Search Results
Overview
| Uniprot ID | Q8N4T8 |
|---|---|
| Protein Name | 3-oxoacyl-[acyl-carrier-protein] reductase |
| Gene Name | CBR4 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 164 | GFSRALAKEVARKKI |
| 190 | TDMTKDLKEEHLKKN |
| 195 | DLKEEHLKKNIPLGR |
| 196 | LKEEHLKKNIPLGRF |
| 59 | AFSCDVAKEHDVQNT |
Function
Component of the heterotetramer complex KAR (3-ketoacyl-[acyl carrier protein] reductase or 3-ketoacyl-[ACP] reductase) that forms part of the mitochondrial fatty acid synthase (mtFAS). Beta-subunit of the KAR heterotetramer complex, responsible for the 3-ketoacyl-ACP reductase activity of the mtFAS, reduces 3-oxoacyl-[ACP] to (3R)-hydroxyacyl-[ACP] in a NADPH-dependent manner with no chain length preference, thereby participating in mitochondrial fatty acid biosynthesis (PubMed:25203508). The homotetramer has NADPH-dependent quinone reductase activity (in vitro), hence could play a role in protection against cytotoxicity of exogenous quinones (PubMed:19000905). As a heterotetramer, it can also reduce 9,10-phenanthrenequinone, 1,4-benzoquinone and various other o-quinones and p-quinones (in vitro) (PubMed:19000905, PubMed:19571038, PubMed:25203508)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0005759 | mitochondrial matrix |
| Biological Process | GO:0051289 | protein homotetramerization |
| Cellular Component | GO:0005739 | mitochondrion |
| Cellular Component | GO:1990204 | oxidoreductase complex |
| Molecular Function | GO:0004316 | 3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity |
| Molecular Function | GO:0003955 | NAD(P)H dehydrogenase (quinone) activity |
| Molecular Function | GO:0070402 | NADPH binding |
| Molecular Function | GO:0008753 | NADPH dehydrogenase (quinone) activity |
| Molecular Function | GO:0016616 | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| Molecular Function | GO:0048038 | quinone binding |
| Biological Process | GO:0044597 | daunorubicin metabolic process |
| Biological Process | GO:0044598 | doxorubicin metabolic process |
| Biological Process | GO:0006633 | fatty acid biosynthetic process |
| Biological Process | GO:0046949 | fatty-acyl-CoA biosynthetic process |
| Biological Process | GO:0051290 | protein heterotetramerization |
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.