ID KCNKG_HUMAN Reviewed; 309 AA.
AC Q96T55; B5TJL9; Q2M2N9; Q5TCF3; Q6X6Z3; Q6X6Z4; Q6X6Z5; Q9H591;
DT 01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 24-JAN-2024, entry version 162.
DE RecName: Full=Potassium channel subfamily K member 16;
DE AltName: Full=2P domain potassium channel Talk-1;
DE AltName: Full=TWIK-related alkaline pH-activated K(+) channel 1;
DE Short=TALK-1;
GN Name=KCNK16; Synonyms=TALK1;
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] (ISOFORM A).
RC TISSUE=Pancreas;
RX PubMed=11263999; DOI=10.1006/bbrc.2001.4562;
RA Girard C., Duprat F., Terrenoire C., Tinel N., Fosset M., Romey G.,
RA Lazdunski M., Lesage F.;
RT "Genomic and functional characteristics of novel human pancreatic 2P domain
RT K(+) channels.";
RL Biochem. Biophys. Res. Commun. 282:249-256(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS B; C AND D), TISSUE SPECIFICITY,
RP ALTERNATIVE SPLICING, AND VARIANT HIS-301.
RX PubMed=12724142; DOI=10.1152/ajpcell.00601.2002;
RA Han J., Kang D., Kim D.;
RT "Functional properties of four splice variants of a human pancreatic
RT tandem-pore K+ channel, TALK-1.";
RL Am. J. Physiol. 285:C529-C538(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B).
RC TISSUE=Pancreas;
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 [4]
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., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., 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., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT HIS-301.
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM C).
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: Outward rectifying potassium channel. Produces rapidly
CC activating and non-inactivating outward rectifier K(+) currents.
CC -!- SUBUNIT: Homodimer. {ECO:0000305}.
CC -!- INTERACTION:
CC Q96T55; P32242: OTX1; NbExp=3; IntAct=EBI-10294109, EBI-740446;
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=a;
CC IsoId=Q96T55-1; Sequence=Displayed;
CC Name=b;
CC IsoId=Q96T55-3; Sequence=VSP_039865;
CC Name=c;
CC IsoId=Q96T55-4; Sequence=VSP_039863;
CC Name=d;
CC IsoId=Q96T55-5; Sequence=VSP_039864;
CC -!- TISSUE SPECIFICITY: Highly expressed in pancreas. Not detectable in the
CC other tissues tested. {ECO:0000269|PubMed:12724142}.
CC -!- MISCELLANEOUS: Inhibited by Ba(2+), quinine, quinidine, chloroform and
CC halothane. Activated at alkaline pH.
CC -!- SIMILARITY: Belongs to the two pore domain potassium channel (TC
CC 1.A.1.8) family. {ECO:0000305}.
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DR EMBL; AF358909; AAK49532.1; -; mRNA.
DR EMBL; AY253145; AAP82866.1; -; mRNA.
DR EMBL; AY253146; AAP82867.1; -; mRNA.
DR EMBL; AY253147; AAP82868.1; -; mRNA.
DR EMBL; EU978943; ACH86102.1; -; mRNA.
DR EMBL; AL136087; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471081; EAX03982.1; -; Genomic_DNA.
DR EMBL; CH471081; EAX03984.1; -; Genomic_DNA.
DR EMBL; CH471081; EAX03985.1; -; Genomic_DNA.
DR EMBL; BC111860; AAI11861.1; -; mRNA.
DR CCDS; CCDS47420.1; -. [Q96T55-5]
DR CCDS; CCDS47421.1; -. [Q96T55-4]
DR CCDS; CCDS47422.1; -. [Q96T55-3]
DR CCDS; CCDS4843.1; -. [Q96T55-1]
DR RefSeq; NP_001128577.1; NM_001135105.1. [Q96T55-4]
DR RefSeq; NP_001128578.1; NM_001135106.1. [Q96T55-3]
DR RefSeq; NP_001128579.1; NM_001135107.1. [Q96T55-5]
DR RefSeq; NP_115491.1; NM_032115.3. [Q96T55-1]
DR RefSeq; XP_016866835.1; XM_017011346.1. [Q96T55-5]
DR AlphaFoldDB; Q96T55; -.
DR SMR; Q96T55; -.
DR BioGRID; 123763; 45.
DR IntAct; Q96T55; 15.
DR STRING; 9606.ENSP00000391498; -.
DR TCDB; 1.A.1.9.10; the voltage-gated ion channel (vic) superfamily.
DR iPTMnet; Q96T55; -.
DR PhosphoSitePlus; Q96T55; -.
DR BioMuta; KCNK16; -.
DR DMDM; 24636281; -.
DR MassIVE; Q96T55; -.
DR PaxDb; 9606-ENSP00000391498; -.
DR ProteomicsDB; 78192; -. [Q96T55-1]
DR ProteomicsDB; 78193; -. [Q96T55-3]
DR ProteomicsDB; 78194; -. [Q96T55-4]
DR ProteomicsDB; 78195; -. [Q96T55-5]
DR Antibodypedia; 15706; 58 antibodies from 13 providers.
DR DNASU; 83795; -.
DR Ensembl; ENST00000373227.8; ENSP00000362324.4; ENSG00000095981.11. [Q96T55-5]
DR Ensembl; ENST00000373229.9; ENSP00000362326.5; ENSG00000095981.11. [Q96T55-1]
DR Ensembl; ENST00000425054.6; ENSP00000391498.2; ENSG00000095981.11. [Q96T55-4]
DR Ensembl; ENST00000437525.3; ENSP00000415375.2; ENSG00000095981.11. [Q96T55-3]
DR GeneID; 83795; -.
DR KEGG; hsa:83795; -.
DR MANE-Select; ENST00000437525.3; ENSP00000415375.2; NM_001135106.2; NP_001128578.1. [Q96T55-3]
DR UCSC; uc003ooq.3; human. [Q96T55-1]
DR AGR; HGNC:14464; -.
DR CTD; 83795; -.
DR DisGeNET; 83795; -.
DR GeneCards; KCNK16; -.
DR HGNC; HGNC:14464; KCNK16.
DR HPA; ENSG00000095981; Group enriched (pancreas, stomach).
DR MIM; 607369; gene.
DR neXtProt; NX_Q96T55; -.
DR OpenTargets; ENSG00000095981; -.
DR PharmGKB; PA30057; -.
DR VEuPathDB; HostDB:ENSG00000095981; -.
DR eggNOG; KOG1418; Eukaryota.
DR GeneTree; ENSGT00940000159813; -.
DR HOGENOM; CLU_022504_6_0_1; -.
DR InParanoid; Q96T55; -.
DR OMA; LQLKWHK; -.
DR OrthoDB; 600333at2759; -.
DR PhylomeDB; Q96T55; -.
DR TreeFam; TF313947; -.
DR PathwayCommons; Q96T55; -.
DR Reactome; R-HSA-1299361; TWIK-related alkaline pH activated K+ channel (TALK).
DR Reactome; R-HSA-5576886; Phase 4 - resting membrane potential.
DR SignaLink; Q96T55; -.
DR BioGRID-ORCS; 83795; 26 hits in 1140 CRISPR screens.
DR GeneWiki; KCNK16; -.
DR GenomeRNAi; 83795; -.
DR Pharos; Q96T55; Tbio.
DR PRO; PR:Q96T55; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q96T55; Protein.
DR Bgee; ENSG00000095981; Expressed in islet of Langerhans and 32 other cell types or tissues.
DR ExpressionAtlas; Q96T55; baseline and differential.
DR Genevisible; Q96T55; HS.
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:0005267; F:potassium channel activity; IDA:MGI.
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:0006813; P:potassium ion transport; IDA:MGI.
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:SF104; POTASSIUM CHANNEL SUBFAMILY K MEMBER 16; 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 Alternative splicing; Ion channel; Ion transport; Membrane; Potassium;
KW Potassium channel; Potassium transport; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport; Voltage-gated channel.
FT CHAIN 1..309
FT /note="Potassium channel subfamily K member 16"
FT /id="PRO_0000101767"
FT TOPO_DOM 1..13
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 14..34
FT /note="Helical"
FT /evidence="ECO:0000255"
FT INTRAMEM 98..116
FT /note="Pore-forming; Name=Pore-forming 1"
FT /evidence="ECO:0000255"
FT TRANSMEM 120..140
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 141..165
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 166..186
FT /note="Helical"
FT /evidence="ECO:0000255"
FT INTRAMEM 202..221
FT /note="Pore-forming; Name=Pore-forming 2"
FT /evidence="ECO:0000255"
FT TRANSMEM 238..258
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 259..309
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT VAR_SEQ 222..309
FT /note="TDPSKHYISVYRSLAAIWILLGLAWLALILPLGPLLLHRCCQLWLLSLRQGC
FT GAKAAPGRRPRRGSTAARGVQVTPQDFPISKKGLGS -> HPLNFITPSGLLPSQEPFQ
FT TPHGKPESQQIPGSFQKVSSMNVWPLSGMHSPGLAFPLPDCNIPDQERFRPLHPGAWKF
FT WPLPLPSSNSKWAPMWLGSSAQV (in isoform c)"
FT /evidence="ECO:0000303|PubMed:12724142,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_039863"
FT VAR_SEQ 222..268
FT /note="Missing (in isoform d)"
FT /evidence="ECO:0000303|PubMed:12724142"
FT /id="VSP_039864"
FT VAR_SEQ 269..309
FT /note="LRQGCGAKAAPGRRPRRGSTAARGVQVTPQDFPISKKGLGS -> RGLGVKD
FT GAASDPSGLPRPQKIPISA (in isoform b)"
FT /evidence="ECO:0000303|PubMed:12724142,
FT ECO:0000303|PubMed:18516069"
FT /id="VSP_039865"
FT VARIANT 215
FT /note="F -> L (in dbSNP:rs9462527)"
FT /id="VAR_063636"
FT VARIANT 275
FT /note="A -> G (in dbSNP:rs1535500)"
FT /id="VAR_063637"
FT VARIANT 301
FT /note="P -> H (in dbSNP:rs11756091)"
FT /evidence="ECO:0000269|PubMed:12724142, ECO:0000269|Ref.5"
FT /id="VAR_052430"
FT CONFLICT 49
FT /note="L -> S (in Ref. 2; AAP82866)"
FT /evidence="ECO:0000305"
FT CONFLICT 149
FT /note="A -> V (in Ref. 2; AAP82867)"
FT /evidence="ECO:0000305"
FT CONFLICT 200
FT /note="S -> G (in Ref. 2; AAP82866)"
FT /evidence="ECO:0000305"
FT CONFLICT 205..207
FT /note="FAF -> LLS (in Ref. 2; AAP82867)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 309 AA; 34153 MW; 99C4B11EB26B0764 CRC64;
MPSAGLCSCW GGRVLPLLLA YVCYLLLGAT IFQLLERQAE AQSRDQFQLE KLRFLENYTC
LDQWAMEQFV QVIMEAWVKG VNPKGNSTNP SNWDFGSSFF FAGTVVTTIG YGNLAPSTEA
GQVFCVFYAL LGIPLNVIFL NHLGTGLRAH LAAIERWEDR PRRSQVLQVL GLALFLTLGT
LVILIFPPMV FSHVEGWSFS EGFYFAFITL STIGFGDYVV GTDPSKHYIS VYRSLAAIWI
LLGLAWLALI LPLGPLLLHR CCQLWLLSLR QGCGAKAAPG RRPRRGSTAA RGVQVTPQDF
PISKKGLGS
//
