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Protein

Potassium voltage-gated channel subfamily KQT member 5

Gene

Kcnq5

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Probably important in the regulation of neuronal excitability. Associates with KCNQ3 to form a potassium channel which contributes to M-type current, a slowly activating and deactivating potassium conductance which plays a critical role in determining the subthreshold electrical excitability of neurons. May contribute, with other potassium channels, to the molecular diversity of a heterogeneous population of M-channels, varying in kinetic and pharmacological properties, which underlie this physiologically important current (By similarity).By similarity

GO - Molecular functioni

  • voltage-gated potassium channel activity Source: MGI

GO - Biological processi

  • potassium ion transport Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Ion channel, Potassium channel, Voltage-gated channel

Keywords - Biological processi

Ion transport, Potassium transport, Transport

Keywords - Ligandi

Potassium

Enzyme and pathway databases

ReactomeiR-MMU-1296072. Voltage gated Potassium channels.

Protein family/group databases

TCDBi1.A.1.15.5. the voltage-gated ion channel (vic) superfamily.

Names & Taxonomyi

Protein namesi
Recommended name:
Potassium voltage-gated channel subfamily KQT member 5
Alternative name(s):
KQT-like 5
Potassium channel subunit alpha KvLQT5
Voltage-gated potassium channel subunit Kv7.5
Gene namesi
Name:Kcnq5
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 1

Organism-specific databases

MGIiMGI:1924937. Kcnq5.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei127 – 14721Helical; Name=Segment S1Sequence analysisAdd
BLAST
Transmembranei158 – 17821Helical; Name=Segment S2Sequence analysisAdd
BLAST
Transmembranei202 – 22221Helical; Name=Segment S3Sequence analysisAdd
BLAST
Transmembranei231 – 25323Helical; Voltage-sensor; Name=Segment S4Sequence analysisAdd
BLAST
Transmembranei268 – 28821Helical; Name=Segment S5Sequence analysisAdd
BLAST
Intramembranei300 – 32021Pore-forming; Name=Segment H5Sequence analysisAdd
BLAST
Transmembranei327 – 34721Helical; Name=Segment S6Sequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 933933Potassium voltage-gated channel subfamily KQT member 5PRO_0000054041Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei89 – 891PhosphoserineCombined sources
Modified residuei448 – 4481PhosphoserineCombined sources
Modified residuei832 – 8321PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9JK45.
PaxDbiQ9JK45.
PRIDEiQ9JK45.

PTM databases

iPTMnetiQ9JK45.
PhosphoSiteiQ9JK45.

Expressioni

Gene expression databases

BgeeiQ9JK45.
ExpressionAtlasiQ9JK45. baseline and differential.
GenevisibleiQ9JK45. MM.

Interactioni

Subunit structurei

Heteromultimer with KCNQ3 (By similarity). Forms homomers when expressed in Xenopus oocytes (PubMed:15963599). Heterotetramer with KCNQ5; have a voltage-gated potassium channel activity (By similarity).By similarity1 Publication

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000110955.

Structurei

3D structure databases

ProteinModelPortaliQ9JK45.
SMRiQ9JK45. Positions 161-399.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi312 – 3176Selectivity filterBy similarity

Domaini

The segment S4 is probably the voltage-sensor and is characterized by a series of positively charged amino acids at every third position.By similarity

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG1419. Eukaryota.
COG1226. LUCA.
GeneTreeiENSGT00550000074513.
HOGENOMiHOG000220839.
HOVERGENiHBG059014.
InParanoidiQ9JK45.
KOiK04930.
OrthoDBiEOG73804Z.
PhylomeDBiQ9JK45.

Family and domain databases

InterProiIPR005821. Ion_trans_dom.
IPR003937. K_chnl_volt-dep_KCNQ.
IPR013821. K_chnl_volt-dep_KCNQ_C.
IPR028325. VG_K_chnl.
[Graphical view]
PANTHERiPTHR11537. PTHR11537. 3 hits.
PfamiPF00520. Ion_trans. 1 hit.
PF03520. KCNQ_channel. 1 hit.
[Graphical view]
PRINTSiPR00169. KCHANNEL.
PR01459. KCNQCHANNEL.

Sequencei

Sequence statusi: Complete.

Q9JK45-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPRHHAGGEE GGAAGLWVRS GAAAAAGAGG GRPGSGMKDV ESGRGRVLLN
60 70 80 90 100
SAAARGDGLL LLGTRAAALG GGGGGLRESR RGKQGARMSL LGKPLSYTSS
110 120 130 140 150
QSCRRNVKYR RVQNYLYNVL ERPRGWAFVY HAFVFLLVFG CLILSVFSTI
160 170 180 190 200
PEHTKLASSC LLILEFVMIV VFGLEFIIRI WSAGCCCRYR GWQGRLRFAR
210 220 230 240 250
KPFCVIDTIV LIASIAVVSA KTQGNIFATS ALRSLRFLQI LRMVRMDRRG
260 270 280 290 300
GTWKLLGSVV YAHSKELITA WYIGFLVLIF SSFLVYLVEK DANKEFSTYA
310 320 330 340 350
DALWWGTITL TTIGYGDKTP LTWLGRLLSA GFALLGISFF ALPAGILGSG
360 370 380 390 400
FALKVQEQHR QKHFEKRRNP AANLIQCVWR SYAADEKSVS IATWKPHLKA
410 420 430 440 450
LHTCSPTKKE QGEASSSQKL SFKERVRMAS PRGQSIKSRQ ASVGDRRSPS
460 470 480 490 500
TDITAEGSPT KVQKSWSFND RTRFRPSLRL KSSQPKPVID ADTALGIDDV
510 520 530 540 550
YDEKGCQCDV SVEDLTPPLK TVIRAIRIMK FHVAKRKFKE TLRPYDVKDV
560 570 580 590 600
IEQYSAGHLD MLCRIKSLQT RVDQILGKGQ MTSDKKSREK ITAEHETTDD
610 620 630 640 650
PSMLARVVKV EKQVQSIESK LDCLLDIYQQ VLRKGSASAL TLASFQIPPF
660 670 680 690 700
ECEQTSDYQS PVDSKDLSGS AQNSGCLTRS ASANISRGLQ FILTPNEFSA
710 720 730 740 750
QTFYALSPTM HSQATQVPMS QNDGSSVVAT NNIANQISAA PKPAAPTTLQ
760 770 780 790 800
IPPPLSAIKH LSRPEPLLSN PTGLQESISD VTTCLVASKE SVQFAQSNLT
810 820 830 840 850
KDRSLRKSFD MGGETLLSVR PMVPKDLGKS LSVQNLIRST EELNLQFSGS
860 870 880 890 900
ESSGSRGSQD FYPKWRESKL FITDEEVGAE ETETDTFDGT PPPAGEAAFS
910 920 930
SDSLRTGRSR SSQNICKTGD STDALSLPHV KLN
Length:933
Mass (Da):102,258
Last modified:January 9, 2007 - v2
Checksum:i92B8C314D7144288
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti636 – 6361S → Y in BAC28145 (PubMed:16141072).Curated
Sequence conflicti923 – 9231D → G in BAC28145 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY679158 mRNA. Translation: AAT76442.1.
AF263836 mRNA. Translation: AAF73447.1.
AK033079 mRNA. Translation: BAC28145.1.
CCDSiCCDS35525.1.
RefSeqiNP_076361.1. NM_023872.3.
UniGeneiMm.336519.
Mm.403737.

Genome annotation databases

EnsembliENSMUST00000029667; ENSMUSP00000029667; ENSMUSG00000028033.
GeneIDi226922.
KEGGimmu:226922.
UCSCiuc007alq.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY679158 mRNA. Translation: AAT76442.1.
AF263836 mRNA. Translation: AAF73447.1.
AK033079 mRNA. Translation: BAC28145.1.
CCDSiCCDS35525.1.
RefSeqiNP_076361.1. NM_023872.3.
UniGeneiMm.336519.
Mm.403737.

3D structure databases

ProteinModelPortaliQ9JK45.
SMRiQ9JK45. Positions 161-399.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000110955.

Protein family/group databases

TCDBi1.A.1.15.5. the voltage-gated ion channel (vic) superfamily.

PTM databases

iPTMnetiQ9JK45.
PhosphoSiteiQ9JK45.

Proteomic databases

MaxQBiQ9JK45.
PaxDbiQ9JK45.
PRIDEiQ9JK45.

Protocols and materials databases

DNASUi226922.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000029667; ENSMUSP00000029667; ENSMUSG00000028033.
GeneIDi226922.
KEGGimmu:226922.
UCSCiuc007alq.2. mouse.

Organism-specific databases

CTDi56479.
MGIiMGI:1924937. Kcnq5.

Phylogenomic databases

eggNOGiKOG1419. Eukaryota.
COG1226. LUCA.
GeneTreeiENSGT00550000074513.
HOGENOMiHOG000220839.
HOVERGENiHBG059014.
InParanoidiQ9JK45.
KOiK04930.
OrthoDBiEOG73804Z.
PhylomeDBiQ9JK45.

Enzyme and pathway databases

ReactomeiR-MMU-1296072. Voltage gated Potassium channels.

Miscellaneous databases

ChiTaRSiKcnq5. mouse.
NextBioi378396.
PROiQ9JK45.
SOURCEiSearch...

Gene expression databases

BgeeiQ9JK45.
ExpressionAtlasiQ9JK45. baseline and differential.
GenevisibleiQ9JK45. MM.

Family and domain databases

InterProiIPR005821. Ion_trans_dom.
IPR003937. K_chnl_volt-dep_KCNQ.
IPR013821. K_chnl_volt-dep_KCNQ_C.
IPR028325. VG_K_chnl.
[Graphical view]
PANTHERiPTHR11537. PTHR11537. 3 hits.
PfamiPF00520. Ion_trans. 1 hit.
PF03520. KCNQ_channel. 1 hit.
[Graphical view]
PRINTSiPR00169. KCHANNEL.
PR01459. KCNQCHANNEL.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The KCNQ5 potassium channel from mouse: a broadly expressed M-current like potassium channel modulated by zinc, pH, and volume changes."
    Jensen H.S., Callo K., Jespersen T., Jensen B.S., Olesen S.-P.
    Brain Res. Mol. Brain Res. 139:52-62(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION, SUBUNIT, MISCELLANEOUS.
    Tissue: Brain.
  2. "A new gene of the voltage-gated potassium channel KCNQ family, KCNQ5, is a candidate gene for retinal disorders."
    Kniazeva M., Han M.
    Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 56-933.
    Strain: BALB/cJ.
    Tissue: Brain.
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 362-933.
    Strain: C57BL/6J.
    Tissue: Brain cortex.
  4. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-89; SER-448 AND SER-832, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain and Lung.

Entry informationi

Entry nameiKCNQ5_MOUSE
AccessioniPrimary (citable) accession number: Q9JK45
Secondary accession number(s): Q4QXS5, Q8BSF6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 2001
Last sequence update: January 9, 2007
Last modified: May 11, 2016
This is version 119 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

The activity of this channel is modulated by zinc, pH and volume changes.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.