Kcnq2
entrez
170848
canonical
uniprot
O88943
canonical
ensembl
ENSRNOG00000011624
resolver
ensp
ENSRNOP00000040830
resolver
ensp
ENSRNOP00000083195
resolver
ensp
ENSRNOP00000094215
resolver
enst
ENSRNOT00000102525
resolver
genesymbol
Kcnq2
resolver
genesymbol_syn
Eef1a1l1
resolver
uniprot
A0A8I5ZWG8
resolver
uniprot_entry
A0A8I5ZWG8_RAT
resolver
uniprot_entry
KCNQ2_RAT
resolver
activity_regulation
ACTIVITY REGULATION: Phosphatidylinositol-4,5-bisphosphate (PIP2) potentiates the activation of KCNQ channels by enhancing the electro-mechanical coupling of the voltage-sensing domain (VSD) and the pore-forming domain (PD). In the closed state of the channel, PIP2 is anchored at the S2-S3 loop; upon channel activation, PIP2 interacts with the S4-S5 linker and is involved in channel gating (By similarity). Calcium suppresses KCNQ2 and KCNQ2-KCNQ3 channel currents, with calcium-bound calmodulin inducing a change in channel configuration which leads to the reduction of channel affinity for PIP2 and subsequent current suppression (PubMed:24349250). {ECO:0000250|UniProtKB:O43526, ECO:0000269|PubMed:24349250}.
uniprot
proteins
amino_acid_sequence
MVQKSRNGGVYPGTSGEKKLKVGFVGLDPGAPDSTRDGALLIAGSEAPKRGSVLSKPRTGGAGAGKPPKRNAFYRKLQNFLYNVLERPRGWAFIYHAYVFLLVFSCLVLSVFSTIKEYEKSSEGALYILEIVTIVVFGVEYFVRIWAAGCCCRYRGWRGRLKFARKPFCVIDIMVLIASIAVLAAGSQGNVFATSALRSLRFLQILRMIRMDRRGGTWKLLGSVVYAHSKELVTAWYIGFLCLILASFLVYLAEKGENDHFDTYADALWWGLITLTTIGYGDKYPQTWNGRLLAATFTLIGVSFFALPAGILGSGFALKVQEQHRQKHFEKRRNPAAGLIQSAWRFYATNLSRTDLHSTWQYYERTVTVPMISSQTQTYGASRLIPPLNQLEMLRNLKSKSGLTFRKEPQPEPSPSQKVSLKDRVFSSPRGVAAKGKGSPQAQTVRRSPSADQSLDDSPSKVPKSWSFGDRSRARQAFRIKGAASRQNSEEASLPGEDIVEDNKSCNCEFVTEDLTPGLKVSIRAVCVMRFLVSKRKFKESLRPYDVMDVIEQYSAGHLDMLSRIKSLQSRVDQIVGRGPTITDKDRTKGPAETELPEDPSMMGRLGKVEKQVLSMEKKLDFLVSIYTQRMGIPPAETEAYFGAKEPEPAPPYHSPEDSRDHADKHGCIIKIVRSTSSTGQRKYAAPPVMPPAECPPSTSWQQSHQRHGTSPVGDHGSLVRIPPPPAHERSLSAYSGGNRASTEFLRLEGTPACRPSEAALRDSDTSISIPSVDHEELERSFSGFSISQSKENLNALASCYAAVAPCAKVRPYIAEGESDTDSDLCTPCGPPPRSATGEGPFGDVAWAGPRK
uniprot
proteins
function
FUNCTION: Pore-forming subunit of the voltage-gated potassium (Kv) M-channel which is responsible for the M-current, a key controller of neuronal excitability (PubMed:11038262, PubMed:11230508, PubMed:24349250). M-channel is composed of pore-forming subunits KCNQ2 and KCNQ3 assembled as heterotetramers (By similarity). The native M-current has 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 (PubMed:11230508). M-channel is selectively permeable in vitro to other cations besides potassium, in decreasing order of affinity K(+) > Rb(+) > Cs(+) > Na(+) (By similarity). M-channel association with SLC5A3/SMIT1 alters channel ion selectivity, increasing Na(+) and Cs(+) permeation relative to K(+) (PubMed:28793216). Suppressed by activation of the muscarinic acetylcholine receptor CHRM1 (PubMed:11230508). {ECO:0000250|UniProtKB:O43526, ECO:0000269|PubMed:11038262, ECO:0000269|PubMed:11230508, ECO:0000269|PubMed:24349250, ECO:0000269|PubMed:28793216}.
uniprot
proteins
mass_dalton
93949
uniprot
proteins
mutagenesis
MUTAGEN 353; /note="R->G: Increased suppression of current in the presence of Ca(2+)."; /evidence="ECO:0000269|PubMed:24349250"; MUTAGEN 527; /note="C->R: No loss of calmodulin binding in the presence of Ca(2+) compared to WT. No difference with WT in current suppression in the presence of Ca(2+)."; /evidence="ECO:0000269|PubMed:24349250
uniprot
proteins
post_translational_modification
PTM: KCNQ2/KCNQ3 heteromeric current can be increased by intracellular cyclic AMP, an effect that depends on phosphorylation of Ser-52 in the N-terminal region. {ECO:0000250|UniProtKB:O43526}.; PTM: KCNQ2/KCNQ3 are ubiquitinated by NEDD4L. Ubiquitination leads to protein degradation. Degradation induced by NEDD4L is inhibited by USP36. {ECO:0000250|UniProtKB:O43526}.
uniprot
proteins
protein_family
KQT (TC 1.A.1.15) subfamily
uniprot
proteins
protein_family
Kv7.2/KCNQ2 sub-subfamily
uniprot
proteins
protein_family
Potassium channel family
uniprot
proteins
pubmed
11038262
uniprot
proteins
pubmed
11230508
uniprot
proteins
pubmed
22673903
uniprot
proteins
pubmed
24349250
uniprot
proteins
pubmed
28793216
uniprot
proteins
pubmed
9836639
uniprot
proteins
sequence_length
852
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11038262, ECO:0000269|PubMed:11230508}; Multi-pass membrane protein {ECO:0000255}.
uniprot
proteins
transmembrane_region
TRANSMEM 91..113; /note="Helical; Name=Segment S1"; /evidence="ECO:0000250|UniProtKB:O43526"; TRANSMEM 124..145; /note="Helical; Name=Segment S2"; /evidence="ECO:0000250|UniProtKB:O43526"; TRANSMEM 164..183; /note="Helical; Name=Segment S3"; /evidence="ECO:0000250|UniProtKB:O43526"; TRANSMEM 197..215; /note="Helical; Voltage-sensor; Name=Segment S4"; /evidence="ECO:0000250|UniProtKB:O43526"; TRANSMEM 228..253; /note="Helical; Name=Segment S5"; /evidence="ECO:0000250|UniProtKB:O43526"; TRANSMEM 288..314; /note="Helical; Name=Segment S6"; /evidence="ECO:0000250|UniProtKB:O43526
uniprot
proteins