O43525: Potassium voltage-gated channel subfamily KQT member 3 (KCNQ3)

Potassium voltage-gated channel subfamily KQT member 3 (KCNQ3) is a 872-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: O43525.

Gene
KCNQ3
Organism
Homo sapiens
Length
872 residues
Mean pLDDT
56.7
Model
AF-O43525-F1 v6
Model created
1 Aug 2025
PDB structures
1

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Model confidence (pLDDT)

The mean pLDDT of this model is 56.7 (low overall). pLDDT is AlphaFold's per-residue confidence score from 0 to 100. In MolViewer, choose the B-factor color scheme to color the model by pLDDT, because AlphaFold stores it in the B-factor column.

pLDDT bandMeaningShare of residues
Above 90Very high: backbone and side chains are usually accurate15%
70 to 90Confident: backbone generally right22%
50 to 70Low: treat with caution10%
Below 50Very low: often disordered regions53%

What pLDDT means and how to read it

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…

Subunit structure

Heterotetramer with KCNQ2; forms heterotetrameric native M-channel responsible for the M-current (PubMed:27564677). Interacts with calmodulin; the interaction is calcium-independent, constitutive and participates in the proper assembly of a functional M-channel (PubMed:27564677). Heteromultimer with KCNQ5 (PubMed:11159685). May associate with KCNE2 (PubMed:11034315). Interacts with IQCJ-SCHIP1…

Subcellular location

Cell membrane

Disease associations

Experimental structures in the PDB

Compare the prediction with experimentally determined structures of the same protein:

PDB IDMethodResolutionChains and residues
5J03X-ray2.0 ÅA=354-409

More AlphaFold highlights

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