Kcnq3
entrez
110862
canonical
uniprot
Q8K3F6
canonical
ensembl
ENSMUSG00000056258
resolver
ensp
ENSMUSP00000063380
resolver
enst
ENSMUST00000070256
resolver
genesymbol
Kcnq3
resolver
uniprot
E9QJY5
resolver
uniprot_entry
KCNQ3_MOUSE
resolver
uniprot_sec
E9QJY5
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-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 (By similarity). {ECO:0000250|UniProtKB:O43526, ECO:0000250|UniProtKB:O88944}.
uniprot
proteins
amino_acid_sequence
MGLKARRAAGAAGGGGGEGGGGGGGAANPAGGDSAVAGDEERKVGLAPGDVEQVTLALGAGADKDGTLLLEGGGREEGQRRTPQGIGLLAKTPLSRPVKRNNAKYRRIQTLIYDALERPRGWALLYHALVFLIVLGCLILAVLTTFKEYETVSGDWLLLLETFAIFIFGAEFALRIWAAGCCCRYKGWRGRLKFARKPLCMLDIFVLIASVPVVAVGNQGNVLATSLRSLRFLQILRMLRMDRRGGTWKLLGSAICAHSKELITAWYIGFLTLILSSFLVYLVEKDVPEMDAQGEEMKEEFETYADALWWGLITLATIGYGDKTPKTWEGRLIAATFSLIGVSFFALPAGILGSGLALKVQEQHRQKHFEKRRKPAAELIQAAWRYYATNPNRLDLVATWRFYESVVSFPFFRKEQLEAAASQKLGLLDRVRLSNPRGSNTKGKLFTPLNVDAIEESPSKEPKPVGLNNKERFRTAFRMKAYAFWQSSEDAGTGDPMAEDRGYGNDFLIEDMIPTLKAAIRAVRILQFRLYKKKFKETLRPYDVKDVIEQYSAGHLDMLSRIKYLQTRIDMIFTPGPPSTPKHKKSQKGSAFTYPSQQSPRNEPYVARAATSETEDQSMMGKFVKVERQVHDMGKKLDFLVDMHMQHMERLQVHVTEYYPTKGASSPAEGEKKEDNRYSDLKTIICNYSETGPPDPPYSFHQVPIDRVGPYGFFAHDPVKLTRGGPSSTKAQANLPSSGSTYAERPTVLPILTLLDSCVSYHSQTELQGPYSDHISPRQRRSITRDSDTPLSLMSVNHEELERSPSGFSISQDRDDYVFGPSGGSSWMREKRYLAEGETDTDTDPFTPSGSMPMSSTGDGISDSIWTPSNKPT
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. 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. M-channel is selectively permeable in vitro to other cations besides potassium, in decreasing order of affinity K(+) > Rb(+) > Cs(+) > Na(+). M-channel association with SLC5A3/SMIT1 alters channel ion selectivity, increasing Na(+) and Cs(+) permeation relative to K(+). Suppressed by activation of M1 muscarinic acetylcholine receptors. KCNQ3 also associates with KCNQ5 to form a functional channel in vitro and may also contribute to the M-current in brain (By similarity). {ECO:0000250|UniProtKB:O43525, ECO:0000250|UniProtKB:O43526}.
uniprot
proteins
mass_dalton
96852
uniprot
proteins
post_translational_modification
PTM: KCNQ2/KCNQ3 are ubiquitinated by NEDD4L. Ubiquitination leads to protein degradation. Degradation induced by NEDD4L is inhibited by USP36. {ECO:0000250|UniProtKB:O43525}.
uniprot
proteins
protein_family
KQT (TC 1.A.1.15) subfamily
uniprot
proteins
protein_family
Kv7.3/KCNQ3 sub-subfamily
uniprot
proteins
protein_family
Potassium channel family
uniprot
proteins
pubmed
17114649
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
27979964
uniprot
proteins
pubmed
38440182
uniprot
proteins
sequence_length
873
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O43525}; Multi-pass membrane protein {ECO:0000255}.
uniprot
proteins
transmembrane_region
TRANSMEM 122..144; /note="Helical; Name=Segment S1"; /evidence="ECO:0000250|UniProtKB:O43526"; TRANSMEM 155..176; /note="Helical; Name=Segment S2"; /evidence="ECO:0000250|UniProtKB:O43526"; TRANSMEM 195..214; /note="Helical; Name=Segment S3"; /evidence="ECO:0000250|UniProtKB:O43526"; TRANSMEM 227..245; /note="Helical; Voltage-sensor; Name=Segment S4"; /evidence="ECO:0000250|UniProtKB:O43526"; TRANSMEM 258..283; /note="Helical; Name=Segment S5"; /evidence="ECO:0000250|UniProtKB:O43526"; TRANSMEM 328..354; /note="Helical; Name=Segment S6"; /evidence="ECO:0000250|UniProtKB:O43526
uniprot
proteins