Amino acid sequence of CAP37, a human neutrophil granule-derived antibacterial and monocyte-specific chemotactic glycoprotein structurally similar to neutrophil elastase

FEBS Lett. 1990 Oct 15;272(1-2):200-4. doi: 10.1016/0014-5793(90)80484-z.

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

  • Comparative Study
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Antimicrobial Cationic Peptides
  • Blood Bactericidal Activity
  • Blood Proteins / chemistry*
  • Carrier Proteins*
  • Chemotactic Factors / chemistry*
  • Chromatography, High Pressure Liquid
  • Disulfides
  • Endopeptidases / metabolism
  • Glycoproteins / chemistry*
  • Glycosylation
  • Leukocyte Elastase
  • Metalloendopeptidases
  • Molecular Sequence Data
  • Pancreatic Elastase / chemistry*
  • Peptide Fragments / chemistry
  • Sequence Homology, Nucleic Acid
  • Trypsin / metabolism

Substances

  • Antimicrobial Cationic Peptides
  • Blood Proteins
  • Carrier Proteins
  • Chemotactic Factors
  • Disulfides
  • Glycoproteins
  • Peptide Fragments
  • cationic antimicrobial protein CAP 37, human
  • Endopeptidases
  • Pancreatic Elastase
  • Leukocyte Elastase
  • Trypsin
  • Metalloendopeptidases
  • endoproteinase Asp-N