title: Characterization of an almost full-length cDNA coding for human blood coagulation factor X.
abstract: A human liver cDNA library was screened by colony hybridization with a bovine factor X cDNA probe. Three of the positive plasmids contained overlapping DNA that coded for most of human factor X mRNA. DNA sequence analysis of these three clones allowed the prediction of the complete amino acid sequence of plasma factor X. From these studies, we predict that human factor X is synthesized as a single polypeptide chain precursor in which the light and heavy chains of plasma factor X are linked by the tripeptide Arg-Lys-Arg. The cDNA sequence also predicts that human factor X is synthesized as a preproprotein having an amino-terminal leader peptide of at least 28 amino acid residues. A comparison of the amino acid sequences of human and bovine factor X shows high sequence identity around the calcium-binding regions and catalytic regions but low sequence identity around the nonfunctional regions.
authors.forename: M R
authors.initials: MR
authors.lastname: Fung
authors.forename: C W
authors.initials: CW
authors.lastname: Hay
authors.forename: R T
authors.initials: RT
authors.lastname: MacGillivray
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D002417:Cattle; D004247:DNA / Q000032:analysis*; D004262:DNA Restriction Enzymes / Q000378:metabolism; D005170:Factor X / Q000235:genetics*; D006801:Humans; D011061:Poly A / Q000032:analysis; D012313:RNA / Q000032:analysis; D012333:RNA, Messenger / Q000032:analysis
chemical_list: D012333:RNA, Messenger; D011061:Poly A; D012313:RNA; D005170:Factor X; D004247:DNA; D004262:DNA Restriction Enzymes