Search Results
Overview
| Uniprot ID | Q14914 |
|---|---|
| Protein Name | Prostaglandin reductase 1 |
| Gene Name | PTGR1 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 100 | THSISDGKDLEKLLT |
| 11 | TKTWTLKKHFVGYPT |
| 168 | IAKLKGCKVVGAVGS |
| 178 | GAVGSDEKVAYLQKL |
| 204 | ESLEETLKKASPDGY |
| 324 | LKGDNLGKTIVKA** |
| 5 | ***MVRTKTWTLKKH |
| 58 | RVAAKRLKEGDTMMG |
| 70 | MMGQQVAKVVESKNV |
| 75 | VAKVVESKNVALPKG |
Function
NAD(P)H-dependent oxidoreductase involved in metabolic inactivation of pro- and anti-inflammatory eicosanoids: prostaglandins (PG), leukotrienes (LT) and lipoxins (LX) (PubMed:25619643). Catalyzes with high efficiency the reduction of the 13,14 double bond of 15-oxoPGs, including 15-oxo-PGE1, 15-oxo-PGE2, 15-oxo-PGF1-alpha and 15-oxo-PGF2-alpha (PubMed:25619643). Catalyzes with lower efficiency the oxidation of the hydroxyl group at C12 of LTB4 and its derivatives, converting them into biologically less active 12-oxo-LTB4 metabolites (By similarity) (PubMed:25619643). Reduces 15-oxo-LXA4 to 13,14 dihydro-15-oxo-LXA4, enhancing neutrophil recruitment at the inflammatory site (By similarity). May play a role in metabolic detoxification of alkenals and ketones. Reduces alpha,beta-unsaturated alkenals and ketones, particularly those with medium-chain length, showing highest affinity toward (2E)-decenal and (3E)-3-nonen-2-one (PubMed:25619643). May inactivate 4-hydroxy-2-nonenal, a cytotoxic lipid constituent of oxidized low-density lipoprotein particles (By similarity)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0005737 | cytoplasm |
| Cellular Component | GO:0070062 | extracellular exosome |
| Molecular Function | GO:0036185 | 13-lipoxin reductase activity |
| Molecular Function | GO:0047522 | 15-oxoprostaglandin 13-reductase [NAD(P)+] activity |
| Molecular Function | GO:0035798 | 2-alkenal reductase (NADPH) activity |
| Molecular Function | GO:0097257 | leukotriene B4 12-hydroxy dehydrogenase activity |
| Biological Process | GO:0036102 | leukotriene B4 metabolic process |
| Biological Process | GO:0006691 | leukotriene metabolic process |
| Biological Process | GO:2001302 | lipoxin A4 metabolic process |
| Biological Process | GO:0006693 | prostaglandin metabolic process |
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] He J, Lai T, Zhou Z, Yang H, Lei Z et al.. Multiomics profiling reveals the involvement of protein lactylation in nonhomologous end joining pathway conferring radioresistance in lung adenocarcinoma cell.. Sci Rep 15(1):24651. 2025 Jul 9. PMID: 40634431.