ID KCNQ5_HUMAN Reviewed; 932 AA. AC Q9NR82; A6NKT6; A6PVT6; A8MSQ5; B4DS33; B5MC83; B7ZL37; F5GZV0; Q17RE1; AC Q5VVP3; Q86W40; Q9NRN0; Q9NYA6; DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot. DT 09-JAN-2007, sequence version 3. DT 27-MAR-2024, entry version 189. DE RecName: Full=Potassium voltage-gated channel subfamily KQT member 5; DE AltName: Full=KQT-like 5; DE AltName: Full=Potassium channel subunit alpha KvLQT5; DE AltName: Full=Voltage-gated potassium channel subunit Kv7.5; GN Name=KCNQ5; 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 1), FUNCTION, SUBUNIT, AND SUBCELLULAR RP LOCATION. RC TISSUE=Brain; RX PubMed=10787416; DOI=10.1074/jbc.m002378200; RA Lerche C., Scherer C.R., Seebohm G., Derst C., Wei A.D., Busch A.E., RA Steinmeyer K.; RT "Molecular cloning and functional expression of KCNQ5, a potassium channel RT subunit that may contribute to neuronal M-current diversity."; RL J. Biol. Chem. 275:22395-22400(2000). RN [2] 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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 4). RC TISSUE=Placenta; 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). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 19-822 (ISOFORM 5). RC TISSUE=Brain; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] OF 36-932 (ISOFORMS 1; 2 AND 3). RC TISSUE=Brain; RX PubMed=10816588; DOI=10.1074/jbc.m003245200; RA Schroeder B.C., Hechenberger M., Weinreich F., Kubisch C., Jentsch T.J.; RT "KCNQ5, a novel potassium channel broadly expressed in brain, mediates M- RT type currents."; RL J. Biol. Chem. 275:24089-24095(2000). RN [6] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 36-932. RA Kananura C., Biervert B., Hechenberger M., Engels H., Steinlein O.K.; RT "The new voltage gated potassium channel KCNQ5 and early infantile RT convulsions."; RL Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [MRNA] OF 72-932 (ISOFORM 1). RC TISSUE=Brain, and Retina; RA Kniazeva M., Han M.; RT "A new gene of the voltage-gated potassium channel KCNQ family, KCNQ5, is a RT candidate gene for retinal disorders."; RL Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases. RN [8] RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND ACTIVATION BY RETICABINE. RX PubMed=11159685; DOI=10.1038/sj.bjp.0703861; RA Wickenden A.D., Zou A., Wagoner P.K., Jegla T.; RT "Characterization of KCNQ5/Q3 potassium channels expressed in mammalian RT cells."; RL Br. J. Pharmacol. 132:381-384(2001). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-831, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [10] RP INTERACTION WITH KCNQ1. RX PubMed=24855057; DOI=10.1161/atvbaha.114.303801; RA Oliveras A., Roura-Ferrer M., Sole L., de la Cruz A., Prieto A., RA Etxebarria A., Manils J., Morales-Cano D., Condom E., Soler C., RA Cogolludo A., Valenzuela C., Villarroel A., Comes N., Felipe A.; RT "Functional assembly of Kv7.1/Kv7.5 channels with emerging properties on RT vascular muscle physiology."; RL Arterioscler. Thromb. Vasc. Biol. 34:1522-1530(2014). RN [11] RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 361-394 AND 512-545. RX PubMed=29429937; DOI=10.1016/j.neuron.2018.01.035; RA Chang A., Abderemane-Ali F., Hura G.L., Rossen N.D., Gate R.E., Minor D.L.; RT "A calmodulin C-lobe Ca(2+)-dependent switch governs Kv7 channel RT function."; RL Neuron 97:836-852(2018). RN [12] RP VARIANTS [LARGE SCALE ANALYSIS] GLY-191 AND CYS-244. RX PubMed=16959974; DOI=10.1126/science.1133427; RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V., RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., RA Velculescu V.E.; RT "The consensus coding sequences of human breast and colorectal cancers."; RL Science 314:268-274(2006). RN [13] RP INVOLVEMENT IN MRD46, VARIANTS MRD46 GLY-145; ILE-341; ARG-369 AND ILE-429, RP CHARACTERIZATION OF VARIANTS MRD46 GLY-145; ILE-341; ARG-369 AND ILE-429, RP AND FUNCTION. RX PubMed=28669405; DOI=10.1016/j.ajhg.2017.05.016; RG CAUSES Study; RG EPGEN Study; RA Lehman A., Thouta S., Mancini G.M.S., Naidu S., van Slegtenhorst M., RA McWalter K., Person R., Mwenifumbo J., Salvarinova R., Guella I., RA McKenzie M.B., Datta A., Connolly M.B., Kalkhoran S.M., Poburko D., RA Friedman J.M., Farrer M.J., Demos M., Desai S., Claydon T.; RT "Loss-of-function and gain-of-function mutations in KCNQ5 cause RT intellectual disability or epileptic encephalopathy."; RL Am. J. Hum. Genet. 101:65-74(2017). CC -!- FUNCTION: Associates with KCNQ3 to form a potassium channel which CC contributes to M-type current, a slowly activating and deactivating CC potassium conductance which plays a critical role in determining the CC subthreshold electrical excitability of neurons. Therefore, it is CC important in the regulation of neuronal excitability. May contribute, CC with other potassium channels, to the molecular diversity of a CC heterogeneous population of M-channels, varying in kinetic and CC pharmacological properties, which underlie this physiologically CC important current. Insensitive to tetraethylammonium, but inhibited by CC barium, linopirdine and XE991. Activated by niflumic acid and the CC anticonvulsant retigabine. As the native M-channel, the potassium CC channel composed of KCNQ3 and KCNQ5 is also suppressed by activation of CC the muscarinic acetylcholine receptor CHRM1. CC {ECO:0000269|PubMed:10787416, ECO:0000269|PubMed:11159685, CC ECO:0000269|PubMed:28669405}. CC -!- SUBUNIT: Heteromultimer with KCNQ3 (PubMed:11159685, PubMed:10787416). CC Heterotetramer with KCNQ1; has a voltage-gated potassium channel CC activity (PubMed:24855057). {ECO:0000269|PubMed:10787416, CC ECO:0000269|PubMed:11159685, ECO:0000269|PubMed:24855057}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10787416, CC ECO:0000269|PubMed:11159685}; Multi-pass membrane protein CC {ECO:0000255}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=7; CC Name=1; CC IsoId=Q9NR82-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9NR82-2; Sequence=VSP_001014; CC Name=3; CC IsoId=Q9NR82-3; Sequence=VSP_001015; CC Name=4; CC IsoId=Q9NR82-4; Sequence=VSP_022318, VSP_022319; CC Name=5; CC IsoId=Q9NR82-5; Sequence=VSP_045487; CC Name=6; CC IsoId=Q9NR82-6; Sequence=VSP_056731; CC Name=7; CC IsoId=Q9NR82-7; Sequence=VSP_056730; CC -!- TISSUE SPECIFICITY: Strongly expressed in brain and skeletal muscle. In CC brain, expressed in cerebral cortex, occipital pole, frontal lobe and CC temporal lobe. Lower levels in hippocampus and putamen. Low to CC undetectable levels in medulla, cerebellum and thalamus. CC -!- DOMAIN: The segment S4 is probably the voltage-sensor and is CC characterized by a series of positively charged amino acids at every CC third position. {ECO:0000250}. CC -!- DISEASE: Intellectual developmental disorder, autosomal dominant 46 CC (MRD46) [MIM:617601]: A disorder characterized by significantly below CC average general intellectual functioning associated with impairments in CC adaptive behavior and manifested during the developmental period. MRD46 CC patients manifest developmental delay and mild to moderate intellectual CC disability. {ECO:0000269|PubMed:28669405}. Note=The disease is caused CC by variants affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the potassium channel family. KQT (TC 1.A.1.15) CC subfamily. Kv7.5/KCNQ5 sub-subfamily. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAG61495.1; Type=Erroneous initiation; Note=Truncated N-terminus.; 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; AF249278; AAF91335.1; -; mRNA. DR EMBL; AL445569; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL049845; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL360232; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL360236; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL365232; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; FO393414; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL513522; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL671823; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC050689; AAH50689.1; -; mRNA. DR EMBL; BC117359; AAI17360.1; -; mRNA. DR EMBL; BC143554; AAI43555.1; -; mRNA. DR EMBL; AK299550; BAG61495.1; ALT_INIT; mRNA. DR EMBL; AF202977; AAF69797.1; -; mRNA. DR EMBL; AJ272506; CAC88112.1; -; Genomic_DNA. DR EMBL; AJ272507; CAC88112.1; JOINED; Genomic_DNA. DR EMBL; AJ272508; CAC88112.1; JOINED; Genomic_DNA. DR EMBL; AJ272509; CAC88112.1; JOINED; Genomic_DNA. DR EMBL; AJ272510; CAC88112.1; JOINED; Genomic_DNA. DR EMBL; AJ272511; CAC88112.1; JOINED; Genomic_DNA. DR EMBL; AJ272512; CAC88112.1; JOINED; Genomic_DNA. DR EMBL; AJ272513; CAC88112.1; JOINED; Genomic_DNA. DR EMBL; AJ272514; CAC88112.1; JOINED; Genomic_DNA. DR EMBL; AJ272515; CAC88112.1; JOINED; Genomic_DNA. DR EMBL; AJ272516; CAC88112.1; JOINED; Genomic_DNA. DR EMBL; AJ272517; CAC88112.1; JOINED; Genomic_DNA. DR EMBL; AJ272518; CAC88112.1; JOINED; Genomic_DNA. DR EMBL; AJ272519; CAC88112.1; JOINED; Genomic_DNA. DR EMBL; AF263835; AAF73446.1; -; mRNA. DR CCDS; CCDS4976.1; -. [Q9NR82-1] DR CCDS; CCDS55034.1; -. [Q9NR82-6] DR CCDS; CCDS55035.1; -. [Q9NR82-5] DR CCDS; CCDS55037.1; -. [Q9NR82-2] DR RefSeq; NP_001153602.1; NM_001160130.1. [Q9NR82-2] DR RefSeq; NP_001153604.1; NM_001160132.1. [Q9NR82-3] DR RefSeq; NP_001153605.1; NM_001160133.1. [Q9NR82-6] DR RefSeq; NP_001153606.1; NM_001160134.1. [Q9NR82-5] DR RefSeq; NP_062816.2; NM_019842.3. [Q9NR82-1] DR PDB; 6B8Q; X-ray; 2.60 A; A/C/E/G=361-394, A/C/E/G=512-545. DR PDBsum; 6B8Q; -. DR AlphaFoldDB; Q9NR82; -. DR EMDB; EMD-33316; -. DR EMDB; EMD-33317; -. DR EMDB; EMD-33318; -. DR EMDB; EMD-33319; -. DR SMR; Q9NR82; -. DR BioGRID; 121149; 32. DR CORUM; Q9NR82; -. DR IntAct; Q9NR82; 14. DR STRING; 9606.ENSP00000345055; -. DR BindingDB; Q9NR82; -. DR ChEMBL; CHEMBL2925; -. DR DrugBank; DB00228; Enflurane. DR DrugBank; DB04953; Ezogabine. DR DrugBank; DB00996; Gabapentin. DR DrugBank; DB06089; ICA-105665. DR DrugBank; DB01110; Miconazole. DR DrugBank; DB01069; Promethazine. DR DrugCentral; Q9NR82; -. DR GuidetoPHARMACOLOGY; 564; -. DR iPTMnet; Q9NR82; -. DR PhosphoSitePlus; Q9NR82; -. DR BioMuta; KCNQ5; -. DR DMDM; 122065285; -. DR EPD; Q9NR82; -. DR jPOST; Q9NR82; -. DR MassIVE; Q9NR82; -. DR PaxDb; 9606-ENSP00000345055; -. DR PeptideAtlas; Q9NR82; -. DR ProteomicsDB; 1710; -. DR ProteomicsDB; 1972; -. DR ProteomicsDB; 25137; -. DR ProteomicsDB; 82300; -. [Q9NR82-1] DR ProteomicsDB; 82301; -. [Q9NR82-2] DR ProteomicsDB; 82302; -. [Q9NR82-3] DR ProteomicsDB; 82303; -. [Q9NR82-4] DR Antibodypedia; 17775; 279 antibodies from 31 providers. DR DNASU; 56479; -. DR Ensembl; ENST00000342056.6; ENSP00000345055.2; ENSG00000185760.18. [Q9NR82-6] DR Ensembl; ENST00000370392.5; ENSP00000359419.1; ENSG00000185760.18. [Q9NR82-4] DR Ensembl; ENST00000370398.6; ENSP00000359425.1; ENSG00000185760.18. [Q9NR82-1] DR Ensembl; ENST00000628967.2; ENSP00000486187.1; ENSG00000185760.18. [Q9NR82-5] DR Ensembl; ENST00000629977.2; ENSP00000485743.1; ENSG00000185760.18. [Q9NR82-2] DR GeneID; 56479; -. DR KEGG; hsa:56479; -. DR MANE-Select; ENST00000370398.6; ENSP00000359425.1; NM_019842.4; NP_062816.2. DR UCSC; uc003pgj.5; human. [Q9NR82-1] DR AGR; HGNC:6299; -. DR CTD; 56479; -. DR DisGeNET; 56479; -. DR GeneCards; KCNQ5; -. DR HGNC; HGNC:6299; KCNQ5. DR HPA; ENSG00000185760; Tissue enhanced (brain, skeletal muscle, tongue). DR MalaCards; KCNQ5; -. DR MIM; 607357; gene. DR MIM; 617601; phenotype. DR neXtProt; NX_Q9NR82; -. DR OpenTargets; ENSG00000185760; -. DR Orphanet; 178469; Autosomal dominant non-syndromic intellectual disability. DR PharmGKB; PA30077; -. DR VEuPathDB; HostDB:ENSG00000185760; -. DR eggNOG; KOG1419; Eukaryota. DR GeneTree; ENSGT00940000155933; -. DR HOGENOM; CLU_673604_0_0_1; -. DR InParanoid; Q9NR82; -. DR OrthoDB; 2911641at2759; -. DR PhylomeDB; Q9NR82; -. DR TreeFam; TF315186; -. DR PathwayCommons; Q9NR82; -. DR Reactome; R-HSA-1296072; Voltage gated Potassium channels. DR SignaLink; Q9NR82; -. DR SIGNOR; Q9NR82; -. DR BioGRID-ORCS; 56479; 20 hits in 1145 CRISPR screens. DR ChiTaRS; KCNQ5; human. DR GeneWiki; KCNQ5; -. DR GenomeRNAi; 56479; -. DR Pharos; Q9NR82; Tclin. DR PRO; PR:Q9NR82; -. DR Proteomes; UP000005640; Chromosome 6. DR RNAct; Q9NR82; Protein. DR Bgee; ENSG00000185760; Expressed in endothelial cell and 131 other cell types or tissues. DR ExpressionAtlas; Q9NR82; baseline and differential. DR GO; GO:0044305; C:calyx of Held; IEA:Ensembl. DR GO; GO:0030118; C:clathrin coat; IDA:UniProtKB. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0042734; C:presynaptic membrane; IEA:Ensembl. DR GO; GO:0008076; C:voltage-gated potassium channel complex; IDA:UniProtKB. DR GO; GO:0099508; F:voltage-gated monoatomic ion channel activity involved in regulation of presynaptic membrane potential; IEA:Ensembl. DR GO; GO:0005249; F:voltage-gated potassium channel activity; IDA:UniProtKB. DR GO; GO:0071805; P:potassium ion transmembrane transport; IDA:UniProtKB. DR Gene3D; 1.10.287.70; -; 1. DR Gene3D; 6.10.140.1910; -; 2. DR InterPro; IPR005821; Ion_trans_dom. DR InterPro; IPR003937; K_chnl_volt-dep_KCNQ. DR InterPro; IPR013821; K_chnl_volt-dep_KCNQ_C. DR PANTHER; PTHR47735; POTASSIUM VOLTAGE-GATED CHANNEL SUBFAMILY KQT MEMBER 4; 1. DR PANTHER; PTHR47735:SF8; POTASSIUM VOLTAGE-GATED CHANNEL SUBFAMILY KQT MEMBER 5; 1. DR Pfam; PF00520; Ion_trans; 1. DR Pfam; PF03520; KCNQ_channel; 1. DR PRINTS; PR00169; KCHANNEL. DR PRINTS; PR01459; KCNQCHANNEL. DR SUPFAM; SSF81324; Voltage-gated potassium channels; 1. DR Genevisible; Q9NR82; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cell membrane; Disease variant; KW Intellectual disability; Ion channel; Ion transport; Membrane; KW Phosphoprotein; Potassium; Potassium channel; Potassium transport; KW Reference proteome; Transmembrane; Transmembrane helix; Transport; KW Voltage-gated channel. FT CHAIN 1..932 FT /note="Potassium voltage-gated channel subfamily KQT member FT 5" FT /id="PRO_0000054040" FT TOPO_DOM 1..125 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 126..146 FT /note="Helical; Name=Segment S1" FT /evidence="ECO:0000255" FT TOPO_DOM 147..156 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 157..177 FT /note="Helical; Name=Segment S2" FT /evidence="ECO:0000255" FT TOPO_DOM 178..200 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 201..221 FT /note="Helical; Name=Segment S3" FT /evidence="ECO:0000255" FT TOPO_DOM 222..229 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 230..252 FT /note="Helical; Voltage-sensor; Name=Segment S4" FT /evidence="ECO:0000255" FT TOPO_DOM 253..266 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 267..287 FT /note="Helical; Name=Segment S5" FT /evidence="ECO:0000255" FT TOPO_DOM 288..298 FT /note="Extracellular" FT /evidence="ECO:0000255" FT INTRAMEM 299..319 FT /note="Pore-forming; Name=Segment H5" FT /evidence="ECO:0000255" FT TOPO_DOM 320..325 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 326..346 FT /note="Helical; Name=Segment S6" FT /evidence="ECO:0000255" FT TOPO_DOM 347..932 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT REGION 404..465 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 655..678 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 876..919 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 311..316 FT /note="Selectivity filter" FT /evidence="ECO:0000250" FT COMPBIAS 407..422 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 432..465 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 903..919 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 88 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9JK45" FT MOD_RES 447 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9JK45" FT MOD_RES 831 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT VAR_SEQ 407..416 FT /note="KKEQGEASSS -> N (in isoform 2)" FT /evidence="ECO:0000303|PubMed:10816588, FT ECO:0000303|PubMed:15489334" FT /id="VSP_001014" FT VAR_SEQ 407..416 FT /note="KKEQGEASSS -> NKFCSNKQKLFRMYTSRKQS (in isoform 3)" FT /evidence="ECO:0000303|PubMed:10816588" FT /id="VSP_001015" FT VAR_SEQ 408..416 FT /note="KEQGEASSS -> QNQQGESQSC (in isoform 7)" FT /evidence="ECO:0000305" FT /id="VSP_056730" FT VAR_SEQ 416..525 FT /note="Missing (in isoform 5)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_045487" FT VAR_SEQ 416..427 FT /note="SQKLSFKERVRM -> RFVISLLLHVCL (in isoform 4)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_022318" FT VAR_SEQ 416 FT /note="S -> SKFCSNKQKLFRMYTSRKQS (in isoform 6)" FT /evidence="ECO:0000305" FT /id="VSP_056731" FT VAR_SEQ 428..932 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_022319" FT VARIANT 145 FT /note="V -> G (in MRD46; decreased protein abundance; FT decreased potassium ion transmembrane transport; changed FT voltage-gated potassium channel activity; changed gating FT properties; dbSNP:rs1135401955)" FT /evidence="ECO:0000269|PubMed:28669405" FT /id="VAR_079219" FT VARIANT 191 FT /note="W -> G (in a colorectal cancer sample; somatic FT mutation)" FT /evidence="ECO:0000269|PubMed:16959974" FT /id="VAR_035772" FT VARIANT 244 FT /note="R -> C (in a colorectal cancer sample; somatic FT mutation; dbSNP:rs1314919218)" FT /evidence="ECO:0000269|PubMed:16959974" FT /id="VAR_035773" FT VARIANT 341 FT /note="L -> I (in MRD46; decreased protein abundance; FT decreased potassium ion transmembrane transport; changed FT voltage-gated potassium channel activity; changed gating FT properties; dbSNP:rs1135401956)" FT /evidence="ECO:0000269|PubMed:28669405" FT /id="VAR_079220" FT VARIANT 369 FT /note="P -> R (in MRD46; no effect on protein abundance; no FT effect on potassium ion transmembrane transport; increased FT voltage-gated potassium channel activity; changed gating FT properties resulting in a gain of function; FT dbSNP:rs1135401958)" FT /evidence="ECO:0000269|PubMed:28669405" FT /id="VAR_079221" FT VARIANT 429 FT /note="S -> I (in MRD46; no effect on protein abundance; no FT effect on potassium ion transmembrane transport; changed FT voltage-gated potassium channel activity; changed gating FT properties; dbSNP:rs1135401957)" FT /evidence="ECO:0000269|PubMed:28669405" FT /id="VAR_079222" FT CONFLICT 92..93 FT /note="KP -> SR (in Ref. 1; AAF91335)" FT /evidence="ECO:0000305" FT CONFLICT 109 FT /note="R -> Q (in Ref. 4; BAG61495)" FT /evidence="ECO:0000305" FT CONFLICT 129 FT /note="Y -> H (in Ref. 7; AAF73446)" FT /evidence="ECO:0000305" FT CONFLICT 727 FT /note="A -> V (in Ref. 7; AAF73446)" FT /evidence="ECO:0000305" FT CONFLICT 799 FT /note="T -> P (in Ref. 7; AAF73446)" FT /evidence="ECO:0000305" FT CONFLICT 857 FT /note="S -> R (in Ref. 7; AAF73446)" FT /evidence="ECO:0000305" FT CONFLICT 909 FT /note="R -> Q (in Ref. 7; AAF73446)" FT /evidence="ECO:0000305" FT HELIX 367..382 FT /evidence="ECO:0007829|PDB:6B8Q" FT HELIX 405..422 FT /evidence="ECO:0007829|PDB:6B8Q" SQ SEQUENCE 932 AA; 102179 MW; CB41C243FD2B00FC CRC64; MPRHHAGGEE GGAAGLWVKS GAAAAAAGGG RLGSGMKDVE SGRGRVLLNS AAARGDGLLL LGTRAATLGG GGGGLRESRR GKQGARMSLL GKPLSYTSSQ SCRRNVKYRR VQNYLYNVLE RPRGWAFIYH AFVFLLVFGC LILSVFSTIP EHTKLASSCL LILEFVMIVV FGLEFIIRIW SAGCCCRYRG WQGRLRFARK PFCVIDTIVL IASIAVVSAK TQGNIFATSA LRSLRFLQIL RMVRMDRRGG TWKLLGSVVY AHSKELITAW YIGFLVLIFS SFLVYLVEKD ANKEFSTYAD ALWWGTITLT TIGYGDKTPL TWLGRLLSAG FALLGISFFA LPAGILGSGF ALKVQEQHRQ KHFEKRRNPA ANLIQCVWRS YAADEKSVSI ATWKPHLKAL HTCSPTKKEQ GEASSSQKLS FKERVRMASP RGQSIKSRQA SVGDRRSPST DITAEGSPTK VQKSWSFNDR TRFRPSLRLK SSQPKPVIDA DTALGTDDVY DEKGCQCDVS VEDLTPPLKT VIRAIRIMKF HVAKRKFKET LRPYDVKDVI EQYSAGHLDM LCRIKSLQTR VDQILGKGQI TSDKKSREKI TAEHETTDDL SMLGRVVKVE KQVQSIESKL DCLLDIYQQV LRKGSASALA LASFQIPPFE CEQTSDYQSP VDSKDLSGSA QNSGCLSRST SANISRGLQF ILTPNEFSAQ TFYALSPTMH SQATQVPISQ SDGSAVAATN TIANQINTAP KPAAPTTLQI PPPLPAIKHL PRPETLHPNP AGLQESISDV TTCLVASKEN VQVAQSNLTK DRSMRKSFDM GGETLLSVCP MVPKDLGKSL SVQNLIRSTE ELNIQLSGSE SSGSRGSQDF YPKWRESKLF ITDEEVGPEE TETDTFDAAP QPAREAAFAS DSLRTGRSRS SQSICKAGES TDALSLPHVK LK //