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Potassium channel subfamily K member 16 (2P domain potassium channel Talk-1) (TWIK-related alkaline pH-activated K( ) channel 1) (TALK-1)

 KCNKG_HUMAN             Reviewed;         309 AA.
Q96T55; B5TJL9; Q2M2N9; Q5TCF3; Q6X6Z3; Q6X6Z4; Q6X6Z5; Q9H591;
01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
01-DEC-2001, sequence version 1.
05-JUL-2017, entry version 127.
RecName: Full=Potassium channel subfamily K member 16;
AltName: Full=2P domain potassium channel Talk-1;
AltName: Full=TWIK-related alkaline pH-activated K(+) channel 1;
Short=TALK-1;
Name=KCNK16; Synonyms=TALK1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
TISSUE=Pancreas;
PubMed=11263999; DOI=10.1006/bbrc.2001.4562;
Girard C., Duprat F., Terrenoire C., Tinel N., Fosset M., Romey G.,
Lazdunski M., Lesage F.;
"Genomic and functional characteristics of novel human pancreatic 2P
domain K(+) channels.";
Biochem. Biophys. Res. Commun. 282:249-256(2001).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS B; C AND D), TISSUE SPECIFICITY,
ALTERNATIVE SPLICING, AND VARIANT HIS-301.
PubMed=12724142; DOI=10.1152/ajpcell.00601.2002;
Han J., Kang D., Kim D.;
"Functional properties of four splice variants of a human pancreatic
tandem-pore K+ channel, TALK-1.";
Am. J. Physiol. 285:C529-C538(2003).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B).
TISSUE=Pancreas;
PubMed=18516069; DOI=10.1038/bjp.2008.213;
Gierten J., Ficker E., Bloehs R., Schlomer K., Kathofer S., Scholz E.,
Zitron E., Kiesecker C., Bauer A., Becker R., Katus H.A., Karle C.A.,
Thomas D.;
"Regulation of two-pore-domain (K2P) potassium leak channels by the
tyrosine kinase inhibitor genistein.";
Br. J. Pharmacol. 154:1680-1690(2008).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=14574404; DOI=10.1038/nature02055;
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT HIS-301.
Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM C).
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
-!- FUNCTION: Outward rectifying potassium channel. Produces rapidly
activating and non-inactivating outward rectifier K(+) currents.
-!- SUBUNIT: Homodimer. {ECO:0000305}.
-!- INTERACTION:
P32242:OTX1; NbExp=3; IntAct=EBI-10294109, EBI-740446;
-!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=a;
IsoId=Q96T55-1; Sequence=Displayed;
Name=b;
IsoId=Q96T55-3; Sequence=VSP_039865;
Name=c;
IsoId=Q96T55-4; Sequence=VSP_039863;
Name=d;
IsoId=Q96T55-5; Sequence=VSP_039864;
-!- TISSUE SPECIFICITY: Highly expressed in pancreas. Not detectable
in the other tissues tested. {ECO:0000269|PubMed:12724142}.
-!- MISCELLANEOUS: Inhibited by Ba(2+), quinine, quinidine, chloroform
and halothane. Activated at alkaline pH.
-!- SIMILARITY: Belongs to the two pore domain potassium channel (TC
1.A.1.8) family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF358909; AAK49532.1; -; mRNA.
EMBL; AY253145; AAP82866.1; -; mRNA.
EMBL; AY253146; AAP82867.1; -; mRNA.
EMBL; AY253147; AAP82868.1; -; mRNA.
EMBL; EU978943; ACH86102.1; -; mRNA.
EMBL; AL136087; CAI19537.1; -; Genomic_DNA.
EMBL; CH471081; EAX03982.1; -; Genomic_DNA.
EMBL; CH471081; EAX03984.1; -; Genomic_DNA.
EMBL; CH471081; EAX03985.1; -; Genomic_DNA.
EMBL; BC111860; AAI11861.1; -; mRNA.
CCDS; CCDS47420.1; -. [Q96T55-5]
CCDS; CCDS47421.1; -. [Q96T55-4]
CCDS; CCDS47422.1; -. [Q96T55-3]
CCDS; CCDS4843.1; -. [Q96T55-1]
RefSeq; NP_001128577.1; NM_001135105.1. [Q96T55-4]
RefSeq; NP_001128578.1; NM_001135106.1. [Q96T55-3]
RefSeq; NP_001128579.1; NM_001135107.1. [Q96T55-5]
RefSeq; NP_115491.1; NM_032115.3. [Q96T55-1]
RefSeq; XP_016866835.1; XM_017011346.1. [Q96T55-5]
UniGene; Hs.287765; -.
ProteinModelPortal; Q96T55; -.
BioGrid; 123763; 24.
IntAct; Q96T55; 2.
STRING; 9606.ENSP00000391498; -.
TCDB; 1.A.1.9.10; the voltage-gated ion channel (vic) superfamily.
iPTMnet; Q96T55; -.
PhosphoSitePlus; Q96T55; -.
BioMuta; KCNK16; -.
DMDM; 24636281; -.
PaxDb; Q96T55; -.
PRIDE; Q96T55; -.
Ensembl; ENST00000373227; ENSP00000362324; ENSG00000095981. [Q96T55-5]
Ensembl; ENST00000373229; ENSP00000362326; ENSG00000095981. [Q96T55-1]
Ensembl; ENST00000425054; ENSP00000391498; ENSG00000095981. [Q96T55-4]
Ensembl; ENST00000437525; ENSP00000415375; ENSG00000095981. [Q96T55-3]
GeneID; 83795; -.
KEGG; hsa:83795; -.
UCSC; uc003ooq.3; human. [Q96T55-1]
CTD; 83795; -.
DisGeNET; 83795; -.
GeneCards; KCNK16; -.
HGNC; HGNC:14464; KCNK16.
MIM; 607369; gene.
neXtProt; NX_Q96T55; -.
OpenTargets; ENSG00000095981; -.
PharmGKB; PA30057; -.
eggNOG; KOG1418; Eukaryota.
eggNOG; COG1226; LUCA.
GeneTree; ENSGT00760000118858; -.
HOVERGEN; HBG104884; -.
InParanoid; Q96T55; -.
KO; K04924; -.
OMA; GWSYGEG; -.
OrthoDB; EOG091G0E3R; -.
PhylomeDB; Q96T55; -.
TreeFam; TF313947; -.
Reactome; R-HSA-1299361; TWIK-related alkaline pH activated K+ channel (TALK).
Reactome; R-HSA-5576886; Phase 4 - resting membrane potential.
GeneWiki; KCNK16; -.
GenomeRNAi; 83795; -.
PRO; PR:Q96T55; -.
Proteomes; UP000005640; Chromosome 6.
Bgee; ENSG00000095981; -.
CleanEx; HS_KCNK16; -.
ExpressionAtlas; Q96T55; baseline and differential.
Genevisible; Q96T55; HS.
GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0005267; F:potassium channel activity; IDA:MGI.
GO; GO:0022841; F:potassium ion leak channel activity; IBA:GO_Central.
GO; GO:0005244; F:voltage-gated ion channel activity; IEA:UniProtKB-KW.
GO; GO:0006813; P:potassium ion transport; IDA:MGI.
GO; GO:0030322; P:stabilization of membrane potential; IBA:GO_Central.
InterPro; IPR003280; 2pore_dom_K_chnl.
InterPro; IPR003092; 2pore_dom_K_chnl_TASK.
InterPro; IPR013099; K_chnl_dom.
Pfam; PF07885; Ion_trans_2; 2.
PRINTS; PR01333; 2POREKCHANEL.
PRINTS; PR01095; TASKCHANNEL.
1: Evidence at protein level;
Alternative splicing; Complete proteome; Ion channel; Ion transport;
Membrane; Polymorphism; Potassium; Potassium channel;
Potassium transport; Reference proteome; Transmembrane;
Transmembrane helix; Transport; Voltage-gated channel.
CHAIN 1 309 Potassium channel subfamily K member 16.
/FTId=PRO_0000101767.
TOPO_DOM 1 13 Cytoplasmic. {ECO:0000255}.
TRANSMEM 14 34 Helical. {ECO:0000255}.
INTRAMEM 98 116 Pore-forming; Name=Pore-forming 1.
{ECO:0000255}.
TRANSMEM 120 140 Helical. {ECO:0000255}.
TOPO_DOM 141 165 Cytoplasmic. {ECO:0000255}.
TRANSMEM 166 186 Helical. {ECO:0000255}.
INTRAMEM 202 221 Pore-forming; Name=Pore-forming 2.
{ECO:0000255}.
TRANSMEM 238 258 Helical. {ECO:0000255}.
TOPO_DOM 259 309 Cytoplasmic. {ECO:0000255}.
VAR_SEQ 222 309 TDPSKHYISVYRSLAAIWILLGLAWLALILPLGPLLLHRCC
QLWLLSLRQGCGAKAAPGRRPRRGSTAARGVQVTPQDFPIS
KKGLGS -> HPLNFITPSGLLPSQEPFQTPHGKPESQQIP
GSFQKVSSMNVWPLSGMHSPGLAFPLPDCNIPDQERFRPLH
PGAWKFWPLPLPSSNSKWAPMWLGSSAQV (in isoform
c). {ECO:0000303|PubMed:12724142,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_039863.
VAR_SEQ 222 268 Missing (in isoform d).
{ECO:0000303|PubMed:12724142}.
/FTId=VSP_039864.
VAR_SEQ 269 309 LRQGCGAKAAPGRRPRRGSTAARGVQVTPQDFPISKKGLGS
-> RGLGVKDGAASDPSGLPRPQKIPISA (in isoform
b). {ECO:0000303|PubMed:12724142,
ECO:0000303|PubMed:18516069}.
/FTId=VSP_039865.
VARIANT 215 215 F -> L (in dbSNP:rs9462527).
/FTId=VAR_063636.
VARIANT 275 275 A -> G (in dbSNP:rs1535500).
/FTId=VAR_063637.
VARIANT 301 301 P -> H (in dbSNP:rs11756091).
{ECO:0000269|PubMed:12724142,
ECO:0000269|Ref.5}.
/FTId=VAR_052430.
CONFLICT 49 49 L -> S (in Ref. 2; AAP82866).
{ECO:0000305}.
CONFLICT 149 149 A -> V (in Ref. 2; AAP82867).
{ECO:0000305}.
CONFLICT 200 200 S -> G (in Ref. 2; AAP82866).
{ECO:0000305}.
CONFLICT 205 207 FAF -> LLS (in Ref. 2; AAP82867).
{ECO:0000305}.
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


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