KCNQ4_MOUSE
ID KCNQ4_MOUSE Reviewed; 696 AA.
AC Q9JK97; A2A7E8; Q8C9Y6;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Potassium voltage-gated channel subfamily KQT member 4;
DE AltName: Full=KQT-like 4;
DE AltName: Full=Potassium channel subunit alpha KvLQT4;
DE AltName: Full=Voltage-gated potassium channel subunit Kv7.4;
GN Name=Kcnq4;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 24-546.
RC STRAIN=C57BL/6J; TISSUE=Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 405-680.
RC STRAIN=BALB/cJ; TISSUE=Brain;
RX PubMed=11042367; DOI=10.1016/s0169-328x(00)00204-7;
RA Beisel K.W., Nelson N.C., Delimont D.C., Fritzsch B.;
RT "Longitudinal gradients of KCNQ4 expression in spiral ganglion and cochlear
RT hair cells correlate with progressive hearing loss in DFNA2(1).";
RL Brain Res. Mol. Brain Res. 82:137-149(2000).
RN [4]
RP TISSUE SPECIFICITY.
RX PubMed=10760300; DOI=10.1073/pnas.97.8.4333;
RA Kharkovets T., Hardelin J.-P., Safieddine S., Schweizer M., El-Amraoui A.,
RA Petit C., Jentsch T.J.;
RT "KCNQ4, a K+ channel mutated in a form of dominant deafness, is expressed
RT in the inner ear and the central auditory pathway.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:4333-4338(2000).
CC -!- FUNCTION: Probably important in the regulation of neuronal
CC excitability. May underlie a potassium current involved in regulating
CC the excitability of sensory cells of the cochlea.
CC -!- SUBUNIT: Homotetramer. May form heteromultimers with KCNQ3 (By
CC similarity). Interacts with HSP90AB1; promotes cell surface expression
CC of KCNQ4 (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:P56696}.
CC -!- SUBCELLULAR LOCATION: Basal cell membrane; Multi-pass membrane protein.
CC Note=Situated at the basal membrane of cochlear outer hair cells.
CC -!- TISSUE SPECIFICITY: In the inner ear expressed in the outer sensory
CC hair cells of the cochlea and in type I hair cells of the vestibular
CC organs. Also expressed in the postsynaptic membrane of the calyx nerve
CC endings innervating type I cells. In the brain expressed in neurons of
CC many, but not all, nuclei of the central auditory pathway. Absent from
CC most other brain regions. {ECO:0000269|PubMed:10760300}.
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 -!- DOMAIN: The A-domain tail carries the major determinants of channel
CC assembly specificity. Its coiled-coil region is Four-stranded (By
CC similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the potassium channel family. KQT (TC 1.A.1.15)
CC subfamily. Kv7.4/KCNQ4 sub-subfamily. {ECO:0000305}.
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DR EMBL; AL606924; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK040190; BAC30534.1; -; mRNA.
DR EMBL; AF249747; AAF66432.1; -; mRNA.
DR CCDS; CCDS38865.1; -.
DR RefSeq; NP_001074611.1; NM_001081142.1.
DR AlphaFoldDB; Q9JK97; -.
DR SMR; Q9JK97; -.
DR BioGRID; 208641; 2.
DR STRING; 10090.ENSMUSP00000030376; -.
DR iPTMnet; Q9JK97; -.
DR PhosphoSitePlus; Q9JK97; -.
DR PaxDb; Q9JK97; -.
DR PRIDE; Q9JK97; -.
DR ProteomicsDB; 263503; -.
DR ABCD; Q9JK97; 1 sequenced antibody.
DR Antibodypedia; 18036; 372 antibodies from 37 providers.
DR DNASU; 60613; -.
DR Ensembl; ENSMUST00000030376; ENSMUSP00000030376; ENSMUSG00000028631.
DR GeneID; 60613; -.
DR KEGG; mmu:60613; -.
DR UCSC; uc008unm.1; mouse.
DR CTD; 9132; -.
DR MGI; MGI:1926803; Kcnq4.
DR VEuPathDB; HostDB:ENSMUSG00000028631; -.
DR eggNOG; KOG1419; Eukaryota.
DR GeneTree; ENSGT00940000159209; -.
DR HOGENOM; CLU_011722_8_3_1; -.
DR InParanoid; Q9JK97; -.
DR OMA; YATCLHM; -.
DR OrthoDB; 1168835at2759; -.
DR PhylomeDB; Q9JK97; -.
DR TreeFam; TF315186; -.
DR Reactome; R-MMU-1296072; Voltage gated Potassium channels.
DR BioGRID-ORCS; 60613; 4 hits in 74 CRISPR screens.
DR PRO; PR:Q9JK97; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q9JK97; protein.
DR Bgee; ENSMUSG00000028631; Expressed in digastric muscle group and 78 other tissues.
DR Genevisible; Q9JK97; MM.
DR GO; GO:0009925; C:basal plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0008076; C:voltage-gated potassium channel complex; IBA:GO_Central.
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; IMP:MGI.
DR GO; GO:0042472; P:inner ear morphogenesis; IMP:MGI.
DR GO; GO:0071805; P:potassium ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0006813; P:potassium ion transport; IMP:MGI.
DR GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
DR GO; GO:0007605; P:sensory perception of sound; IMP:MGI.
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; IPR015573; KCQN4.
DR InterPro; IPR028325; VG_K_chnl.
DR PANTHER; PTHR11537; PTHR11537; 1.
DR PANTHER; PTHR11537:SF4; PTHR11537:SF4; 1.
DR Pfam; PF00520; Ion_trans; 1.
DR Pfam; PF03520; KCNQ_channel; 1.
DR PRINTS; PR01459; KCNQCHANNEL.
PE 2: Evidence at transcript level;
KW Cell membrane; Coiled coil; Hearing; Ion channel; Ion transport; Membrane;
KW Potassium; Potassium channel; Potassium transport; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport; Voltage-gated channel.
FT CHAIN 1..696
FT /note="Potassium voltage-gated channel subfamily KQT member
FT 4"
FT /id="PRO_0000054038"
FT TOPO_DOM 1..97
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 98..118
FT /note="Helical; Name=Segment S1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 119..131
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 132..152
FT /note="Helical; Name=Segment S2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 153..172
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 173..193
FT /note="Helical; Name=Segment S3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 194..201
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 202..224
FT /note="Helical; Voltage-sensor; Name=Segment S4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 225..237
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 238..258
FT /note="Helical; Name=Segment S5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 259..270
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT INTRAMEM 271..292
FT /note="Pore-forming; Name=Segment H5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 293..296
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 297..317
FT /note="Helical; Name=Segment S6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 318..695
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 445..484
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 546..650
FT /note="A-domain (Tetramerization)"
FT /evidence="ECO:0000250"
FT REGION 589..609
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 610..645
FT MOTIF 284..289
FT /note="Selectivity filter"
FT /evidence="ECO:0000250"
FT COMPBIAS 467..484
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 445
FT /note="S -> I (in Ref. 3; AAF66432)"
FT /evidence="ECO:0000305"
FT CONFLICT 502
FT /note="C -> S (in Ref. 3; AAF66432)"
FT /evidence="ECO:0000305"
FT CONFLICT 533
FT /note="T -> S (in Ref. 2; BAC30534)"
FT /evidence="ECO:0000305"
FT CONFLICT 608
FT /note="T -> A (in Ref. 3; AAF66432)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 696 AA; 77057 MW; 762B19DA32043E95 CRC64;
MAEAPPRRLG LGPPPGDAPR AELVALTAVQ SEQGEAGGGG SPRRLGLLGS PLPPGAPLPG
PGSGSGSACG GQRSSAAQKR YRRLQNWVYN VLERPRGWAF VYHVFIFLLV FSCLVLSVLS
TIQEHQELAN ECLLILEFVM IVVFGLEYII RVWSAGCCCR YRGWQGRFRF ARKPFCVIDF
IVFVASVAVI AAGTQGNIFA TSALRSMRFL QILRMVRMDR RGGTWKLLGS VVYAHSKELI
TAWYIGFLVL IFASFLVYLA EKDANSDFSS YADSLWWGTI TLTTIGYGDK TPHTWLGRVL
AAGFALLGIS FFALPAGILG SGFALKVQEQ HRQKHFEKRR MPAANLIQAA WRLYSTDTSR
AYLTATWYYY DSILPSFREL ALLFEHIQRA RNGGLRPLEV RRAPVPDGAP SRYPPVATCH
RPGSASFCPG ESSRMGIKDR IRISSSQKRT GPSKQHLAPP PIPTSPSSEQ VGEASSPSKV
QKSWSFNDRT RFRASLRLKP RCSAEEGPSE EVAEEKSYQC ELTVDDVMPA VKTVIRSVRI
LKFLVAKRKF KETLRPYDVK DVIEQYSAGH LDMLGRIKSL QARVDQIVGR GPGDRKTREK
GDKGPSDTEA VDEISMMGRV VKVEKQVQSI EHKLDLLLGF YSRCLRSGTS ASLGTVQVPL
FDPDITSDYH SPVDHEDISV SAQTLSISRS VSTNMD
