Abstract
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.
Publication types
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Comparative Study
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Amino Acid Sequence
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Antimicrobial Cationic Peptides
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Blood Bactericidal Activity
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Blood Proteins / chemistry*
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Carrier Proteins*
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Chemotactic Factors / chemistry*
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Chromatography, High Pressure Liquid
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Disulfides
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Endopeptidases / metabolism
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Glycoproteins / chemistry*
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Glycosylation
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Leukocyte Elastase
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Metalloendopeptidases
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Molecular Sequence Data
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Pancreatic Elastase / chemistry*
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Peptide Fragments / chemistry
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Sequence Homology, Nucleic Acid
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Trypsin / metabolism
Substances
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AZU1 protein, human
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Antimicrobial Cationic Peptides
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Blood Proteins
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Carrier Proteins
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Chemotactic Factors
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Disulfides
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Glycoproteins
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Peptide Fragments
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Endopeptidases
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Pancreatic Elastase
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Leukocyte Elastase
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Trypsin
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Metalloendopeptidases
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endoproteinase Asp-N