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Human protein S cDNA encodes Phe-16 and Tyr 222 in consensus sequences for the post-translational processing
H K Ploos van Amstel1, A L van der Zanden, P H Reitsma
1Dept of Hematology, Leiden University Hospital, The Netherlands.
FEBS Letters
|September 28, 1987
Summary
Researchers identified partial human protein S cDNAs, revealing sequence variations important for post-translational modifications like gamma-carboxylation and hydroxylation.
Area of Science:
- Molecular Biology
- Biochemistry
Background:
- Human protein S is a crucial vitamin K-dependent plasma glycoprotein involved in the regulation of blood coagulation.
- Accurate protein sequencing is vital for understanding protein function and post-translational modifications.
Purpose of the Study:
- To isolate and characterize partial complementary DNAs (cDNAs) encoding human protein S.
- To identify sequence variations in human protein S and their potential impact on post-translational modifications.
Main Methods:
- Isolation of partial human protein S cDNAs from a human liver cDNA library using pUC9 vectors.
- Sequence analysis of overlapping cDNA clones to determine the coding and untranslated regions.
- Comparison of the derived amino acid sequence with previously reported sequences.
Main Results:
- Overlapping cDNA clones provided a partial 5'-non-coding region and complete protein S coding and 3'-untranslated regions.
- The derived amino acid sequence exhibited five deviations from two previously reported protein S sequences.
- Two specific sequence differences were noted in regions critical for gamma-carboxylation of glutamic acid and hydroxylation of asparagine.
Conclusions:
- The identified sequence variations in human protein S may influence its post-translational modification processes.
- Further investigation is warranted to fully elucidate the functional consequences of these sequence differences on protein S activity and regulation of coagulation.