Search Results
Overview
| Uniprot ID | Q9DCS3 |
|---|---|
| Protein Name | Enoyl-[acyl-carrier-protein] reductase, mitochondrial |
| Gene Name | Mecr |
| Organism | Mus musculus |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 222 | VRDRPDIKKLTDRLK |
| 248 | ELRMPETKTIFKDLP |
| 252 | PETKTIFKDLPLPRL |
| 267 | ALNCVGGKSSTELLR |
| 56 | GNHGDPAKVVQLKNL |
Function
Catalyzes the NADPH-dependent reduction of trans-2-enoyl thioesters in mitochondrial fatty acid synthesis (fatty acid synthesis type II). Fatty acid chain elongation in mitochondria uses acyl carrier protein (ACP) as an acyl group carrier, but the enzyme accepts both ACP and CoA thioesters as substrates in vitro. Displays a preference for medium-chain over short- and long-chain substrates (By similarity). May provide the octanoyl chain used for lipoic acid biosynthesis, regulating protein lipoylation and mitochondrial respiratory activity particularly in Purkinje cells (PubMed:30266742). Involved in iron homeostasis; affecting Fe-S cluster assembly and ceramide metabolism (By similarity). Required for proper morphology and bioenergetic functions of mitochondria (By similarity). Required for maintenance of neurons (By similarity)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Biological Process | GO:0006879 | intracellular iron ion homeostasis |
| Cellular Component | GO:0005829 | cytosol |
| Cellular Component | GO:0016020 | membrane |
| Cellular Component | GO:0005739 | mitochondrion |
| Cellular Component | GO:0005634 | nucleus |
| Molecular Function | GO:0141148 | enoyl-[acyl-carrier-protein] reductase (NADPH) activity |
| Molecular Function | GO:0016922 | nuclear receptor binding |
| Molecular Function | GO:0005102 | signaling receptor binding |
| Biological Process | GO:0046513 | ceramide biosynthetic process |
| Biological Process | GO:0006633 | fatty acid biosynthetic process |
| Biological Process | GO:0006631 | fatty acid metabolic process |
Reference
[1] Zhuo W, Zhang M, Tan J, Gao Y, Wang Y et al.. Lysine lactylation analysis of proteins in the heart of the Kawasaki disease mouse model.. Front Cell Dev Biol 13:1550220. 2025. PMID: 40114965.
[2] Wu D, Tang Y, Li X, Xiong S, Zhang Z et al.. Characterization of protein lactylation in healthy and ischemic mouse hearts.. Front Cardiovasc Med 12:1644886. 2025. PMID: 41089239.