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PMID: 3888670 Published · ppublish English Comparative Study Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Amino acid sequence of bovine protein Z: a vitamin K-dependent serine protease homolog.

FEBS letters ·Vol. 184 ·No. 2 ·1985-05-20 ·Pages 333-8

Højrup P, Jensen MS, Petersen TE

Abstract

The amino acid sequence of protein Z has been determined from sequence analysis performed on fragments obtained by chemical and enzymatic degradations. The polypeptide consists of a single chain containing 396 amino acid residues (Mr 43 677). Comparison with the vitamin K-dependent plasma proteins reveals an extensive homology. The N-terminal part, containing 13 gamma-carboxyglutamic acid and one beta-hydroxyaspartic acid residue, is extensively homologous to and of similar length to the light chain of factor X. The remainder of protein Z is homologous to the serine proteases and of similar size to the heavy chain of factor Xa, but of the active site residues only aspartic acid-102 is present. Histidine-57 and serine-195 are replaced in protein Z by threonine and alanine, respectively. The physiological function of protein Z is still uncertain.

MeSH Terms
Amino Acid Sequence Amino Acids/analysis Animals Blood Proteins/genetics Cattle Endopeptidases/genetics Mutation Protein Processing, Post-Translational Serine Endopeptidases
Chemicals
Amino Acids Blood Proteins plasma protein Z Endopeptidases Serine Endopeptidases
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Højrup P
Jensen M S
Petersen T E
Article Info
Journal
FEBS letters
Abbr.
FEBS Lett
ISSN
0014-5793
Published
1985-05-20
Pages
333-8
Language
English
Region
England
NLM ID
0155157
Subset
IM
Grants
NHLBI NIH HHS · HL 16238 · United States
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