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Protein

Potassium voltage-gated channel subfamily KQT member 2

Gene

Kcnq2

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 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 with essentially identical properties to the channel underlying the native M-current, a slowly activating and deactivating potassium conductance which plays a critical role in determining the subthreshold electrical excitability of neurons as well as the responsiveness to synaptic inputs. KCNQ2 current is blocked by barium and tetraethylammonium whereas 4-aminopyridine and charybdotoxin have no effect on KCNQ2 current. Tyrosine kinase inhibitors genistein or herbimycin a markedly down-regulate KCNQ2 current. Muscarinic agonist oxotremorine-M suppress KCNQ2/KCNQ3 current in CHO cells in which cloned KCNQ2/KCNQ3 channels were coexpressed with human M1 muscarinic receptors.

GO - Molecular functioni

  • delayed rectifier potassium channel activity Source: GO_Central
  • protein N-terminus binding Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Ion channel, Potassium channel, Voltage-gated channel

Keywords - Biological processi

Ion transport, Potassium transport, Transport

Keywords - Ligandi

Potassium

Names & Taxonomyi

Protein namesi
Recommended name:
Potassium voltage-gated channel subfamily KQT member 2
Alternative name(s):
KQT-like 2
Potassium channel subunit alpha KvLQT2
Voltage-gated potassium channel subunit Kv7.2
Gene namesi
Name:Kcnq2
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi621504. Kcnq2.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei92 – 11221Helical; Name=Segment S1Sequence analysisAdd
BLAST
Topological domaini113 – 12210ExtracellularSequence analysis
Transmembranei123 – 14321Helical; Name=Segment S2Sequence analysisAdd
BLAST
Topological domaini144 – 16623CytoplasmicSequence analysisAdd
BLAST
Transmembranei167 – 18721Helical; Name=Segment S3Sequence analysisAdd
BLAST
Topological domaini188 – 19710ExtracellularSequence analysis
Transmembranei198 – 22124Helical; Voltage-sensor; Name=Segment S4Sequence analysisAdd
BLAST
Topological domaini222 – 23110CytoplasmicSequence analysis
Transmembranei232 – 25221Helical; Name=Segment S5Sequence analysisAdd
BLAST
Topological domaini253 – 26412ExtracellularSequence analysisAdd
BLAST
Intramembranei265 – 28521Pore-forming; Name=Segment H5Sequence analysisAdd
BLAST
Topological domaini286 – 2916ExtracellularSequence analysis
Transmembranei292 – 31221Helical; Name=Segment S6Sequence analysisAdd
BLAST
Topological domaini313 – 852540CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL5530.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 852852Potassium voltage-gated channel subfamily KQT member 2PRO_0000054032Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei52 – 521Phosphoserine; by PKABy similarity
Modified residuei448 – 4481PhosphoserineBy similarity
Modified residuei450 – 4501PhosphoserineBy similarity
Modified residuei454 – 4541PhosphoserineBy similarity
Modified residuei458 – 4581PhosphoserineBy similarity
Modified residuei460 – 4601PhosphoserineBy similarity
Modified residuei489 – 4891PhosphoserineCombined sources
Modified residuei655 – 6551PhosphoserineCombined sources
Modified residuei781 – 7811PhosphoserineCombined sources
Modified residuei783 – 7831PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiO88943.
PRIDEiO88943.

PTM databases

iPTMnetiO88943.
PhosphoSiteiO88943.
SwissPalmiO88943.

Expressioni

Tissue specificityi

Expressed in brain and sympathetic ganglia. In brain, expressed in cortex, hippocampus, and cerebellum. In sympathetic ganglia, expressed at lower levels in celiac ganglia and superior mesenteric ganglia than in superior cervical ganglia.1 Publication

Interactioni

Subunit structurei

Heteromultimer with KCNQ3.

Binary interactionsi

WithEntry#Exp.IntActNotes
Calm3P621614EBI-7900557,EBI-397530

GO - Molecular functioni

  • protein N-terminus binding Source: RGD

Protein-protein interaction databases

BioGridi251003. 2 interactions.
IntActiO88943. 1 interaction.
MINTiMINT-8393842.
STRINGi10116.ENSRNOP00000043732.

Chemistry

BindingDBiO88943.

Structurei

3D structure databases

ProteinModelPortaliO88943.
SMRiO88943. Positions 598-627.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi277 – 2826Selectivity 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.
HOGENOMiHOG000220839.
HOVERGENiHBG059014.
InParanoidiO88943.
KOiK04927.

Family and domain databases

InterProiIPR020969. Ankyrin-G_BS.
IPR005821. Ion_trans_dom.
IPR003937. K_chnl_volt-dep_KCNQ.
IPR003947. K_chnl_volt-dep_KCNQ2.
IPR013821. K_chnl_volt-dep_KCNQ_C.
IPR028325. VG_K_chnl.
[Graphical view]
PANTHERiPTHR11537. PTHR11537. 4 hits.
PfamiPF00520. Ion_trans. 1 hit.
PF03520. KCNQ_channel. 1 hit.
PF11956. KCNQC3-Ank-G_bd. 1 hit.
[Graphical view]
PRINTSiPR00169. KCHANNEL.
PR01461. KCNQ2CHANNEL.
PR01459. KCNQCHANNEL.

Sequences (9)i

Sequence statusi: Complete.

This entry describes 9 isoformsi produced by alternative splicing. AlignAdd to basket

Note: Splice isoforms fell into three classes, those that contain an in frame exon 16 (Isoforms A-I) those that contain an out-of-frame exon 16 due to an alternative splice junction in exon 14 and those that terminate prematurely to exon 16. Only the forms containing an in frame exon 16 are able to form functional channels. A similar splice pattern is also produced for splice variants that contain an out-of-frame exon 16. A wide variety of different truncated isoforms were isolated for splice variants that terminate prematurely to exon 16.

Isoform A (identifier: O88943-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MVQKSRNGGV YPGTSGEKKL KVGFVGLDPG APDSTRDGAL LIAGSEAPKR
60 70 80 90 100
GSVLSKPRTG GAGAGKPPKR NAFYRKLQNF LYNVLERPRG WAFIYHAYVF
110 120 130 140 150
LLVFSCLVLS VFSTIKEYEK SSEGALYILE IVTIVVFGVE YFVRIWAAGC
160 170 180 190 200
CCRYRGWRGR LKFARKPFCV IDIMVLIASI AVLAAGSQGN VFATSALRSL
210 220 230 240 250
RFLQILRMIR MDRRGGTWKL LGSVVYAHSK ELVTAWYIGF LCLILASFLV
260 270 280 290 300
YLAEKGENDH FDTYADALWW GLITLTTIGY GDKYPQTWNG RLLAATFTLI
310 320 330 340 350
GVSFFALPAG ILGSGFALKV QEQHRQKHFE KRRNPAAGLI QSAWRFYATN
360 370 380 390 400
LSRTDLHSTW QYYERTVTVP MISSQTQTYG ASRLIPPLNQ LEMLRNLKSK
410 420 430 440 450
SGLTFRKEPQ PEPSPSQKVS LKDRVFSSPR GVAAKGKGSP QAQTVRRSPS
460 470 480 490 500
ADQSLDDSPS KVPKSWSFGD RSRARQAFRI KGAASRQNSE EASLPGEDIV
510 520 530 540 550
EDNKSCNCEF VTEDLTPGLK VSIRAVCVMR FLVSKRKFKE SLRPYDVMDV
560 570 580 590 600
IEQYSAGHLD MLSRIKSLQS RVDQIVGRGP TITDKDRTKG PAETELPEDP
610 620 630 640 650
SMMGRLGKVE KQVLSMEKKL DFLVSIYTQR MGIPPAETEA YFGAKEPEPA
660 670 680 690 700
PPYHSPEDSR DHADKHGCII KIVRSTSSTG QRKYAAPPVM PPAECPPSTS
710 720 730 740 750
WQQSHQRHGT SPVGDHGSLV RIPPPPAHER SLSAYSGGNR ASTEFLRLEG
760 770 780 790 800
TPACRPSEAA LRDSDTSISI PSVDHEELER SFSGFSISQS KENLNALASC
810 820 830 840 850
YAAVAPCAKV RPYIAEGESD TDSDLCTPCG PPPRSATGEG PFGDVAWAGP

RK
Length:852
Mass (Da):93,949
Last modified:November 1, 1998 - v1
Checksum:i82A5FE462A5F259A
GO
Isoform B (identifier: O88943-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     417-428: Missing.
     571-571: R → RIDMIVGPPPPSTPRHKKYPTKGPTAPSRESPQYSPR

Show »
Length:876
Mass (Da):96,527
Checksum:i06AE81A7E5C27C4D
GO
Isoform C (identifier: O88943-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     373-382: Missing.

Show »
Length:842
Mass (Da):92,938
Checksum:i308CAC7617E71566
GO
Isoform D (identifier: O88943-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     416-416: S → SKGRPCRGCLCGCRPGHSS
     491-491: Missing.

Show »
Length:869
Mass (Da):95,676
Checksum:iADBA2B0BFC7352E5
GO
Isoform E (identifier: O88943-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     416-416: S → SKGRPCRGCLCGCRPGHSS

Show »
Length:870
Mass (Da):95,806
Checksum:iEFE03926DD670D01
GO
Isoform F (identifier: O88943-6) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     373-382: Missing.
     416-416: S → SKGRPCRGCLCGCRPGHSS
     491-491: Missing.

Show »
Length:859
Mass (Da):94,665
Checksum:i802DB2815AB14F81
GO
Isoform G (identifier: O88943-7) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     571-571: R → RIDMIVGPPPPSTPRHKKYPTKGPTAPSRESPQYSPR

Show »
Length:888
Mass (Da):97,903
Checksum:i7B08419F3BED3C66
GO
Isoform H (identifier: O88943-8) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     373-382: Missing.
     416-416: S → SKGRPCRGCLCGCRPGHSS

Show »
Length:860
Mass (Da):94,795
Checksum:iB30DAEBF57C1CF1C
GO
Isoform I (identifier: O88943-9) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     491-491: Missing.

Show »
Length:851
Mass (Da):93,820
Checksum:i587D4BFCC45BC9A4
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei373 – 38210Missing in isoform C, isoform F and isoform H. CuratedVSP_001007
Alternative sequencei416 – 4161S → SKGRPCRGCLCGCRPGHSS in isoform D, isoform E, isoform F and isoform H. CuratedVSP_001008
Alternative sequencei417 – 42812Missing in isoform B. CuratedVSP_001009Add
BLAST
Alternative sequencei491 – 4911Missing in isoform D, isoform F and isoform I. CuratedVSP_001010
Alternative sequencei571 – 5711R → RIDMIVGPPPPSTPRHKKYP TKGPTAPSRESPQYSPR in isoform B and isoform G. CuratedVSP_001011

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF087453 mRNA. Translation: AAC36722.1.
RefSeqiNP_579856.1. NM_133322.1. [O88943-1]
UniGeneiRn.33317.

Genome annotation databases

GeneIDi170848.
KEGGirno:170848.
UCSCiRGD:621504. rat. [O88943-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF087453 mRNA. Translation: AAC36722.1.
RefSeqiNP_579856.1. NM_133322.1. [O88943-1]
UniGeneiRn.33317.

3D structure databases

ProteinModelPortaliO88943.
SMRiO88943. Positions 598-627.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi251003. 2 interactions.
IntActiO88943. 1 interaction.
MINTiMINT-8393842.
STRINGi10116.ENSRNOP00000043732.

Chemistry

BindingDBiO88943.
ChEMBLiCHEMBL5530.

PTM databases

iPTMnetiO88943.
PhosphoSiteiO88943.
SwissPalmiO88943.

Proteomic databases

PaxDbiO88943.
PRIDEiO88943.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi170848.
KEGGirno:170848.
UCSCiRGD:621504. rat. [O88943-1]

Organism-specific databases

CTDi3785.
RGDi621504. Kcnq2.

Phylogenomic databases

eggNOGiKOG1419. Eukaryota.
COG1226. LUCA.
HOGENOMiHOG000220839.
HOVERGENiHBG059014.
InParanoidiO88943.
KOiK04927.

Miscellaneous databases

PROiO88943.

Family and domain databases

InterProiIPR020969. Ankyrin-G_BS.
IPR005821. Ion_trans_dom.
IPR003937. K_chnl_volt-dep_KCNQ.
IPR003947. K_chnl_volt-dep_KCNQ2.
IPR013821. K_chnl_volt-dep_KCNQ_C.
IPR028325. VG_K_chnl.
[Graphical view]
PANTHERiPTHR11537. PTHR11537. 4 hits.
PfamiPF00520. Ion_trans. 1 hit.
PF03520. KCNQ_channel. 1 hit.
PF11956. KCNQC3-Ank-G_bd. 1 hit.
[Graphical view]
PRINTSiPR00169. KCHANNEL.
PR01461. KCNQ2CHANNEL.
PR01459. KCNQCHANNEL.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Derst C., Preisig-Mueller R., Hennighausen A., Daut J.
    Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
    Tissue: Brain.
  2. "Cloning and functional expression of rKCNQ2 K(+) channel from rat brain."
    Jow F., Wang K.-W.
    Brain Res. Mol. Brain Res. 80:269-278(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
    Tissue: Brain.
  3. "Alternative splicing of KCNQ2 potassium channel transcripts contributes to the functional diversity of M-currents."
    Pan Z., Selyanko A.A., Hadley J.K., Brown D.A., Dixon J.E., McKinnon D.
    J. Physiol. (Lond.) 531:347-358(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], ALTERNATIVE SPLICING.
    Tissue: Brain and Sympathetic ganglion.
  4. "KCNQ2 and KCNQ3 potassium channel subunits: molecular correlates of the M-channel."
    Wang H.-S., Pan Z., Shi W., Brown B.S., Wymore R.S., Cohen I.S., Dixon J.E., McKinnon D.
    Science 282:1890-1893(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  5. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-489; SER-655; SER-781 AND SER-783, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiKCNQ2_RAT
AccessioniPrimary (citable) accession number: O88943
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 2001
Last sequence update: November 1, 1998
Last modified: July 6, 2016
This is version 130 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

When coexpressed with KCNQ3 subunit in CHO cells or Xenopus oocytes, isoform B was found to have significantly different deactivation-activation kinetics. The kinetics was 2.5 times more slowly than the kinetics of other isoforms. The presence of exon 15a in isoform B accounts for the slow deactivation-activation kinetics. Alternative splicing of the KCNQ2 gene may contribute to the variation in M-current kinetics seen in vivo.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. 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.