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Molecular cloning and sequence analysis of cDNA encoding human cholesterol 7α‐hydroxylase
Author(s) -
Noshiro Mitsuhide,
Okuda Kyuichiro
Publication year - 1990
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(90)80992-r
Subject(s) - complementary dna , open reading frame , microbiology and biotechnology , untranslated region , biology , peptide sequence , amino acid , nucleic acid sequence , base pair , genetics , molecular cloning , biochemistry , gene , messenger rna
A complete cDNA clone encoding human cholesterol 7α‐hydroxylase has been isolated using a rat P‐450 ch7α 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‐450 ch7α . Unique amino acid residues were observed in putative binding domains for heme and steroid which are highly conserved in most steroidogenic P‐450s.