KCNQ5_HUMAN
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 03-AUG-2022, entry version 180.
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};
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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 SMR; Q9NR82; -.
DR BioGRID; 121149; 24.
DR CORUM; Q9NR82; -.
DR IntAct; Q9NR82; 7.
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; Q9NR82; -.
DR PeptideAtlas; Q9NR82; -.
DR PRIDE; 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; 247 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 CTD; 56479; -.
DR DisGeNET; 56479; -.
DR GeneCards; KCNQ5; -.
DR HGNC; HGNC:6299; KCNQ5.
DR HPA; ENSG00000185760; Group enriched (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; 1168835at2759; -.
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; 19 hits in 1067 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 129 other tissues.
DR ExpressionAtlas; Q9NR82; baseline and differential.
DR Genevisible; Q9NR82; HS.
DR GO; GO:0030118; C:clathrin coat; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0008076; C:voltage-gated potassium channel complex; IDA:UniProtKB.
DR GO; GO:0005516; F:calmodulin binding; IBA:GO_Central.
DR GO; GO:0005251; F:delayed rectifier potassium channel activity; IBA:GO_Central.
DR GO; GO:0005249; F:voltage-gated potassium channel activity; IDA:UniProtKB.
DR GO; GO:0071805; P:potassium ion transmembrane transport; IDA:UniProtKB.
DR GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
DR InterPro; IPR005821; Ion_trans_dom.
DR InterPro; IPR003937; K_chnl_volt-dep_KCNQ.
DR InterPro; IPR013821; K_chnl_volt-dep_KCNQ_C.
DR InterPro; IPR043238; KCNQ5.
DR InterPro; IPR028325; VG_K_chnl.
DR PANTHER; PTHR11537; PTHR11537; 1.
DR PANTHER; PTHR11537:SF128; PTHR11537:SF128; 1.
DR Pfam; PF00520; Ion_trans; 1.
DR Pfam; PF03520; KCNQ_channel; 1.
DR PRINTS; PR01459; KCNQCHANNEL.
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
