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Post‐translational processing of prepro‐urotensin II
Author(s) -
Conlon J.M.,
Arnold-Reed D.,
Balment R.J.
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)81500-n
Subject(s) - urotensin ii , monobasic acid , peptide sequence , biochemistry , peptide , amino acid , biology , chemistry , cleavage (geology) , protein primary structure , microbiology and biotechnology , gene , paleontology , receptor , fracture (geology) , polymer chemistry
The primary structure of a teleost prepro‐urotensin II may be deduced from the nucleotide sequence of cloned DNA complementary to carp prepro‐urotensin II mRNA but the pathway of post‐translational processing of the precursor is unknown. In this study, we have isolated four peptides from an extract of flounder urophysis that are derived from prepro‐urotensin II by proteolytic cleavage. The amino acid sequences of the peptides demonstrate that flounder prepro‐urotensin II is cleaved at two monobasic processing sites (single arginine residues) to generate peptides with limited homology to carp prepro‐urotensin II‐(22–4l)‐, ‐(42–87)‐ and ‐(88–110)‐peptides. Cleavage at a tribasic residue processing site generates a urotensin II with the primary structure: Ala‐Gly‐Thr‐Thr‐Glu‐Cys‐Phe‐Trp‐Lys‐Tyr‐Cys‐Val. Urotensin II‐(4–12)‐peptide represented a minor component in the extract.