Search Results
Overview
| Uniprot ID | Q9CQ62 |
|---|---|
| Protein Name | 2,4-dienoyl-CoA reductase [(3E)-enoyl-CoA-producing], mitochondrial |
| Gene Name | Decr1 |
| Organism | Mus musculus |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 106 | TAEEISSKTGNKVHA |
| 110 | ISSKTGNKVHAIRCD |
| 185 | EIGKQLIKAQKGAAF |
| 244 | IIQPGPIKTKGAFSR |
| 260 | DPTGRFEKEMIDRIP |
| 42 | SKDAPQSKFFQPVLK |
| 97 | SRNIDVLKATAEEIS |
Function
Auxiliary enzyme in the beta-oxidation of mono- and polyunsaturated fatty acids. Together with the Enoyl-CoA delta isomerase 1 (ECI1) and the Delta(3,5)-Delta(2,4)-dienoyl-CoA isomerase (ECH1) they allow reentrance of the enoyl-CoA into the beta-oxidation cycle. It participates in the metabolism of unsaturated fatty enoyl-CoA esters having double bonds in both even- and odd-numbered positions in mitochondria. Acts primarily on polyunsaturated fatty acids. Catalyzes the NADP-dependent reduction of 2,4-dienoyl-CoA to yield trans-3-enoyl-CoA. Based on its established catalytic mechanism, it is predicted to act also on other fatty acids besides those tested experimentally
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:1902494 | catalytic complex |
| Cellular Component | GO:0005829 | cytosol |
| Cellular Component | GO:0005739 | mitochondrion |
| Cellular Component | GO:0005654 | nucleoplasm |
| Molecular Function | GO:0008670 | 2,4-dienoyl-CoA reductase (NADPH) activity |
| Molecular Function | GO:0042802 | identical protein binding |
| Molecular Function | GO:0070402 | NADPH binding |
| Biological Process | GO:0006635 | fatty acid beta-oxidation |
| Biological Process | GO:0120162 | positive regulation of cold-induced thermogenesis |
Reference
[1] Chang J, Wu W, Qian P, Lu Z, He X et al.. Multi-omics study on the effect of moderate-intensity exercise on protein lactylation in mouse muscle tissue.. Front Cell Dev Biol 12:1472338. 2024. PMID: 39935788.
[2] 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.
[3] 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.