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. 1987 Aug;84(15):5148–5152. doi: 10.1073/pnas.84.15.5148

Isolation of cDNA clones coding for human tissue factor: primary structure of the protein and cDNA.

E K Spicer, R Horton, L Bloem, R Bach, K R Williams, A Guha, J Kraus, T C Lin, Y Nemerson, W H Konigsberg
PMCID: PMC298811  PMID: 3037536

Abstract

Tissue factor is a membrane-bound procoagulant protein that activates the extrinsic pathway of blood coagulation in the presence of factor VII and calcium. lambda Phage containing the tissue factor gene were isolated from a human placental cDNA library. The amino acid sequence deduced from the nucleotide sequence of the cDNAs indicates that tissue factor is synthesized as a higher molecular weight precursor with a leader sequence of 32 amino acids, while the mature protein is a single polypeptide chain composed of 263 residues. The derived primary structure of tissue factor has been confirmed by comparison to protein and peptide sequence data. The sequence of the mature protein suggests that there are three distinct domains: extracellular, residues 1-219; hydrophobic, residues 220-242; and cytoplasmic, residues 243-263. Three potential N-linked carbohydrate attachment sites occur in the extracellular domain. The amino acid sequence of tissue factor shows no significant homology with the vitamin K-dependent serine proteases, coagulation cofactors, or any other protein in the National Biomedical Research Foundation sequence data bank (Washington, DC).

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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