17-Beta-Hydroxysteroid Dehydrogenase Type 14 (HSD17b14)

DHRS10; RetSDR3, SDR47C1; Retinal Short-Chain Dehydrogenase/Reductase 3; Short Chain Dehydrogenase/Reductase Family 47C,Member 1

SPN	R627
HGNC	23238
MGI	1913315
PubMed	22792371
RGD	1588673
UniProt	Q9BPX1

17-beta-hydroxysteroid dehydrogenases, such as HSD17B14, are primarily involved in metabolism of steroids at the C17 position and also of other substrates, such as fatty acids, prostaglandins, and xenobiotics.

The deduced 270-amino acid protein has a calculated molecular mass of 28.0 kD. It has all the characteristics of SDRs, including a cofactor-binding Rossman-fold domain and highly conserved motifs in the nucleotide-binding site and active site. Northern blot analysis detected HSD17B14 expression in liver, kidney, and retina.recombinant human DHRS10 converted NAD+ to NADH in the presence of estradiol, testosterone, or 5-androstene-3-beta,17-beta diol. Nonsaturable kinetics were found for testosterone, and no conversion was observed in the presence of NADPH.

Reference

"Short-chain dehydrogenases/reductases in retina."
Methods Enzymol. 316:372-383(2000) [PubMed] [Europe PMC] [Abstract]

"The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment."
Genome Res. 13:2265-2270(2003) [PubMed] [Europe PMC] [Abstract]

"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]

"Structural and biochemical characterization of human orphan DHRS10 reveals a novel cytosolic enzyme with steroid dehydrogenase activity."
Biochem. J. 402:419-427(2007) [PubMed] [Europe PMC] [Abstract]