Structure of bovine adrenal dopamine .beta.-monooxygenase, as deduced from cDNA and protein sequencing: evidence that the membrane-bound form of the enzyme is anchored by an uncleaved signal peptide

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Abstract
A full-length cDNA for dopamine .beta.-monooxygenase (D.beta.M) from bovine adrenal glands has been cloned and sequenced. The soluble and membrane-derived forms of D.beta.M have also been sequenced from their N-termini. While the observed sequences for the soluble protein correspond to those previously reported [Joh, T. H., and Hwang, O. (1986) Ann. N.Y. Acad. Sci. 493, 343-350], the heavy subunit of membrane-derived enzyme is found to contain a unique N-terminus. Alignment of this N-terminus with that deduced from cDNA cloning indicates identity at 22 (and possibly 26) out of 27 residues. This comparison leads us to conclude that the membranous form of bovine D.beta.M retains an uncleaved N-terminal signal peptide as the source of membrane anchoring.