KCNQ3
entrez
3786
canonical
uniprot
O43525
canonical
ensembl
ENSG00000184156
resolver
ensp
ENSP00000373648
resolver
ensp
ENSP00000428790
resolver
ensp
ENSP00000429799
resolver
ensp
ENSP00000491940
resolver
enst
ENST00000519445
resolver
genesymbol
KCNQ3
resolver
hgnc
HGNC:6297
resolver
uniprot
A2VCT8
resolver
uniprot
B4DJY4
resolver
uniprot
E7EQ89
resolver
uniprot
E7ET42
resolver
uniprot_entry
E7ET42_HUMAN
resolver
uniprot_entry
KCNQ3_HUMAN
resolver
uniprot_sec
A2VCT8
resolver
uniprot_sec
B4DJY4
resolver
uniprot_sec
E7EQ89
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) (By similarity). 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). M-channel is activated by the anticonvulsant retigabine (PubMed:10713399, PubMed:10908292, PubMed:10953053, PubMed:11159685). {ECO:0000250|UniProtKB:O43526, ECO:0000250|UniProtKB:O88944, ECO:0000269|PubMed:10713399, ECO:0000269|PubMed:10908292, ECO:0000269|PubMed:10953053, ECO:0000269|PubMed:11159685}.
uniprot
proteins
amino_acid_sequence
MGLKARRAAGAAGGGGDGGGGGGGAANPAGGDAAAAGDEERKVGLAPGDVEQVTLALGAGADKDGTLLLEGGGRDEGQRRTPQGIGLLAKTPLSRPVKRNNAKYRRIQTLIYDALERPRGWALLYHALVFLIVLGCLILAVLTTFKEYETVSGDWLLLLETFAIFIFGAEFALRIWAAGCCCRYKGWRGRLKFARKPLCMLDIFVLIASVPVVAVGNQGNVLATSLRSLRFLQILRMLRMDRRGGTWKLLGSAICAHSKELITAWYIGFLTLILSSFLVYLVEKDVPEVDAQGEEMKEEFETYADALWWGLITLATIGYGDKTPKTWEGRLIAATFSLIGVSFFALPAGILGSGLALKVQEQHRQKHFEKRRKPAAELIQAAWRYYATNPNRIDLVATWRFYESVVSFPFFRKEQLEAASSQKLGLLDRVRLSNPRGSNTKGKLFTPLNVDAIEESPSKEPKPVGLNNKERFRTAFRMKAYAFWQSSEDAGTGDPMAEDRGYGNDFPIEDMIPTLKAAIRAVRILQFRLYKKKFKETLRPYDVKDVIEQYSAGHLDMLSRIKYLQTRIDMIFTPGPPSTPKHKKSQKGSAFTFPSQQSPRNEPYVARPSTSEIEDQSMMGKFVKVERQVQDMGKKLDFLVDMHMQHMERLQVQVTEYYPTKGTSSPAEAEKKEDNRYSDLKTIICNYSETGPPEPPYSFHQVTIDKVSPYGFFAHDPVNLPRGGPSSGKVQATPPSSATTYVERPTVLPILTLLDSRVSCHSQADLQGPYSDRISPRQRRSITRDSDTPLSLMSVNHEELERSPSGFSISQDRDDYVFGPNGGSSWMREKRYLAEGETDTDTDPFTPSGSMPLSSTGDGISDSVWTPSNKPI
uniprot
proteins
disease_involvement
DISEASE: Seizures, benign familial neonatal 2 (BFNS2) [MIM:121201]: A disorder characterized by clusters of seizures occurring in the first days of life. Most patients have spontaneous remission by 12 months of age and show normal psychomotor development. The disorder is distinguished from benign familial infantile seizures by an earlier age at onset. {ECO:0000269|PubMed:10852552, ECO:0000269|PubMed:14534157, ECO:0000269|PubMed:25982755, ECO:0000269|PubMed:9425900, ECO:0000269|PubMed:9872318}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Note=Defects in KCNQ3 may be involved in epileptic disorders. These are characterized by paroxysmal transient disturbances of the electrical activity of the brain that may be manifested as episodic impairment or loss of consciousness, abnormal motor phenomena, psychic or sensory disturbances, or perturbation of the autonomic nervous system. {ECO:0000269|PubMed:22612257}.
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:16319223, PubMed:27564677, PubMed:28793216, PubMed:9872318). M-channel is composed of pore-forming subunits KCNQ2 and KCNQ3 assembled as heterotetramers (PubMed:14534157, PubMed:16319223, PubMed:27564677, PubMed:9872318). 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:14534157, PubMed:16319223, PubMed:28793216). M-channel is selectively permeable in vitro to other cations besides potassium, in decreasing order of affinity K(+) > Rb(+) > Cs(+) > Na(+) (PubMed:28793216). M-channel association with SLC5A3/SMIT1 alters channel ion selectivity, increasing Na(+) and Cs(+) permeation relative to K(+) (PubMed:28793216). Suppressed by activation of M1 muscarinic acetylcholine receptors (PubMed:10713961). KCNQ3 also associates with KCNQ5 to form a functional channel in vitro and may also contribute to the M-current in brain (PubMed:11159685). {ECO:0000250|UniProtKB:O43526, ECO:0000269|PubMed:10713961, ECO:0000269|PubMed:11159685, ECO:0000269|PubMed:14534157, ECO:0000269|PubMed:16319223, ECO:0000269|PubMed:27564677, ECO:0000269|PubMed:28793216, ECO:0000269|PubMed:9872318}.
uniprot
proteins
mass_dalton
96742
uniprot
proteins
mutagenesis
MUTAGEN 246; /note="T->A: No effect on current or expression."; /evidence="ECO:0000269|PubMed:16319223"; MUTAGEN 246; /note="T->D: Abolishes currents without reducing channel protein expression."; /evidence="ECO:0000269|PubMed:16319223"; MUTAGEN 318; /note="G->S: >50% Reduction of wt heteromeric current; ratio of 1:1 and 1:1:2."; /evidence="ECO:0000269|PubMed:9872318
uniprot
proteins
post_translational_modification
PTM: KCNQ2/KCNQ3 are ubiquitinated by NEDD4L. Ubiquitination leads to protein degradation (Probable). Degradation induced by NEDD4L is inhibited by USP36 (PubMed:27445338). {ECO:0000269|PubMed:27445338, ECO:0000305|PubMed:27445338}.
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
10479678
uniprot
proteins
pubmed
10713399
uniprot
proteins
pubmed
10713961
uniprot
proteins
pubmed
10788442
uniprot
proteins
pubmed
10852552
uniprot
proteins
pubmed
10908292
uniprot
proteins
pubmed
10953053
uniprot
proteins
pubmed
11034315
uniprot
proteins
pubmed
11159685
uniprot
proteins
pubmed
14534157
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16319223
uniprot
proteins
pubmed
16421571
uniprot
proteins
pubmed
22612257
uniprot
proteins
pubmed
23360469
uniprot
proteins
pubmed
25982755
uniprot
proteins
pubmed
27445338
uniprot
proteins
pubmed
27564677
uniprot
proteins
pubmed
28793216
uniprot
proteins
pubmed
9425900
uniprot
proteins
pubmed
9677360
uniprot
proteins
pubmed
9872318
uniprot
proteins
sequence_length
872
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10788442}; Multi-pass membrane protein {ECO:0000255}.
uniprot
proteins
transmembrane_region
TRANSMEM 121..143; /note="Helical; Name=Segment S1"; /evidence="ECO:0000250|UniProtKB:O43526"; TRANSMEM 154..175; /note="Helical; Name=Segment S2"; /evidence="ECO:0000250|UniProtKB:O43526"; TRANSMEM 194..213; /note="Helical; Name=Segment S3"; /evidence="ECO:0000250|UniProtKB:O43526"; TRANSMEM 226..244; /note="Helical; Voltage-sensor; Name=Segment S4"; /evidence="ECO:0000250|UniProtKB:O43526"; TRANSMEM 257..282; /note="Helical; Name=Segment S5"; /evidence="ECO:0000250|UniProtKB:O43526"; TRANSMEM 327..353; /note="Helical; Name=Segment S6"; /evidence="ECO:0000250|UniProtKB:O43526
uniprot
proteins