HSD3B1 — Hydroxy-delta-5-steroid dehydrogenase, 3 beta- and steroid delta-isomerase 1
HSD3B1 belongs to a gene co-expression module in 1 of 28 SCUBA cell types. Each module groups genes that rise and fall together in that cell type; the genes it shares a module with are its closest co-expression partners there.
HSD3B1's module in each cell type
| Cell type | Module | Shares the module with | |
|---|---|---|---|
| Enterocytes | Xenobiotic Detoxification Nutrient metabolism | ARHGDIG, FAM151A, FMO1, GSTA2, HADH, IDH1, KCNJ13, OTC +1 more | View in SCUBA |
About the gene
| Synonyms | HSD3B, HSDB3, SDR11E1 |
|---|---|
| Chromosome | 1: 119507198-119515054 |
| Predicted location | Intracellular, Membrane |
| Essential gene | No |
| Protein class | Enzymes, FDA approved drug targets, Metabolic proteins, Predicted intracellular proteins, Predicted membrane proteins |
| Molecular function | Isomerase, Multifunctional enzyme, Oxidoreductase |
| Biological process | Lipid metabolism, Steroid metabolism, Steroidogenesis |
Function
A bifunctional enzyme responsible for the oxidation and isomerization of 3beta-hydroxy-Delta(5)-steroid precursors to 3-oxo- Delta(4)-steroids, an essential step in steroid hormone biosynthesis. Specifically catalyzes the conversion of pregnenolone to progesterone, 17alpha-hydroxypregnenolone to 17alpha-hydroxyprogesterone, dehydroepiandrosterone (DHEA) to 4-androstenedione, and androstenediol to testosterone. Additionally, catalyzes the interconversion between 3beta-hydroxy and 3-oxo-5alpha-androstane steroids controlling the bioavalability of the active forms. Specifically converts dihydrotestosterone to its inactive form 5alpha-androstanediol, that does not bind androgen receptor/AR. Also converts androstanedione, a precursor of testosterone and estrone, to epiandrosterone. Expected to use NAD(+) as preferred electron donor for the 3beta-hydroxy-steroid dehydrogenase activity and NADPH for the 3-ketosteroid reductase activity (Probable).
Human Protein Atlas · Open Targets · UniProt
Gene annotation from the Human Protein Atlas and UniProt; see sources & licences.