Abstract
The nucleotide and deduced amino acid sequances of the coding regions of human and rat keratinocyte transglutaminases (protein-glutamine: amine γ-glutamyltransferase; EC 2.3.2.13) 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 language | English (US) |
|---|---|
| Pages (from-to) | 9333-9337 |
| Number of pages | 5 |
| Journal | Proceedings of the National Academy of Sciences of the United States of America |
| Volume | 87 |
| Issue number | 23 |
| State | Published - 1990 |
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Keywords
- Cross-linked envelopes
- Evolution
- Molecular cloning
ASJC Scopus subject areas
- Genetics
- General
Cite this
Primary structure of keratinocyte transglutaminase. / Phillips, M. A.; Stewart, B. E.; Qin, Q.; Chakravarty, R.; Floyd, E. E.; Jetten, A. M.; Rice, R. H.
In: Proceedings of the National Academy of Sciences of the United States of America, Vol. 87, No. 23, 1990, p. 9333-9337.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Primary structure of keratinocyte transglutaminase
AU - Phillips, M. A.
AU - Stewart, B. E.
AU - Qin, Q.
AU - Chakravarty, R.
AU - Floyd, E. E.
AU - Jetten, A. M.
AU - Rice, R. H.
PY - 1990
Y1 - 1990
N2 - The nucleotide and deduced amino acid sequances of the coding regions of human and rat keratinocyte transglutaminases (protein-glutamine: amine γ-glutamyltransferase; EC 2.3.2.13) 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.
AB - The nucleotide and deduced amino acid sequances of the coding regions of human and rat keratinocyte transglutaminases (protein-glutamine: amine γ-glutamyltransferase; EC 2.3.2.13) 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.
KW - Cross-linked envelopes
KW - Evolution
KW - Molecular cloning
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UR - http://www.scopus.com/inward/citedby.url?scp=0025695585&partnerID=8YFLogxK
M3 - Article
C2 - 1979171
AN - SCOPUS:0025695585
VL - 87
SP - 9333
EP - 9337
JO - Proceedings of the National Academy of Sciences of the United States of America
JF - Proceedings of the National Academy of Sciences of the United States of America
SN - 0027-8424
IS - 23
ER -