KCNKH_HUMAN
ID KCNKH_HUMAN Reviewed; 332 AA.
AC Q96T54; E9PB46; Q5TCF4; Q8TAW4; Q9BXD1; Q9H592;
DT 01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Potassium channel subfamily K member 17;
DE AltName: Full=2P domain potassium channel Talk-2;
DE AltName: Full=Acid-sensitive potassium channel protein TASK-4;
DE AltName: Full=TWIK-related acid-sensitive K(+) channel 4;
DE AltName: Full=TWIK-related alkaline pH-activated K(+) channel 2;
DE Short=TALK-2;
GN Name=KCNK17; Synonyms=TALK2, TASK4; ORFNames=UNQ5816/PRO19634;
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].
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], AND VARIANT GLY-21.
RC TISSUE=Adrenal gland;
RX PubMed=11248242; DOI=10.1016/s0014-5793(01)02222-0;
RA Decher N., Maier M., Dittrich W., Gassenhuber J., Brueggemann A.,
RA Busch A.E., Steinmeyer K.;
RT "Characterization of TASK-4, a novel member of the pH-sensitive, two-pore
RT domain potassium channel family.";
RL FEBS Lett. 492:84-89(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
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 MRNA], AND VARIANT GLY-21.
RC TISSUE=Lung, and Spleen;
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 -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q96T54-3; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96T54-4; Sequence=VSP_047354;
CC -!- MISCELLANEOUS: Inhibited by Ba(2+), quinidine, chloroform and
CC halothane. Activated at alkaline pH. Activated by quinine and
CC isoflurane.
CC -!- SIMILARITY: Belongs to the two pore domain potassium channel (TC
CC 1.A.1.8) family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK28551.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF358910; AAK49533.1; -; mRNA.
DR EMBL; AF339912; AAK28551.1; ALT_FRAME; mRNA.
DR EMBL; AY358853; AAQ89212.1; -; mRNA.
DR EMBL; AL136087; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC025726; AAH25726.1; -; mRNA.
DR CCDS; CCDS47419.1; -. [Q96T54-4]
DR CCDS; CCDS4842.1; -. [Q96T54-3]
DR RefSeq; NP_001128583.1; NM_001135111.1. [Q96T54-4]
DR RefSeq; NP_113648.2; NM_031460.3. [Q96T54-3]
DR AlphaFoldDB; Q96T54; -.
DR SMR; Q96T54; -.
DR BioGRID; 124608; 1.
DR STRING; 9606.ENSP00000362328; -.
DR BindingDB; Q96T54; -.
DR ChEMBL; CHEMBL4523433; -.
DR TCDB; 1.A.1.9.6; the voltage-gated ion channel (vic) superfamily.
DR GlyGen; Q96T54; 2 sites.
DR BioMuta; KCNK17; -.
DR DMDM; 24636280; -.
DR PaxDb; Q96T54; -.
DR PeptideAtlas; Q96T54; -.
DR PRIDE; Q96T54; -.
DR Antibodypedia; 45856; 65 antibodies from 18 providers.
DR DNASU; 89822; -.
DR Ensembl; ENST00000373231.9; ENSP00000362328.4; ENSG00000124780.14. [Q96T54-3]
DR Ensembl; ENST00000453413.2; ENSP00000401271.2; ENSG00000124780.14. [Q96T54-4]
DR GeneID; 89822; -.
DR KEGG; hsa:89822; -.
DR MANE-Select; ENST00000373231.9; ENSP00000362328.4; NM_031460.4; NP_113648.2.
DR UCSC; uc003ooo.4; human. [Q96T54-3]
DR CTD; 89822; -.
DR DisGeNET; 89822; -.
DR GeneCards; KCNK17; -.
DR HGNC; HGNC:14465; KCNK17.
DR HPA; ENSG00000124780; Tissue enhanced (lung, thyroid gland).
DR MIM; 607370; gene.
DR neXtProt; NX_Q96T54; -.
DR OpenTargets; ENSG00000124780; -.
DR PharmGKB; PA30058; -.
DR VEuPathDB; HostDB:ENSG00000124780; -.
DR eggNOG; KOG1418; Eukaryota.
DR GeneTree; ENSGT00940000162681; -.
DR HOGENOM; CLU_022504_1_0_1; -.
DR InParanoid; Q96T54; -.
DR OMA; NPDKEYP; -.
DR OrthoDB; 1211599at2759; -.
DR PhylomeDB; Q96T54; -.
DR TreeFam; TF313947; -.
DR PathwayCommons; Q96T54; -.
DR Reactome; R-HSA-1299361; TWIK-related alkaline pH activated K+ channel (TALK).
DR Reactome; R-HSA-5576886; Phase 4 - resting membrane potential.
DR BioGRID-ORCS; 89822; 11 hits in 1058 CRISPR screens.
DR ChiTaRS; KCNK17; human.
DR GeneWiki; KCNK17; -.
DR GenomeRNAi; 89822; -.
DR Pharos; Q96T54; Tchem.
DR PRO; PR:Q96T54; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q96T54; protein.
DR Bgee; ENSG00000124780; Expressed in ascending aorta and 96 other tissues.
DR Genevisible; Q96T54; HS.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
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:UniProtKB.
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:UniProtKB.
DR GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
DR GO; GO:0030322; P:stabilization of membrane potential; IBA:GO_Central.
DR InterPro; IPR003280; 2pore_dom_K_chnl.
DR InterPro; IPR003092; 2pore_dom_K_chnl_TASK.
DR InterPro; IPR013099; K_chnl_dom.
DR PANTHER; PTHR11003; PTHR11003; 1.
DR Pfam; PF07885; Ion_trans_2; 2.
DR PIRSF; PIRSF038061; K_channel_subfamily_K_type; 1.
DR PRINTS; PR01333; 2POREKCHANEL.
DR PRINTS; PR01095; TASKCHANNEL.
PE 2: Evidence at transcript level;
KW Alternative splicing; Glycoprotein; Ion channel; Ion transport; Membrane;
KW Potassium; Potassium channel; Potassium transport; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport; Voltage-gated channel.
FT CHAIN 1..332
FT /note="Potassium channel subfamily K member 17"
FT /id="PRO_0000101768"
FT TOPO_DOM 1..20
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 21..43
FT /note="Helical"
FT /evidence="ECO:0000255"
FT INTRAMEM 106..124
FT /note="Pore-forming; Name=Pore-forming 1"
FT /evidence="ECO:0000255"
FT TRANSMEM 128..148
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 149..179
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 180..200
FT /note="Helical"
FT /evidence="ECO:0000255"
FT INTRAMEM 211..230
FT /note="Pore-forming; Name=Pore-forming 2"
FT /evidence="ECO:0000255"
FT TRANSMEM 244..264
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 265..332
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 287..312
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 65
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 94
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 230..332
FT /note="GMNPSQRYPLWYKNMVSLWILFGMAWLALIIKLILSQLETPGRVCSCCHHSS
FT KEDFKSQSWRQGPDREPESHSPQQGCYPEGPMGIIQHLEPSAHAAGCGKDS -> ASCL
FT ISDTRKPNRDWQTLERTSKSSGGLLKYRFLAGHGGSHL (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_047354"
FT VARIANT 21
FT /note="S -> G (in dbSNP:rs10947804)"
FT /evidence="ECO:0000269|PubMed:11248242,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_032362"
FT VARIANT 253
FT /note="M -> L (in dbSNP:rs35677794)"
FT /id="VAR_032363"
FT VARIANT 296
FT /note="R -> Q (in dbSNP:rs2758910)"
FT /id="VAR_024683"
SQ SEQUENCE 332 AA; 36895 MW; 1848DBC06E078158 CRC64;
MYRPRARAAP EGRVRGCAVP STVLLLLAYL AYLALGTGVF WTLEGRAAQD SSRSFQRDKW
ELLQNFTCLD RPALDSLIRD VVQAYKNGAS LLSNTTSMGR WELVGSFFFS VSTITTIGYG
NLSPNTMAAR LFCIFFALVG IPLNLVVLNR LGHLMQQGVN HWASRLGGTW QDPDKARWLA
GSGALLSGLL LFLLLPPLLF SHMEGWSYTE GFYFAFITLS TVGFGDYVIG MNPSQRYPLW
YKNMVSLWIL FGMAWLALII KLILSQLETP GRVCSCCHHS SKEDFKSQSW RQGPDREPES
HSPQQGCYPE GPMGIIQHLE PSAHAAGCGK DS
