulation of two-pore-domain (K2P) potassium leak channels by the
RT tyrosine kinase inhibitor genistein.";
RL Br. J. Pharmacol. 154:1680-1690(2008).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
RA Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
RA Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP INTERCHAIN DISULFIDE BOND.
RX PubMed=12851074; DOI=10.1080/0968768031000084181;
RA Niemeyer M.I., Cid L.P., Valenzuela X., Paeile V., Sepulveda F.V.;
RT "Extracellular conserved cysteine forms an intersubunit disulphide
RT bridge in the KCNK5 (TASK-2) K+ channel without having an essential
RT effect upon activity.";
RL Mol. Membr. Biol. 20:185-191(2003).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-371, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
CC -!- FUNCTION: pH-dependent, voltage insensitive, outwardly rectifying
CC potassium channel. Outward rectification is lost at high external
CC K(+) concentrations.
CC -!- SUBUNIT: Homodimer; disulfide-linked.
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein
CC (Potential).
CC -!- TISSUE SPECIFICITY: Abundant expression in kidney, also detected
CC in liver, placenta and small intestine. In the kidney, expression
CC is restricted to the distal tubules and collecting ducts. Not
CC expressed in proximal tubules or glomeruli.
CC -!- MISCELLANEOUS: Inhibited by quinine, quinidine and external
CC acidification.
CC -!- SIMILARITY: Belongs to the two pore domain potassium channel
CC (TC 1.A.1.8) family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AF084830; AAC79458.1; -; mRNA.
DR EMBL; EU978936; ACH86095.1; -; mRNA.
DR EMBL; AL451185; CAH70466.1; -; Genomic_DNA.
DR EMBL; CH471081; EAX03979.1; -; Genomic_DNA.
DR EMBL; BC060793; AAH60793.1; -; mRNA.
DR EMBL; BC069573; AAH69573.1; -; mRNA.
DR RefSeq; NP_003731.1; NM_003740.3.
DR UniGene; Hs.444448; -.
DR ProteinModelPortal; O95279; -.
DR SMR; O95279; 19-244.
DR IntAct; O95279; 1.
DR TCDB; 1.A.1.8.2; the voltage-gated ion channel (vic) superfamily.
DR PhosphoSite; O95279; -.
DR PaxDb; O95279; -.
DR PRIDE; O95279; -.
DR Ensembl; ENST00000359534; ENSP00000352527; ENSG00000164626.
DR GeneID; 8645; -.
DR KEGG; hsa:8645; -.
DR UCSC; uc003oon.3; human.
DR CTD; 8645; -.
DR GeneCards; GC06M039242; -.
DR HGNC; HGNC:6280; KCNK5.
DR MIM; 603493; gene.
DR neXtProt; NX_O95279; -.
DR PharmGKB; PA30062; -.
DR eggNOG; NOG323264; -.
DR HOGENOM; HOG000113211; -.
DR HOVERGEN; HBG052236; -.
DR InParanoid; O95279; -.
DR KO; K04916; -.
DR OMA; PYEQLMN; -.
DR OrthoDB; EOG7TTQ85; -.
DR PhylomeDB; O95279; -.
DR ChiTaRS; KCNK5; human.
DR GeneWiki; KCNK5; -.
DR GenomeRNAi; 8645; -.
DR NextBio; 32411; -.
DR PRO; PR:O95279; -.
DR Bgee; O95279; -.
DR CleanEx; HS_KCNK5; -.
DR Genevestigator; O95279; -.
DR GO; GO:0005887; C:integral to plasma membrane; TAS:ProtInc.
DR GO; GO:0005267; F:potassium channel activity; TAS:ProtInc.
DR GO; GO:0005244; F:voltage-gated ion channel activity; IEA:UniProtKB-KW.
DR GO; GO:0007588; P:excretion; TAS:ProtInc.
DR InterPro; IPR003280; 2pore_dom_K_chnl.
DR InterPro; IPR013099; 2pore_dom_K_chnl_dom.
DR InterPro; IPR003092; 2pore_dom_K_chnl_TASK.
DR Pfam; PF07885; Ion_trans_2; 2.
DR PRINTS; PR01333; 2POREKCHANEL.
DR PRINTS; PR01095; TASKCHANNEL.
PE 1: Evidence at protein level;
KW Complete proteome; Disulfide bond; Glycoprotein; Ion channel;
KW Ion transport; Membrane; Phosphoprotein; Polymorphism; Potassium;
KW Potassium channel; Potassium transport; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport; Voltage-gated channel.
FT CHAIN 1 499 Potassium channel subfamily K member 5.
FT /FTId=PRO_0000101749.
FT TOPO_DOM 1 7 Cytoplasmic (Potential).
FT TRANSMEM 8 26 Helical; (Potential).
FT INTRAMEM 85 112 Pore-forming; Name=Pore-forming 1;
FT (Potential).
FT TRANSMEM 113 133 Helical; (Potential).
FT TOPO_DOM 134 157 Cytoplasmic (Potential).
FT TRANSMEM 158 180 Helical; (Potential).
FT INTRAMEM 190 215 Pore-forming; Name=Pore-forming 2;
FT (Potential).
FT TRANSMEM 230 250 Helical; (Potential).
FT TOPO_DOM 251 325 Cytoplasmic (Potential).
FT MOD_RES 371 371 Phosphoserine.
FT CARBOHYD 77 77 N-linked (GlcNAc...) (Potential).
FT DISULFID 51 51 Interchain.
FT VARIANT 465 465 P -> T (in dbSNP:rs9462487).
FT /FTId=VAR_052425.
SQ SEQUENCE 499 AA; 55130 MW; E871A7A4823DDA00 CRC64;
MVDRGPLLTS AIIFYLAIGA AIFEVLEEPH WKEAKKNYYT QKLHLLKEFP CLGQEGLDKI
LEVVSDAAGQ GVAITGNQTF NNWNWPNAMI FAATVITTIG YGNVAPKTPA GRLFCVFYGL
FGVPLCLTWI SALGKFFGGR AKRLGQFLTK RGVSLRKAQI TCTVIFIVWG VLVHLVIPPF
VFMVTEGWNY IEGLYYSFIT ISTIGFGDFV AGVNPSANYH ALYRYFVELW IYLGLAWLSL
FVNWKVSMFV EVHKAIKKRR RRRKESFESS PHSRKALQVK GSTASKDVNI FSFLSKKEET
YNDLIKQIGK KAMKTSGGGE TGPGPGLGPQ GGGLPALPPS LVPLVVYSKN RVPTLEEVSQ
TLRSKGHVSR SPDEEAVARA PEDSSPAPEV FMNQLDRISE ECEPWDAQDY HPLIFQDASI
TFVNTEAGLS DEETSKSSLE DNLAGEESPQ QGAEAKAPLN MGEFPSSSES TFTSTESELS
VPYEQLMNEY NKANSPKGT
//
MIM
603493
*RECORD*
*FIELD* NO
603493
*FIELD* TI
*603493 POTASSIUM CHANNEL, SUBFAMILY K, MEMBER 5; KCNK5
;;TASK2
*FIELD* TX
DESCRIPTION
read more
The KCNK5 gene encodes a noninactivating, outwardly rectifying,
potassium channel expressed in the kidney and in T cells (summary by
Bittner et al., 2010). Potassium channels conduct the flux of potassium
ions through the membranes of virtually all living cells and are
involved in the control of numerous cellular functions, such as neuronal
firing, muscle contraction, volume regulation, and hormone secretion.
One class of mammalian potassium channels, which includes TWIK1 (KCNK1;
601745), TREK (KCNK2; 603219), and TASK1 (KCNK3; 603220), is
characterized by 2 pore-forming (P) domains and 4 transmembrane segments
(Reyes et al., 1998).
CLONING
By searching sequence databases with the protein sequences of 2P domain
potassium channels, Reyes et al. (1998) identified an EST encoding
TASK2, a new member of this class. They used the EST to screen a human
kidney cDNA library and isolated a full-length TASK2 (GenBank GENBANK
AF084830) cDNA that encodes a deduced 499-amino acid polypeptide with a
calculated molecular mass of 55.1 kD. TASK2 has all the hallmarks of a
2P domain potassium channel, but shows only 18 to 22% amino acid
identity with other 2P domain potassium channels. COS cells expressing
TASK2 displayed noninactivating currents, and the current-voltage
relationship was outwardly rectifying. Like TASK1 currents, TASK2
currents were highly sensitive to extracellular pH in the physiologic
range. Northern blot analysis of adult human tissues detected a 4-kb
TASK2 transcript that was expressed abundantly in kidney and to a lesser
extent in the pancreas, liver, placenta, and small intestine. In situ
hybridization of human kidney localized TASK2 mRNA to the cortical
distal tubules and collecting ducts. Reyes et al. (1998) suggested that
TASK2 plays an important role in renal potassium transport.
MAPPING
Reyes et al. (1998) mapped the TASK2 gene to chromosome 6p21 by
radiation hybrid mapping.
GENE FUNCTION
Bittner et al. (2010) demonstrated that TASK2 is constitutively
expressed on human T cells, contributes to the resting membrane
potential, is sensitive to clofilium and quinidine, and is upregulated
by stimulation of T cells. TASK2 is preferentially expressed on CD4+ T
helper and CD8+ cytotoxic T cells. Peripheral CD4+ T cells derived from
patients with relapsing-remitting multiple sclerosis (MS; 126200) showed
a significant upregulation of TASK2 (2-fold) during relapse compared to
those from MS patients with stable disease and to controls. TASK2
expression on peripheral CD8+ T cells was more significantly increased
in MS patients with acute relapse (7.6-fold) and in those with stable
disease (3.3-fold). CSF-derived and CNS lesion-derived cytotoxic T cells
from MS patients showed an even greater increase in TASK2 expression
compared to peripheral cells. No increase in TASK2 expression was seen
in patients with neuromyelitis optica, another neurologic inflammatory
disease believed to be mediated by B cells. Pharmacologic or
siRNA-mediated knockdown of TASK2 in T cells reduced proliferation and
cytokine production, indicating that TASK2 is a key mediator of T-cell
physiology.
ANIMAL MODEL
Warth et al. (2004) found that Task2-null mice showed increased
perinatal mortality. After weaning, knockout mice thrived and were
fertile, but they had reduced body weight and arterial blood pressure
compared with wildtype mice. Patch-clamp experiments on wildtype and
Task2-knockout renal proximal tubular cells indicated that Task2
channels were activated by the rise in basolateral extracellular pH
induced by bicarbonate transport. Inulin clearance measurements showed
Task2-null mice had normal NaCl and water excretion. During intravenous
bicarbonate perfusion, however, renal Na(+) and water reabsorption
capacity was reduced. In conscious Task2-null mice, blood pH,
bicarbonate concentration, and systemic base excess were reduced, but
urinary pH and bicarbonate concentration were increased. Warth et al.
(2004) concluded that Task2-knockout mice exhibited metabolic acidosis
caused by renal loss of bicarbonate ion.
*FIELD* RF
1. Bittner, S.; Bobak, N.; Herrmann, A. M.; Gobel, K.; Meuth, P.;
Hohn, K. G.; Stenner, M.-P.; Budde, T.; Wiendl, H.; Meuth, S. G.:
Upregulation of K(2P)5.1 potassium channels in multiple sclerosis. Ann.
Neurol. 68: 58-69, 2010.
2. Reyes, R.; Duprat, F.; Lesage, F.; Fink, M.; Salinas, M.; Farman,
N.; Lazdunski, M.: Cloning and expression of a novel pH-sensitive
two pore domain K+ channel from human kidney. J. Biol. Chem. 273:
30863-30869, 1998.
3. Warth, R.; Barriere, H.; Meneton, P.; Bloch, M.; Thomas, J.; Tauc,
M.; Heitzmann, D.; Romeo, E.; Verrey, F.; Mengual, R.; Guy, N.; Bendahhou,
S.; Lesage, F.; Poujeol, P.; Barhanin, J.: Proximal renal tubular
acidosis in TASK2 K(+) channel-deficient mice reveals a mechanism
for stabilizing bicarbonate transport. Proc. Nat. Acad. Sci. 101:
8215-8220, 2004.
*FIELD* CN
Cassandra L. Kniffin - updated: 8/2/2011
Patricia A. Hartz - updated: 9/20/2005
*FIELD* CD
Beth A. Dombroski: 2/5/1999
*FIELD* ED
wwang: 08/09/2011
ckniffin: 8/2/2011
alopez: 12/2/2010
wwang: 9/21/2005
wwang: 9/20/2005
psherman: 2/9/1999
psherman: 2/8/1999
psherman: 2/5/1999
*RECORD*
*FIELD* NO
603493
*FIELD* TI
*603493 POTASSIUM CHANNEL, SUBFAMILY K, MEMBER 5; KCNK5
;;TASK2
*FIELD* TX
DESCRIPTION
read more
The KCNK5 gene encodes a noninactivating, outwardly rectifying,
potassium channel expressed in the kidney and in T cells (summary by
Bittner et al., 2010). Potassium channels conduct the flux of potassium
ions through the membranes of virtually all living cells and are
involved in the control of numerous cellular functions, such as neuronal
firing, muscle contraction, volume regulation, and hormone secretion.
One class of mammalian potassium channels, which includes TWIK1 (KCNK1;
601745), TREK (KCNK2; 603219), and TASK1 (KCNK3; 603220), is
characterized by 2 pore-forming (P) domains and 4 transmembrane segments
(Reyes et al., 1998).
CLONING
By searching sequence databases with the protein sequences of 2P domain
potassium channels, Reyes et al. (1998) identified an EST encoding
TASK2, a new member of this class. They used the EST to screen a human
kidney cDNA library and isolated a full-length TASK2 (GenBank GENBANK
AF084830) cDNA that encodes a deduced 499-amino acid polypeptide with a
calculated molecular mass of 55.1 kD. TASK2 has all the hallmarks of a
2P domain potassium channel, but shows only 18 to 22% amino acid
identity with other 2P domain potassium channels. COS cells expressing
TASK2 displayed noninactivating currents, and the current-voltage
relationship was outwardly rectifying. Like TASK1 currents, TASK2
currents were highly sensitive to extracellular pH in the physiologic
range. Northern blot analysis of adult human tissues detected a 4-kb
TASK2 transcript that was expressed abundantly in kidney and to a lesser
extent in the pancreas, liver, placenta, and small intestine. In situ
hybridization of human kidney localized TASK2 mRNA to the cortical
distal tubules and collecting ducts. Reyes et al. (1998) suggested that
TASK2 plays an important role in renal potassium transport.
MAPPING
Reyes et al. (1998) mapped the TASK2 gene to chromosome 6p21 by
radiation hybrid mapping.
GENE FUNCTION
Bittner et al. (2010) demonstrated that TASK2 is constitutively
expressed on human T cells, contributes to the resting membrane
potential, is sensitive to clofilium and quinidine, and is upregulated
by stimulation of T cells. TASK2 is preferentially expressed on CD4+ T
helper and CD8+ cytotoxic T cells. Peripheral CD4+ T cells derived from
patients with relapsing-remitting multiple sclerosis (MS; 126200) showed
a significant upregulation of TASK2 (2-fold) during relapse compared to
those from MS patients with stable disease and to controls. TASK2
expression on peripheral CD8+ T cells was more significantly increased
in MS patients with acute relapse (7.6-fold) and in those with stable
disease (3.3-fold). CSF-derived and CNS lesion-derived cytotoxic T cells
from MS patients showed an even greater increase in TASK2 expression
compared to peripheral cells. No increase in TASK2 expression was seen
in patients with neuromyelitis optica, another neurologic inflammatory
disease believed to be mediated by B cells. Pharmacologic or
siRNA-mediated knockdown of TASK2 in T cells reduced proliferation and
cytokine production, indicating that TASK2 is a key mediator of T-cell
physiology.
ANIMAL MODEL
Warth et al. (2004) found that Task2-null mice showed increased
perinatal mortality. After weaning, knockout mice thrived and were
fertile, but they had reduced body weight and arterial blood pressure
compared with wildtype mice. Patch-clamp experiments on wildtype and
Task2-knockout renal proximal tubular cells indicated that Task2
channels were activated by the rise in basolateral extracellular pH
induced by bicarbonate transport. Inulin clearance measurements showed
Task2-null mice had normal NaCl and water excretion. During intravenous
bicarbonate perfusion, however, renal Na(+) and water reabsorption
capacity was reduced. In conscious Task2-null mice, blood pH,
bicarbonate concentration, and systemic base excess were reduced, but
urinary pH and bicarbonate concentration were increased. Warth et al.
(2004) concluded that Task2-knockout mice exhibited metabolic acidosis
caused by renal loss of bicarbonate ion.
*FIELD* RF
1. Bittner, S.; Bobak, N.; Herrmann, A. M.; Gobel, K.; Meuth, P.;
Hohn, K. G.; Stenner, M.-P.; Budde, T.; Wiendl, H.; Meuth, S. G.:
Upregulation of K(2P)5.1 potassium channels in multiple sclerosis. Ann.
Neurol. 68: 58-69, 2010.
2. Reyes, R.; Duprat, F.; Lesage, F.; Fink, M.; Salinas, M.; Farman,
N.; Lazdunski, M.: Cloning and expression of a novel pH-sensitive
two pore domain K+ channel from human kidney. J. Biol. Chem. 273:
30863-30869, 1998.
3. Warth, R.; Barriere, H.; Meneton, P.; Bloch, M.; Thomas, J.; Tauc,
M.; Heitzmann, D.; Romeo, E.; Verrey, F.; Mengual, R.; Guy, N.; Bendahhou,
S.; Lesage, F.; Poujeol, P.; Barhanin, J.: Proximal renal tubular
acidosis in TASK2 K(+) channel-deficient mice reveals a mechanism
for stabilizing bicarbonate transport. Proc. Nat. Acad. Sci. 101:
8215-8220, 2004.
*FIELD* CN
Cassandra L. Kniffin - updated: 8/2/2011
Patricia A. Hartz - updated: 9/20/2005
*FIELD* CD
Beth A. Dombroski: 2/5/1999
*FIELD* ED
wwang: 08/09/2011
ckniffin: 8/2/2011
alopez: 12/2/2010
wwang: 9/21/2005
wwang: 9/20/2005
psherman: 2/9/1999
psherman: 2/8/1999
psherman: 2/5/1999