Search Results
Overview
| Uniprot ID | Q16698 |
|---|---|
| Protein Name | 2,4-dienoyl-CoA reductase [(3E)-enoyl-CoA-producing], mitochondrial |
| Gene Name | DECR1 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 110 | ISSQTGNKVHAIQCD |
| 185 | EIGKQLIKAQKGAAF |
| 222 | AGVEAMSKSLAAEWG |
| 230 | SLAAEWGKYGMRFNV |
| 244 | VIQPGPIKTKGAFSR |
| 246 | QPGPIKTKGAFSRLD |
| 260 | DPTGTFEKEMIGRIP |
| 319 | NDLRKVTKEQWDTIE |
| 49 | KFFSPLQKAMLPPNS |
| 73 | GGGTGLGKGMTTLLS |
| 97 | SRKMDVLKATAEQIS |
Function
Auxiliary enzyme in the beta-oxidation of mono- and polyunsaturated fatty acids (Probable) (PubMed:15531764, PubMed:26474213). 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 (PubMed:26474213). It participates in the metabolism of unsaturated fatty enoyl-CoA esters having double bonds in both even- and odd-numbered positions in mitochondria (PubMed:15531764). Acts primarily on polyunsaturated fatty acids (Probable). Catalyzes the NADP-dependent reduction of 2,4-dienoyl-CoA to yield trans-3-enoyl-CoA (PubMed:15531764). Based on its established catalytic mechanism, it is predicted to act also on other fatty acids besides those tested experimentally (Probable)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:1902494 | catalytic complex |
| Cellular Component | GO:0005759 | mitochondrial matrix |
| Cellular Component | GO:0005739 | mitochondrion |
| Cellular Component | GO:0005634 | nucleus |
| 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] Yang Z, Yan C, Ma J, Peng P, Ren X et al.. Lactylome analysis suggests lactylation-dependent mechanisms of metabolic adaptation in hepatocellular carcinoma.. Nat Metab 5(1):61-79. 2023 Jan. PMID: 36593272.
[2] Hong H, Chen X, Wang H, Gu X, Yuan Y et al.. Global profiling of protein lysine lactylation and potential target modified protein analysis in hepatocellular carcinoma.. Proteomics 23(9):e2200432. 2023 May. PMID: 36625413.
[3] Shi CM, Wang QC, Li XL, Yang YH, Tang XY et al.. Global Profiling of Protein Lactylation in Human Hippocampi.. Proteomics Clin Appl 19(2):e202400061. 2025 Mar. PMID: 39610256.
[4] Yan M, Tu H, Tang S, Gai Z, Shi Q et al.. Lactylated Proteomic Analysis Reveals Functional Implications of Lysine Lactylation In Asthenozoospermia.. Mol Cell Proteomics 24(12):101439. 2025 Dec. PMID: 41192556.