Molecular cloning and sequence analysis of cDNA encoding human cholesterol 7α‐hydroxylase

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Abstract
A complete cDNA clone encoding human cholesterol 7α-hydroxylase has been isolated using a rat P-450ch7α cDNA insert [(1989) FEBS Lett. 257, 97-100] as a probe and totally sequenced. The cDNA contained 1512-base pair open reading frame encoding 504 amino acid residues (M r, 57630), 39-base pair 5'-untranslated region 1322-base pair 3'-untranslated region including 20 nucleotides of poly A tail in the total length of 2873 base pairs. The deduced amino acid sequence showed 82% similarity to rat P-450ch7α. Unique amino acid residues were observed in putative binding domains for heme and steroid which are highly conserved in most steroidogenic P-450s.