KCNQ5_MOUSE
ID KCNQ5_MOUSE Reviewed; 933 AA.
AC Q9JK45; Q4QXS5; Q8BSF6;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 153.
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 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 [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND
RP MISCELLANEOUS.
RC TISSUE=Brain;
RX PubMed=15963599; DOI=10.1016/j.molbrainres.2005.05.007;
RA Jensen H.S., Callo K., Jespersen T., Jensen B.S., Olesen S.-P.;
RT "The KCNQ5 potassium channel from mouse: a broadly expressed M-current like
RT potassium channel modulated by zinc, pH, and volume changes.";
RL Brain Res. Mol. Brain Res. 139:52-62(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 56-933.
RC STRAIN=BALB/cJ; TISSUE=Brain;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 362-933.
RC STRAIN=C57BL/6J; TISSUE=Brain cortex;
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-89; SER-448 AND SER-832, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Lung;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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. {ECO:0000269|PubMed:15963599}.
CC -!- SUBUNIT: Heteromultimer with KCNQ3. Heterotetramer with KCNQ1; has a
CC voltage-gated potassium channel activity.
CC {ECO:0000250|UniProtKB:Q9NR82}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15963599};
CC Multi-pass membrane protein {ECO:0000255}.
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 -!- MISCELLANEOUS: The activity of this channel is modulated by zinc, pH
CC and volume changes. {ECO:0000269|PubMed:15963599}.
CC -!- SIMILARITY: Belongs to the potassium channel family. KQT (TC 1.A.1.15)
CC subfamily. Kv7.5/KCNQ5 sub-subfamily. {ECO:0000305}.
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DR EMBL; AY679158; AAT76442.1; -; mRNA.
DR EMBL; AF263836; AAF73447.1; -; mRNA.
DR EMBL; AK033079; BAC28145.1; -; mRNA.
DR CCDS; CCDS35525.1; -.
DR RefSeq; NP_076361.1; NM_023872.3.
DR AlphaFoldDB; Q9JK45; -.
DR SMR; Q9JK45; -.
DR IntAct; Q9JK45; 1.
DR MINT; Q9JK45; -.
DR STRING; 10090.ENSMUSP00000110955; -.
DR TCDB; 1.A.1.15.5; the voltage-gated ion channel (vic) superfamily.
DR iPTMnet; Q9JK45; -.
DR PhosphoSitePlus; Q9JK45; -.
DR PaxDb; Q9JK45; -.
DR PRIDE; Q9JK45; -.
DR ProteomicsDB; 269206; -.
DR Antibodypedia; 17775; 247 antibodies from 31 providers.
DR DNASU; 226922; -.
DR Ensembl; ENSMUST00000029667; ENSMUSP00000029667; ENSMUSG00000028033.
DR GeneID; 226922; -.
DR KEGG; mmu:226922; -.
DR UCSC; uc007alq.2; mouse.
DR CTD; 56479; -.
DR MGI; MGI:1924937; Kcnq5.
DR VEuPathDB; HostDB:ENSMUSG00000028033; -.
DR eggNOG; KOG1419; Eukaryota.
DR GeneTree; ENSGT00940000155933; -.
DR InParanoid; Q9JK45; -.
DR PhylomeDB; Q9JK45; -.
DR Reactome; R-MMU-1296072; Voltage gated Potassium channels.
DR BioGRID-ORCS; 226922; 5 hits in 74 CRISPR screens.
DR ChiTaRS; Kcnq5; mouse.
DR PRO; PR:Q9JK45; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q9JK45; protein.
DR Bgee; ENSMUSG00000028033; Expressed in caudate-putamen and 157 other tissues.
DR ExpressionAtlas; Q9JK45; baseline and differential.
DR Genevisible; Q9JK45; MM.
DR GO; GO:0030118; C:clathrin coat; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0008076; C:voltage-gated potassium channel complex; ISS: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:MGI.
DR GO; GO:0071805; P:potassium ion transmembrane transport; ISO:MGI.
DR GO; GO:0006813; P:potassium ion transport; IDA:MGI.
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 Cell membrane; Ion channel; Ion transport; Membrane; Phosphoprotein;
KW Potassium; Potassium channel; Potassium transport; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport; Voltage-gated channel.
FT CHAIN 1..933
FT /note="Potassium voltage-gated channel subfamily KQT member
FT 5"
FT /id="PRO_0000054041"
FT TOPO_DOM 1..126
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 127..147
FT /note="Helical; Name=Segment S1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 148..157
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 158..178
FT /note="Helical; Name=Segment S2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 179..201
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 202..222
FT /note="Helical; Name=Segment S3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 223..230
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 231..253
FT /note="Helical; Voltage-sensor; Name=Segment S4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 254..267
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 268..288
FT /note="Helical; Name=Segment S5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 289..299
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT INTRAMEM 300..320
FT /note="Pore-forming; Name=Segment H5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 321..326
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 327..347
FT /note="Helical; Name=Segment S6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 348..933
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 405..465
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 578..598
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 878..933
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 312..317
FT /note="Selectivity filter"
FT /evidence="ECO:0000250"
FT COMPBIAS 408..423
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 433..465
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 582..598
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 902..921
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 89
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 448
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 832
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 636
FT /note="S -> Y (in Ref. 3; BAC28145)"
FT /evidence="ECO:0000305"
FT CONFLICT 923
FT /note="D -> G (in Ref. 3; BAC28145)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 933 AA; 102258 MW; 92B8C314D7144288 CRC64;
MPRHHAGGEE GGAAGLWVRS GAAAAAGAGG GRPGSGMKDV ESGRGRVLLN SAAARGDGLL
LLGTRAAALG GGGGGLRESR RGKQGARMSL LGKPLSYTSS QSCRRNVKYR RVQNYLYNVL
ERPRGWAFVY HAFVFLLVFG CLILSVFSTI PEHTKLASSC LLILEFVMIV VFGLEFIIRI
WSAGCCCRYR GWQGRLRFAR KPFCVIDTIV LIASIAVVSA KTQGNIFATS ALRSLRFLQI
LRMVRMDRRG GTWKLLGSVV YAHSKELITA WYIGFLVLIF SSFLVYLVEK DANKEFSTYA
DALWWGTITL TTIGYGDKTP LTWLGRLLSA GFALLGISFF ALPAGILGSG FALKVQEQHR
QKHFEKRRNP AANLIQCVWR SYAADEKSVS IATWKPHLKA LHTCSPTKKE QGEASSSQKL
SFKERVRMAS PRGQSIKSRQ ASVGDRRSPS TDITAEGSPT KVQKSWSFND RTRFRPSLRL
KSSQPKPVID ADTALGIDDV YDEKGCQCDV SVEDLTPPLK TVIRAIRIMK FHVAKRKFKE
TLRPYDVKDV IEQYSAGHLD MLCRIKSLQT RVDQILGKGQ MTSDKKSREK ITAEHETTDD
PSMLARVVKV EKQVQSIESK LDCLLDIYQQ VLRKGSASAL TLASFQIPPF ECEQTSDYQS
PVDSKDLSGS AQNSGCLTRS ASANISRGLQ FILTPNEFSA QTFYALSPTM HSQATQVPMS
QNDGSSVVAT NNIANQISAA PKPAAPTTLQ IPPPLSAIKH LSRPEPLLSN PTGLQESISD
VTTCLVASKE SVQFAQSNLT KDRSLRKSFD MGGETLLSVR PMVPKDLGKS LSVQNLIRST
EELNLQFSGS ESSGSRGSQD FYPKWRESKL FITDEEVGAE ETETDTFDGT PPPAGEAAFS
SDSLRTGRSR SSQNICKTGD STDALSLPHV KLN
