The new vertebrate CYP1C family: Cloning of new subfamily members and phylogenetic analysis
- Godard, C.A., Goldstone, J.V., Said, M.R., Dickerson, R.L., Woodin, B.R., and Stegeman, J.J.
- Biochemical and Biophysical Research Communications 331(4): 1016-1024 (Journal)
- Registered Authors
- Goldstone, Jed, Stegeman, John J.
- Cytochrome P450; CYP1A; CYP1B1; CYP1C; PAH; Planar aromatic hydrocarbons
- MeSH Terms
- Amino Acid Sequence
- Cloning, Molecular
- Molecular Sequence Data
- Reverse Transcriptase Polymerase Chain Reaction
- Sequence Homology, Amino Acid
- 15882979 Full text @ Biochem. Biophys. Res. Commun.
Godard, C.A., Goldstone, J.V., Said, M.R., Dickerson, R.L., Woodin, B.R., and Stegeman, J.J. (2005) The new vertebrate CYP1C family: Cloning of new subfamily members and phylogenetic analysis. Biochemical and Biophysical Research Communications. 331(4):1016-1024.
Two novel CYP1 genes from teleost fish constituting a new subfamily have been cloned. These paralogous sequences are designated CYP1C1 and CYP1C2. Both genes were initially obtained from untreated scup Stenotomus chrysops tissues by RT-PCR and RACE. Scup CYP1C1 and CYP1C2 code for 524 and 525 amino acids, respectively, and share 80-81% identity at the nucleotide and amino acid levels. Orthologues of CYP1C1 and CYP1C2 were identified in genome databases for other fish species, and both CYP1B1 and CYP1C1 were cloned from zebrafish (Danio rerio). Phylogenetic analysis shows that CYP1Cs and CYP1Bs constitute a sister clade to the CYP1As. Analysis of sequence domains likely to have functional significance suggests that the two CYP1Cs in scup may have catalytic functions and/or substrate specificity that differ from each other and from those of mammalian CYP1Bs or CYP1As. RT-PCR results indicate that CYP1C1 and CYP1C2 are variously expressed in several scup organs.
Genes / Markers
Mutations / Transgenics
Human Disease / Model
Sequence Targeting Reagents
Engineered Foreign Genes