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 24-JAN-2024, entry version 177. 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 CC (TC 1.A.1.8) family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAK28551.1; Type=Frameshift; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 GlyCosmos; Q96T54; 2 sites, No reported glycans. DR GlyGen; Q96T54; 2 sites. DR BioMuta; KCNK17; -. DR DMDM; 24636280; -. DR PaxDb; 9606-ENSP00000362328; -. DR PeptideAtlas; Q96T54; -. DR Antibodypedia; 45856; 81 antibodies from 19 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 AGR; HGNC:14465; -. 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; WRQGPDR; -. DR OrthoDB; 600333at2759; -. 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; 12 hits in 1140 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 97 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: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: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:SF340; POTASSIUM CHANNEL SUBFAMILY K MEMBER 17; 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; PR01095; TASKCHANNEL. DR SUPFAM; SSF81324; Voltage-gated potassium channels; 2. DR Genevisible; Q96T54; HS. 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 //