PMID- 11306067
OWN - NLM
STAT- MEDLINE
DCOM- 20010510
LR  - 20190826
IS  - 0009-2797 (Print)
IS  - 0009-2797 (Linking)
VI  - 130-132
IP  - 1-3
DP  - 2001 Jan 30
TI  - Cloning of the human RoDH-related short chain dehydrogenase gene and analysis of 
      its structure.
PG  - 457-67
AB  - We have previously characterized the first human NAD(+)-dependent short chain 
      dehydrogenase capable of oxidizing all-trans-retinol and androgens, and found 
      only in the liver and skin. In a search for related human enzymes, we identified 
      a partial open reading frame, which exhibited >60% sequence identity to human 
      RoDH-4. The full-length cDNA for this enzyme was determined in our laboratory by 
      5'-RACE PCR and was found to be identical to the recently reported novel type of 
      oxidative human 3alpha-hydroxysteroid dehydrogenase (3alpha-HSD). Analysis of the 
      genomic structure revealed that the gene for RoDH-like 3alpha-HSD has four 
      translated exons and, possibly, a fifth exon that codes for the 5'-untranslated 
      region. The gene for RoDH-4 appears to have only four exons. The positions of 
      exon-intron boundaries and the sizes of the protein coding regions are identical 
      in 3alpha-HSD and RoDH-4. Moreover, both genes are mapped to chromosome 12q13, 
      and are located in a close proximity to each other. Both genes appear to have 
      satellite pseudogenes. Thus, RoDH-4 and 3alpha-HSD genes share similar structural 
      organization and cluster on human chromosome 12, near the gene for 11-cis retinol 
      dehydrogenase.
FAU - Kedishvili, N Y
AU  - Kedishvili NY
AD  - Division of Molecular Biology and Biochemistry, School of Biological Sciences, 
      University of Missouri-Kansas City, 5007 Rockhill Road, 103 BSB, 64110, Kansas 
      City, MO, USA. kedishvilin@umkc.edu
FAU - Belyaeva, O V
AU  - Belyaeva OV
FAU - Gough, W H
AU  - Gough WH
LA  - eng
SI  - GENBANK/AF016509
GR  - R01 AA012153/AA/NIAAA NIH HHS/United States
GR  - AA00221/AA/NIAAA NIH HHS/United States
PT  - Comparative Study
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - Ireland
TA  - Chem Biol Interact
JT  - Chemico-biological interactions
JID - 0227276
RN  - 0 (DNA Primers)
RN  - 0 (DNA, Complementary)
RN  - EC 1.1.- (3-Hydroxysteroid Dehydrogenases)
RN  - EC 1.1.- (Alcohol Oxidoreductases)
RN  - EC 1.1.1.- (trans-retinol dehydrogenase)
RN  - EC 1.1.1.105 (retinol dehydrogenase)
RN  - EC 1.1.1.50 (3-alpha-Hydroxysteroid Dehydrogenase (B-Specific))
SB  - IM
MH  - 3-Hydroxysteroid Dehydrogenases/chemistry/genetics/metabolism
MH  - 3-alpha-Hydroxysteroid Dehydrogenase (B-Specific)
MH  - Alcohol Oxidoreductases/chemistry/*genetics/metabolism
MH  - Amino Acid Sequence
MH  - Base Sequence
MH  - Chromosome Mapping
MH  - Cloning, Molecular
MH  - DNA Primers/genetics
MH  - DNA, Complementary/genetics
MH  - Exons
MH  - Humans
MH  - Introns
MH  - Molecular Sequence Data
MH  - Sequence Homology, Amino Acid
EDAT- 2001/04/18 10:00
MHDA- 2001/05/22 10:01
CRDT- 2001/04/18 10:00
PHST- 2001/04/18 10:00 [pubmed]
PHST- 2001/05/22 10:01 [medline]
PHST- 2001/04/18 10:00 [entrez]
AID - S000927970000291X [pii]
AID - 10.1016/s0009-2797(00)00291-x [doi]
PST - ppublish
SO  - Chem Biol Interact. 2001 Jan 30;130-132(1-3):457-67. doi: 
      10.1016/s0009-2797(00)00291-x.