THIMET OLIGOPEPTIDASE - SIMILARITY TO SOLUBLE ANGIOTENSIN II-BINDING PROTEIN AND SOME CORRECTIONS TO THE PUBLISHED AMINO-ACID-SEQUENCE OF THE RAT TESTIS ENZYME

The deduced amino acid sequence of pig liver soluble angiotensin II-bi nding protein [Sugiura, Hagiwara and Hirose (1992) J. Biol. Chem. 267, 18067-18072] is similar over most of its length to that reported for rat testis thimet oligopeptidase (EC 3.4.24.15) by Pierotti, Dong, Glu cksman, Orlowski and Roberts [(1990) (Biochemistry 29, 10323-10329]. W e have found that homogeneous rat testis thimet oligopeptidase binds a ngiotensin II with the same distinctive characteristics as the pig liv er protein. Analysis of the nucleotide sequences reported for the two proteins pointed to the likelihood that sequencing errors had caused t wo segments of the amino acid sequence of the rat protein to be transl ated out of frame, and re-sequencing of selected parts of the clone (k indly provided by the previous authors) confirmed this. The revised de duced amino acid sequence of rat thimet oligopeptidase contains 687 re sidues, representing a protein of 78 308 Da, and is more closely relat ed to those of the pig liver protein and other known homologues of thi met oligopeptidase than that described previously.