Q1KLY5 · CAMP_CEBCA

Function

function

Antimicrobial protein that is an integral component of the innate immune system (By similarity).
Binds to bacterial lipopolysaccharides (LPS) (By similarity).
Acts via neutrophil N-formyl peptide receptors to enhance the release of CXCL2 (By similarity).
Postsecretory processing generates multiple cathelicidin antimicrobial peptides with various lengths which act as a topical antimicrobial defense in sweat on skin (By similarity).
The unprocessed precursor form, cathelicidin antimicrobial peptide, inhibits the growth of Gram-negative E.coli and E.aerogenes with efficiencies comparable to that of the mature peptide LL-37 (in vitro) (By similarity).

Antibacterial peptide LL-37

Antimicrobial peptide that is an integral component of the innate immune system (By similarity).
Binds to bacterial lipopolysaccharides (LPS) (By similarity).
Causes membrane permeabilization by forming transmembrane pores (in vitro) (By similarity).
Causes lysis of E.coli (By similarity).
Exhibits antimicrobial activity against Gram-negative bacteria such as P.aeruginosa, S.typhimurium, E.aerogenes, E.coli and P.syringae, Gram-positive bacteria such as L.monocytogenes, S.epidermidis, S.pyogenes and S.aureus, as well as vancomycin-resistant enterococci (in vitro) (By similarity).
Exhibits antimicrobial activity against methicillin-resistant S.aureus, P.mirabilis, and C.albicans in low-salt media, but not in media containing 100 mM NaCl (in vitro) (By similarity).
Forms chiral supramolecular assemblies with quinolone signal (PQS) molecules of P.aeruginosa, which may lead to interference of bacterial quorum signaling and perturbance of bacterial biofilm formation (By similarity).
May form supramolecular fiber-like assemblies on bacterial membranes (By similarity).
Induces cytokine and chemokine producation as well as TNF/TNFA and CSF2/GMCSF production in normal human keratinocytes (By similarity).
Exhibits hemolytic activity against red blood cells (By similarity).

Antibacterial peptide FALL-39

Exhibits antimicrobial activity against E.coli and B.megaterium (in vitro).

GO annotations

AspectTerm
Cellular Componentextracellular space
Cellular Componentvesicle
Molecular Functionlipopolysaccharide binding
Biological Processantimicrobial humoral immune response mediated by antimicrobial peptide
Biological Processdefense response to Gram-negative bacterium
Biological Processdefense response to Gram-positive bacterium
Biological Processinnate immune response
Biological Processneutrophil activation

Keywords

Names & Taxonomy

Protein names

Gene names

    • Name
      CAMP

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Platyrrhini > Cebidae > Cebinae > Cebus

Accessions

  • Primary accession
    Q1KLY5

Subcellular Location

Secreted
Vesicle
Note: Stored as pro-peptide in granules and phagolysosomes of neutrophils (By similarity).
Secreted in sweat onto skin (By similarity).

Keywords

PTM/Processing

Features

Showing features for signal, propeptide, disulfide bond, peptide.

TypeIDPosition(s)Description
Signal1-30
PropeptidePRO_000025174631-131Cathelin-like domain (CLD)
Disulfide bond86↔97
Disulfide bond108↔125
PeptidePRO_0000251747132-170Antibacterial peptide FALL-39
PeptidePRO_0000251748134-170Antibacterial peptide LL-37

Post-translational modification

Proteolytically cleaved by proteinase PRTN3 into antibacterial peptide LL-37 (By similarity).
Proteolytically cleaved by cathepsin CTSG and neutrophil elastase ELANE (By similarity).

Antibacterial peptide LL-37

Resistant to proteolytic degradation in solution, and when bound to both zwitterionic (mimicking mammalian membranes) and negatively charged membranes (mimicking bacterial membranes).
After secretion onto the skin surface, the CAMP gene product is processed by a serine protease-dependent mechanism into multiple novel antimicrobial peptides distinct from and shorter than cathelicidin LL-37 (By similarity).
These peptides show enhanced antimicrobial action, acquiring the ability to kill skin pathogens such as S.aureus, E.coli and C.albicans. These peptides have lost the ability to stimulate CXCL8/IL8 release from keratinocytes (By similarity).
The peptides act synergistically, killing bacteria at lower concentrations when present together, and maintain activity at increased salt condition (By similarity).

Keywords

Interaction

Subunit

Antibacterial peptide LL-37

Monomer, homodimer or homotrimer (in vitro) (By similarity).
Oligomerizes as tetra- or hexamer in solution (in vitro) (By similarity).

Structure

Family & Domains

Features

Showing features for region.

TypeIDPosition(s)Description
Region150-162Active core

Domain

The cathelin-like domain (CLD), which is the propeptide part, does not seem to exhibit auto-inhibitory function, as it does not inhibit the antibacterial activity of antibacterial peptide LL-37.

Antibacterial peptide LL-37

Undergoes conformational change in the presence of lipid A, transitioning from a random coil to an alpha-helical structure.

Antibacterial peptide LL-37

Residues 17-29 of LL-37 represent the active core of the antimicrobial peptide. Forms ribbon-like fibrils and exhibits antibacterial activity against Gram-positive M.luteus (By similarity).
Also exhibits antibacterial activity against Gram-negative E.coli and P.fluorescens (By similarity).

Sequence similarities

Belongs to the cathelicidin family.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    170
  • Mass (Da)
    18,967
  • Last updated
    2006-05-30 v1
  • Checksum
    5830E3F24647DEA7
MKTQRDGPSLGRWSLVLLLLGLTMPLAITAQVLSYQEAVLRAVDGLNQRSLDANLYRLLNLDPRPTLDGDPDTPKPVSFTVKETVCPRTIQRSPEECDFKKDGLVKRCVGTVILNQARDSFDISCDKDERKVARLGGFLQKAREKIARGFKKIGQKINDFLGKLAPRTEA

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
DQ471357
EMBL· GenBank· DDBJ
ABE96621.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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