Primary structure of keratinocyte transglutaminase

M. A. Phillips, B. E. Stewart, Q. Qin, R. Chakravarty, E. E. Floyd, A. M. Jetten, R. H. Rice

Research output: Contribution to journalArticlepeer-review

100 Scopus citations


The nucleotide and deduced amino acid sequances of the coding regions of human and rat keratinocyte transglutaminases (protein-glutamine: amine γ-glutamyltransferase; EC have been determined. These yield proteins of ≈90 kDa that are 92% identical, indicative of the conservation of important structural features. Alignments of amino acid sequences show substantial similarity among the keratinocyte transglutaminase, human clotting factor XIII catalytic subunit, guinea pig liver tissue transglutaminase, and the human erythrocyte band-4.2 protein. The keratinocyte enzyme is most similar to factor XIII, whereas the band-4.2 protein is most similar to the tissue transglutaminase. A salient feature of the keratinocyte transglutaminase is its 105-residue estension beyond the N terminus of the tissue transglutaminase. This extension and the unrelated activation peptide of factor XIII (a 37-residue extension) appear to be added for specialized functions after divergence of the tissue transglutaminase from their common lineage.

Original languageEnglish (US)
Pages (from-to)9333-9337
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Issue number23
StatePublished - 1990


  • Cross-linked envelopes
  • Evolution
  • Molecular cloning

ASJC Scopus subject areas

  • Genetics
  • General


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