DHRS2
Function
NADPH-dependent oxidoreductase which catalyzes the reduction of dicarbonyl compounds. Displays reductase activity in vitro with 3,4-hexanedione, 2,3-heptanedione and 1-phenyl-1,2-propanedione as substrates (PubMed:16685466). May function as a dicarbonyl reductase in the enzymatic inactivation of reactive carbonyls involved in covalent modification of cellular components (PubMed:16685466). Also displays a minor hydroxysteroid dehydrogenase activity toward bile acids such as ursodeoxycholic acid (UDCA) and isoursodeoxycholic acid (isoUDCA), which makes it unlikely to control hormone levels (PubMed:16685466). Doesn't show any activity in vitro with retinoids and sugars as substrates (PubMed:16685466). Attenuates MDM2-mediated p53/TP53 degradation, leading to p53/TP53 stabilization and increased transcription activity, resulting in the accumulation of MDM2 and CDKN1A/p21 (PubMed:20547751). Reduces proliferation, migration and invasion of cancer cells and well as the production of ROS in cancer (PubMed:29106393).
Sequence Similarities
Belongs to the short-chain dehydrogenases/reductases (SDR) family.
Tissue Specificity
Widely expressed, with highest levels in liver and kidney, followed by heart, spleen, skeletal muscle and placenta. In hemopoietic cells, expressed in dendritic cells, but not in monocytes, macrophages, granulocytes, nor in B and T lymphocytes.
Cellular localization
- Mitochondrion matrix
- Nucleus
- A minor fraction of the protein is translocated from the mitochondria to the nucleus, after cleavage of the targeting signal.
Alternative names
SDR25C1, DHRS2, Dicarbonyl reductase HEP27, Protein D, Short chain dehydrogenase/reductase family 25C member 1, Protein SDR25C1