Human protein S cDNA encodes Phe-16 and Tyr 222 in consensus sequences for the post-translational processing.
Partial cDNAs coding for human protein S were isolated from a pUC9 human liver cDNA library. Together, the overlapping clones span a (partial) 5'-non-coding region, and the complete protein S coding and 3'-untranslated regions. The derived amino acid sequence deviates at five positions from two previously reported protein S sequences. Two of these differences (Phe instead of Leu at position -16 and Tyr instead of Asp at position 222) are found in regions that are important for the post-translational modification of protein S, the gamma-carboxylation of glutamic acid and the hydroxylation of asparagine, respectively.
Ploos van Amstel
H K
HK
Dept of Hematology, Leiden University Hospital, The Netherlands.
van der Zanden
A L
AL
Reitsma
P H
PH
Bertina
R M
RM
D000595:Amino Acid Sequence; D001483:Base Sequence; D003001:Cloning, Molecular; D004247:DNA / Q000378:metabolism*; D004262:DNA Restriction Enzymes; D005784:Gene Amplification; D005796:Genes; D006023:Glycoproteins / Q000235:genetics*; D006801:Humans; D008099:Liver / Q000378:metabolism; D008969:Molecular Sequence Data; D010649:Phenylalanine; D011499:Protein Processing, Post-Translational; D017293:Protein S; D014443:Tyrosine
D006023:Glycoproteins; D017293:Protein S; D014443:Tyrosine; D010649:Phenylalanine; D004247:DNA; D004262:DNA Restriction Enzymes