Primary structure of vitamin K-dependent human protein Z.
The primary structure of a vitamin K-dependent human protein Z was determined by a combination of analyses of 41 amino acid residues of the NH2-terminal region and 1265 nucleotide base pairs of a cDNA encoding the residual COOH-terminal part of the protein and the 3' noncoding region. Human protein Z has 360 amino acid residues which is less than that of bovine protein Z containing 396 residues. Human protein Z was composed of an NH2-terminal domain rich in gamma-carboxyglutamic acids, two epidermal growth factor-like domains and a COOH-terminal serine protease-like domain as was bovine protein Z.
Division of Enzyme Cytology, Institute for Enzyme Research, University of Tokushima, Japan.
H
H
Sejima
T
T
Hayashi
Y
Y
Deyashiki
J
J
Nishioka
K
K
Suzuki
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D001798:Blood Proteins / Q000235:genetics* / Q000302:isolation & purification; D002417:Cattle; D003488:Cyanogen Bromide; D004247:DNA / Q000235:genetics; D006801:Humans; D008969:Molecular Sequence Data; D015183:Restriction Mapping; D012689:Sequence Homology, Nucleic Acid; D014812:Vitamin K
D001798:Blood Proteins; C026080:plasma protein Z; D014812:Vitamin K; D004247:DNA; D003488:Cyanogen Bromide