Primary structure of keratinocyte transglutaminase
- Univ. of California, Davis (United States)
- Univ. of Cincinnati Medical Center, OH (United States)
- National Inst. of Environmental Health Sciences, Research Triangle Park, NC (United States)
The nucleotide and deduced amino acid sequences of the coding regions of human and rat keratinocyte transglutaminases (protein-glutamine: amine {gamma}-glutamyltransferase; EC 2.3.2.13) have been determined. These yield proteins of {approximately}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 extension beyond the N terminus of the tissue transglutaminase. This extension and the unreltaed 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.
- OSTI ID:
- 5044523
- Journal Information:
- Proceedings of the National Academy of Sciences of the United States of America; (United States), Vol. 87:23; ISSN 0027-8424
- Country of Publication:
- United States
- Language:
- English
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