UNC79

Chr 14q32.12

unc-79 subunit of NALCN channel complex

MANE:: ENST00000695012.1

OMIM: 616884 ↗NCBI: 57578 ↗Ensembl ↗

Annotations refreshed 1 month ago.

Predicted protein structure

AlphaFold predicted structure

UNC79 · Q9P2D8

v62025-08-01

Predicted Aligned Error matrix for UNC79 — diagonal shows residue index, colour shows pairwise prediction confidence (lower is better) — Predicted Aligned Error

Mean pLDDT

63.5/ 100

Low

2,635 residues

Confidence breakdown

Very high(≥ 90)4%
Confident(70–90)53%
Low(50–70)11%
Very low(< 50)33%

Open interactive 3D viewer

AlphaFold (Jumper et al., 2021) · CC BY 4.0

Clinical relevance (Genomics England PanelApp)

Moderate Evidence (Amber)

Early onset or syndromic epilepsy
MONOALLELIC, autosomal or pseudoautosomal, NOT imprinted
Intellectual disability
MONOALLELIC, autosomal or pseudoautosomal, NOT imprinted
DDG2P
MONOALLELIC, autosomal or pseudoautosomal, imprinted status unknown

Disease associations (Open Targets)

hereditary disease
0.51
neurodevelopmental disorder
0.44
mathematical ability
0.43
Abnormality of the skeletal system
0.40
smoking initiation
0.33
asthma
0.30
gallbladder disorder
0.26
head injury
0.25
preeclampsia
0.24
neurodegenerative disease
0.22

Score is the Open Targets composite evidence score (0-1). Higher = stronger gene-disease association.

Protein function (UniProt)

Protein unc-79 homolog

Auxilary subunit of the NALCN channelosome complex, which regulates the resting membrane potential by depolarizing sodium leak currents (PubMed:32494638, PubMed:35387979, PubMed:34929720). The NALCN channelosome complex is a voltage-gated ion channel responsible for the resting Na(+) permeability that controls neuronal excitability (PubMed:35387979, PubMed:34929720). The NALCN channelosome is constitutively active and conducts monovalent cations but is blocked by physiological concentrations of extracellular divalent cations (PubMed:32494638). Activated by neuropeptides substance P, neurotensin, and extracellular Ca(2+) that regulates neuronal excitability by controlling the sizes of NALCN-dependent sodium-leak current (By similarity)