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Overview
Cathelicidin (IPR001894)
Short name: Cathelicidin
Overlapping homologous superfamilies
None.
Family relationships
None.
Description
The precursor sequences of a number of antimicrobial peptides secreted by neutrophils (polymorphonuclear leukocytes) upon activation have been found to be evolutionarily related and are collectively known as cathelicidins [PMID: 7589491].
Structurally, these proteins consist of three domains: a signal sequence, a conserved region of about 100 residues that contains four cysteines involved in two disulphide bonds, and a highly divergent C-terminal section of variable size. It is in this C-terminal section that the antibacterial peptides are found; they are proteolytically processed from their precursor by enzymes such as elastase. This structure is shown in the following schematic representation:
+---+--------------------------------+--------------------+ |Sig| Propeptide C C C C | Antibacterial pep. | +---+----------------|--|--|--|------+--------------------+ | | | | +--+ +--+ 'C': conserved cysteine involved in a disulphide bond.
GO terms
Biological Process
GO:0006952 defense response
Molecular Function
No terms assigned in this category.
Cellular Component
GO:0005576 extracellular region
Contributing signatures
- PTHR10206 (PTHR10206)