protein
Acyl-CoA synthetase short-chain family member 3, mitochondrial
Gene
ACSS3
Organism
Homo sapiens(9606)
Length
686 aa
Mass
74,778 Da
ACSS3 (acyl-CoA synthetase short-chain family member 3, mitochondrial) is a mitochondrial enzyme that catalyzes the conversion of short-chain fatty acids to acetyl-CoA, with propionate as the preferred substrate and lower-affinity activity toward acetate and butyrate (UniProt: Q9H6R3). This enzymatic function positions the protein within lipid metabolism and acetyl-CoA generation pathways, critical for mitochondrial energy production and biosynthetic processes.
ACSS3 has been detected in human post-mortem brain tissue and localized to mitochondrial subcellular fractions. No disease associations are listed in UniProt; however, the protein is tagged as relevant to Alzheimer's Disease in the Chaparral Knowledge Platform.
In Alzheimer's Disease brain tissue, ACSS3 is significantly upregulated compared to age-matched controls (mean log2FC = 0.59; Chaparral AD proteomics). This elevation across multiple subcellular fractions of human post-mortem AD brain suggests altered lipid and energy metabolism in the disease state, potentially reflecting compensatory or pathological shifts in mitochondrial acetyl-CoA production.
Generated from the curated entity record below. May contain errors — verify against source links.
Proteomics Evidence · AD
↑ Up in ADP3
+0.633
P2
+0.851
S2
+0.273
S3
not detected
Mean log₂FC across detected fractions: +0.5857 (3 of 4 fractions detected)
Human post-mortem AD brain vs age-matched controls, TMT-labeled, 4 subcellular fractions (P2, P3, S2, S3), DDA proteomics.
Related Publications
Browse all →Tau molecular diversity contributes to clinical heterogeneity in Alzheimer's disease.
Dujardin Simon et al.Nature medicine2020PMID 32572268Deep Multilayer Brain Proteomics Identifies Molecular Networks in Alzheimer's Disease Progression.
Bai Bing et al.Neuron2020PMID 31926610A Multi-network Approach Identifies Protein-Specific Co-expression in Asymptomatic and Symptomatic Alzheimer's Disease.
Seyfried Nicholas T et al.Cell systems2017PMID 27989508Large-scale deep multi-layer analysis of Alzheimer's disease brain reveals strong proteomic disease-related changes not observed at the RNA level.
Johnson Erik C B et al.Nature neuroscience2022PMID 35115731Organization and regulation of gene transcription.
Cramer PatrickNature2019PMID 31462772
Function
Catalyzes the synthesis of acetyl-CoA from short-chain fatty acids (PubMed:28003429). Propionate is the preferred substrate (PubMed:28003429). Can utilize acetate and butyrate with a much lower affinity (By similarity)
Sources
Last updated 5/8/2026, 6:37:32 AM
