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Diminuto the enzyme 3-beta-hydroxysterol delta-24-reductase (DHCR24), a member of the flavin adenine dinucleotide (FAD)-dependent oxidoreductases, catalyzes the reduction of the delta-24 double bond of sterol intermediates during cholesterol biosynthesis. Highly expressed in brain and adrenal gland with moderate expression in liver, lung, spleen, prostate and spinal cord. Low expression in heart, uterus and prostate. Undetectable in blood cells. Overexpressed in the adenoma tissue of patients with Cushing's syndrome. May be involved in the molecular events of adrenocortical tumorigenesis by facilitating steroid synthesis and cell growth. Note: This description may include information from UniProtKB.
Protein type: EC; Lipid Metabolism - steroid biosynthesis; Membrane protein, integral; Oxidoreductase
Chromosomal Location of Human Ortholog: 1p32.3
Cellular Component: endoplasmic reticulum; endoplasmic reticulum membrane; membrane; nucleus
Molecular Function: delta24(24-1) sterol reductase activity; delta24-sterol reductase activity; enzyme binding; oxidoreductase activity, acting on the CH-CH group of donors, NAD or NADP as acceptor; peptide antigen binding
Biological Process: cholesterol biosynthetic process; cholesterol biosynthetic process via desmosterol; cholesterol biosynthetic process via lathosterol; negative regulation of apoptosis; negative regulation of caspase activity; response to oxidative stress; skin development; tissue development
Disease: Desmosterolosis
Reference #:  Q15392 (UniProtKB)
Alt. Names/Synonyms: 24-dehydrocholesterol reductase; 3 beta-hydroxysterol delta 24-reductase; 3-beta-hydroxysterol delta-24-reductase; DCE; desmosterol-to-cholesterol enzyme; DHC24; DHCR24; Diminuto/dwarf1 homolog; KIAA0018; Nbla03646; seladin 1; Seladin-1; SELADIN1; selective AD indicator 1
Gene Symbols: DHCR24
Molecular weight: 60,101 Da
Basal Isoelectric point: 8.42  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
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Protein Structure Not Found.

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