ID   KCNKF_HUMAN             Reviewed;         330 AA.
AC   Q9H427; Q52LL3; Q9HBC8;
DT   01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   23-FEB-2022, sequence version 3.
DT   24-JAN-2024, entry version 158.
DE   RecName: Full=Potassium channel subfamily K member 15;
DE   AltName: Full=Acid-sensitive potassium channel protein TASK-5;
DE   AltName: Full=TWIK-related acid-sensitive K(+) channel 5;
DE   AltName: Full=Two pore potassium channel KT3.3;
DE            Short=Two pore K(+) channel KT3.3;
GN   Name=KCNK15; Synonyms=TASK5;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX   PubMed=11409881; DOI=10.1006/bbrc.2001.5064;
RA   Kim D., Gnatenco C.;
RT   "TASK-5, a new member of the tandem-pore K(+) channel family.";
RL   Biochem. Biophys. Res. Commun. 284:923-930(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS GLY-95; PRO-260 AND PRO-323.
RC   TISSUE=Brain;
RX   PubMed=11431495; DOI=10.1152/jn.2001.86.1.130;
RA   Vega-Saenz de Miera E., Lau D.H.P., Zhadina M., Pountney D., Coetzee W.A.,
RA   Rudy B.;
RT   "KT3.2 and KT3.3, two novel human two-pore K(+) channels closely related to
RT   TASK-1.";
RL   J. Neurophysiol. 86:130-142(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], POLYMORPHISM, VARIANTS GLY-95;
RP   PRO-260; HIS-261 AND PRO-323, AND MUTAGENESIS OF ARG-138; 141-LEU--CYS-145;
RP   TRP-151 AND CYS-153.
RC   TISSUE=Brain, Colon, and Ovarian carcinoma;
RX   PubMed=11749039; DOI=10.1006/mcne.2001.1045;
RA   Karschin C., Wischmeyer E., Preisig-Mueller R., Rajan S., Derst C.,
RA   Grzeschik K.-H., Daut J., Karschin A.;
RT   "Expression pattern in brain of TASK-1, TASK-3, and a tandem pore domain
RT   K(+) channel subunit, TASK-5, associated with the central auditory nervous
RT   system.";
RL   Mol. Cell. Neurosci. 18:632-648(2001).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA], VARIANTS GLY-95; PRO-260 AND PRO-323, AND
RP   TISSUE SPECIFICITY.
RX   PubMed=11680614; DOI=10.1007/s004240100620;
RA   Ashmole I., Goodwin P.A., Stanfield P.R.;
RT   "TASK-5, a novel member of the tandem pore K+ channel family.";
RL   Pflugers Arch. 442:828-833(2001).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=11780052; DOI=10.1038/414865a;
RA   Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA   Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA   Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA   Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA   Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA   Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA   Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA   Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA   Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA   Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA   Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA   Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA   Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA   Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA   Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA   Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA   Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA   Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA   Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA   Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA   Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA   Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA   Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT   "The DNA sequence and comparative analysis of human chromosome 20.";
RL   Nature 414:865-871(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
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 project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Probable potassium channel subunit. No channel activity
CC       observed in heterologous systems. May need to associate with another
CC       protein to form a functional channel.
CC   -!- SUBUNIT: Heterodimer. {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC   -!- TISSUE SPECIFICITY: Detected in pancreas, heart, placenta, lung, liver,
CC       kidney, ovary, testis, skeletal muscle and adrenal gland, and at lower
CC       levels in prostate, spleen and thyroid gland.
CC       {ECO:0000269|PubMed:11409881, ECO:0000269|PubMed:11680614}.
CC   -!- POLYMORPHISM: Three alleles are known: TASK-5A, TASK-5B and TASK-5C.
CC       The sequence shown is that of allele TASK-5B.
CC       {ECO:0000269|PubMed:11409881, ECO:0000269|PubMed:11749039,
CC       ECO:0000269|PubMed:11780052, ECO:0000269|PubMed:15489334}.
CC   -!- SIMILARITY: Belongs to the two pore domain potassium channel
CC       (TC 1.A.1.8) family. {ECO:0000305}.
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DR   EMBL; AF257081; AAG33127.1; -; mRNA.
DR   EMBL; AF294350; AAK97091.1; -; mRNA.
DR   EMBL; AF294351; AAK97092.1; -; mRNA.
DR   EMBL; AF294352; AAK97093.1; -; Genomic_DNA.
DR   EMBL; AF336342; AAK37518.1; -; mRNA.
DR   EMBL; AL118522; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC093874; AAH93874.1; -; mRNA.
DR   EMBL; BC143282; AAI43283.1; -; mRNA.
DR   CCDS; CCDS13337.1; -.
DR   PIR; JC7703; JC7703.
DR   RefSeq; NP_071753.2; NM_022358.3.
DR   AlphaFoldDB; Q9H427; -.
DR   SMR; Q9H427; -.
DR   STRING; 9606.ENSP00000361952; -.
DR   TCDB; 1.A.1.9.12; the voltage-gated ion channel (vic) superfamily.
DR   PhosphoSitePlus; Q9H427; -.
DR   BioMuta; KCNK15; -.
DR   DMDM; 24636282; -.
DR   MassIVE; Q9H427; -.
DR   MaxQB; Q9H427; -.
DR   PaxDb; 9606-ENSP00000361952; -.
DR   PeptideAtlas; Q9H427; -.
DR   ProteomicsDB; 80784; -.
DR   Antibodypedia; 27447; 125 antibodies from 21 providers.
DR   DNASU; 60598; -.
DR   Ensembl; ENST00000372861.5; ENSP00000361952.3; ENSG00000124249.7.
DR   GeneID; 60598; -.
DR   KEGG; hsa:60598; -.
DR   MANE-Select; ENST00000372861.5; ENSP00000361952.3; NM_022358.4; NP_071753.2.
DR   UCSC; uc002xmr.4; human.
DR   AGR; HGNC:13814; -.
DR   CTD; 60598; -.
DR   DisGeNET; 60598; -.
DR   GeneCards; KCNK15; -.
DR   HGNC; HGNC:13814; KCNK15.
DR   HPA; ENSG00000124249; Low tissue specificity.
DR   MIM; 607368; gene.
DR   neXtProt; NX_Q9H427; -.
DR   OpenTargets; ENSG00000124249; -.
DR   PharmGKB; PA30056; -.
DR   VEuPathDB; HostDB:ENSG00000124249; -.
DR   eggNOG; KOG4404; Eukaryota.
DR   GeneTree; ENSGT00940000160902; -.
DR   HOGENOM; CLU_022504_4_2_1; -.
DR   InParanoid; Q9H427; -.
DR   OMA; FCYLLVG; -.
DR   OrthoDB; 600333at2759; -.
DR   PhylomeDB; Q9H427; -.
DR   TreeFam; TF313947; -.
DR   PathwayCommons; Q9H427; -.
DR   Reactome; R-HSA-5576886; Phase 4 - resting membrane potential.
DR   SignaLink; Q9H427; -.
DR   BioGRID-ORCS; 60598; 8 hits in 1135 CRISPR screens.
DR   ChiTaRS; KCNK15; human.
DR   GeneWiki; KCNK15; -.
DR   GenomeRNAi; 60598; -.
DR   Pharos; Q9H427; Tbio.
DR   PRO; PR:Q9H427; -.
DR   Proteomes; UP000005640; Chromosome 20.
DR   RNAct; Q9H427; Protein.
DR   Bgee; ENSG00000124249; Expressed in thoracic aorta and 91 other cell types or tissues.
DR   GO; GO:0034702; C:monoatomic ion channel complex; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:0015271; F:outward rectifier potassium channel activity; IBA:GO_Central.
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   InterPro; IPR008073; TASK5.
DR   PANTHER; PTHR11003:SF18; POTASSIUM CHANNEL SUBFAMILY K MEMBER 15; 1.
DR   PANTHER; PTHR11003; POTASSIUM CHANNEL, SUBFAMILY K; 1.
DR   Pfam; PF07885; Ion_trans_2; 2.
DR   PIRSF; PIRSF038061; K_channel_subfamily_K_type; 1.
DR   PRINTS; PR01333; 2POREKCHANEL.
DR   PRINTS; PR01690; TASK5CHANNEL.
DR   PRINTS; PR01095; TASKCHANNEL.
DR   SUPFAM; SSF81324; Voltage-gated potassium channels; 1.
PE   1: Evidence at protein level;
KW   Ion channel; Ion transport; Membrane; Potassium; Potassium channel;
KW   Potassium transport; Reference proteome; Transmembrane;
KW   Transmembrane helix; Transport; Voltage-gated channel.
FT   CHAIN           1..330
FT                   /note="Potassium channel subfamily K member 15"
FT                   /id="PRO_0000101765"
FT   TOPO_DOM        1..8
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        9..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   INTRAMEM        80..101
FT                   /note="Pore-forming; Name=Pore-forming 1"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        108..128
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        129..158
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        159..179
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   INTRAMEM        189..209
FT                   /note="Pore-forming; Name=Pore-forming 2"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        223..243
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        244..330
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          256..276
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VARIANT         95
FT                   /note="E -> G (in allele TASK-5A and allele TASK-5C;
FT                   dbSNP:rs1111032)"
FT                   /evidence="ECO:0000269|PubMed:11431495,
FT                   ECO:0000269|PubMed:11749039"
FT                   /id="VAR_014211"
FT   VARIANT         260
FT                   /note="T -> P (in allele TASK-5A and allele TASK-5C;
FT                   dbSNP:rs6073538)"
FT                   /evidence="ECO:0000269|PubMed:11431495,
FT                   ECO:0000269|PubMed:11749039"
FT                   /id="VAR_014212"
FT   VARIANT         261
FT                   /note="P -> H (in allele TASK-5A; dbSNP:rs13037900)"
FT                   /evidence="ECO:0000269|PubMed:11749039,
FT                   ECO:0000269|PubMed:15489334"
FT                   /id="VAR_014213"
FT   VARIANT         323
FT                   /note="L -> P (in allele TASK-5A and allele TASK-5C;
FT                   dbSNP:rs13042905)"
FT                   /evidence="ECO:0000269|PubMed:11431495,
FT                   ECO:0000269|PubMed:11749039"
FT                   /id="VAR_014214"
FT   MUTAGEN         138
FT                   /note="R->Y: No effect on lack of functional expression."
FT                   /evidence="ECO:0000269|PubMed:11749039"
FT   MUTAGEN         141..145
FT                   /note="LAAKC->HRAKK: No effect on lack of functional
FT                   expression."
FT                   /evidence="ECO:0000269|PubMed:11749039"
FT   MUTAGEN         151
FT                   /note="W->R: No effect on lack of functional expression."
FT                   /evidence="ECO:0000269|PubMed:11749039"
FT   MUTAGEN         153
FT                   /note="C->D: No effect on lack of functional expression."
FT                   /evidence="ECO:0000269|PubMed:11749039"
SQ   SEQUENCE   330 AA;  36222 MW;  24F428721A1C7790 CRC64;
     MRRPSVRAAG LVLCTLCYLL VGAAVFDALE SEAESGRQRL LVQKRGALRR KFGFSAEDYR
     ELERLALQAE PHRAGRQWKF PGSFYFAITV ITTIEYGHAA PGTDSGKVFC MFYALLGIPL
     TLVTFQSLGE RLNAVVRRLL LAAKCCLGLR WTCVSTENLV VAGLLACAAT LALGAVAFSH
     FEGWTFFHAY YYCFITLTTI GFGDFVALQS GEALQRKLPY VAFSFLYILL GLTVIGAFLN
     LVVLRFLVAS ADWPERAART PSPRPPGAPE SRGLWLPRRP ARSVGSASVF CHVHKLERCA
     RDNLGFSPPS SPGVVRGGQA PRLGARWKSI
//