Premium
Amino acid sequence of CAP37, a human neutrophil granule‐derived antibacterial and monocyte‐specific chemotactic glycoprotein structurally similar to neutrophil elastase
Author(s) -
Pohl Jan,
Pereira H.Anne,
Martin Nancy M.,
Spitznagel John K.
Publication year - 1990
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(90)80484-z
Subject(s) - serine , neutrophil elastase , biochemistry , glycoprotein , peptide sequence , elastase , amino acid , azurophilic granule , glycosylation , chemotaxis , proteinase 3 , monocyte , biology , granule (geology) , serine protease , serine proteinase inhibitors , microbiology and biotechnology , protease , enzyme , inflammation , immunology , myeloperoxidase , receptor , gene , paleontology
We report the amino acid sequence of CAP37, a human neutrophil granule protein with antibacterial and monocyte‐specific chemotactic activity. CAP37 is a single‐chain protein consisting of 222 amino acid residues. It has three N ‐glycosylation sites, at Asn residues 100, 114 and 145. Some species of CAP37 are glycosylated at all three sites; some at Asn‐114 alone, others at Asn‐114 and Asn‐110 or Asn‐145. CAP37 has 45% sequence identity to human neutrophil elastase, and 30–37% identity to several other granule serine proteinases. Despite these similarities, CAP37 is not a serine proteinase because the active site residues serine and histidine are replaced.