Post Translational Modifications | KCNQ2/KCNQ3 are ubiquitinated by NEDD4L. Ubiquitination leads to protein degradation. Degradation induced by NEDD4L is inhibited by USP36. |
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. 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. |
Protein Name | Potassium Voltage-Gated Channel Subfamily Kqt Member 3Kqt-Like 3Potassium Channel Subunit Alpha Kvlqt3Voltage-Gated Potassium Channel Subunit Kv7.3 |
Cellular Localisation | Cell MembraneMulti-Pass Membrane Protein |
Alternative Antibody Names | Anti-Potassium Voltage-Gated Channel Subfamily Kqt Member 3 antibodyAnti-Kqt-Like 3 antibodyAnti-Potassium Channel Subunit Alpha Kvlqt3 antibodyAnti-Voltage-Gated Potassium Channel Subunit Kv7.3 antibodyAnti-Kcnq3 antibody |
Information sourced from Uniprot.org