Target intelligence / Profile preview

ATPase family AAA domain-containing protein 3C (ATAD3C)

Target
ATAD3C
Molecular classification
Enzyme, AAA+ (ATPases Associated with diverse cellular Activities) protein superfamily, Classic clade AAA+ ATPase (in mitochondrial membrane organization)
01

Overview

ATPase family AAA domain-containing protein 3C (ATAD3C) is a mitochondrial membrane-associated ATPase in the AAA+ superfamily, sharing homology with ATAD3A and ATAD3B. While previously considered a pseudogene product, ATAD3C is now recognized as a protein expressed in human cells, localizing to the mitochondria where it influences the structure and function of the mitochondrial inner membrane. ATAD3C modulates ATP binding and hydrolysis, affecting the assembly of mitochondrial respiratory complexes and oxidative phosphorylation, often by negatively regulating the function of ATAD3A through dominant-negative interactions. Functional disturbances in ATAD3C expression can impact mitochondrial organization, cellular proliferation, ROS production, and are associated with mitochondrial diseases and developmental syndromes. No drugs are known to directly interact with ATAD3C, and it is not currently an established therapeutic target.

Other names
ATPase family AAA domain containing 3CATAD3CFLJ34599ATPase family AAA domain-containing protein 3C
02

Biological functions

Mitochondrion organizationATP binding and hydrolysisRegulation of mitochondrial structure and respiratory chain assemblyNegative regulator of ATAD3A function in OXPHOS (oxidative phosphorylation) complex organizationIntegral membrane protein of the mitochondria
03

Disease associations

Mitochondrial disordersChromosome 1p36.33 duplication syndromeHarel-Yoon syndromeDiseases associated with dysregulation of mitochondrial dynamics or OXPHOS
04

Safety considerations

Potential pleiotropic effects due to disruption of mitochondrial function if modulated unnaturallyImpact on mitochondrial respiration, cellular proliferation, and oxidative stress if ATAD3C function is altered (as shown by overexpression studies)

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