Binds to bacterial lipopolysaccharides (LPS), has antibacterial activity. (updated: Jan. 7, 2015)
The data and differentiation stages presented below come from the proteomic study and analysis performed by our partners of the GReX consortium, more details are available in their published work.
No sequence conservation computed yet.
Total structural coverage: 63%
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The reference OMIM entry for this protein is 600474
Cathelicidin antimicrobial peptide; camp
Cationic antimicrobial protein, 18-kd; cap18
Cramp, mouse, homolog of; cramp ll37, included
Peptide antibiotic, pr-39, porcine, homolog of, included; fall39, included
DESCRIPTION
Antimicrobial peptides, such as cathelicidins, are secreted by activated epithelial cells and invading leukocytes and play an important role in host defense. Like other cathelicidins, the full-length CAMP protein (also called CAP18) consists of an N-terminal signal peptide, a conserved cathelin-like domain, and a C-terminal antimicrobial domain corresponding to the mature antimicrobial peptide. The mature antimicrobial peptide cleaved from full-length CAMP, LL37, promotes inflammation, angiogenesis, wound healing, and tumor metastasis (summary by Subramanian et al., 2011).
CLONING
Animal peptide antibiotics can functionally be divided into 2 groups: those that accumulate in the granule of phagocytes and kill engulfed microbes (e.g., HNP1;
125220), and those that are delivered into body fluids or epithelial layers (e.g., DEF5;
600472). By PCR screen of a human cDNA library, Agerberth et al. (1995) isolated FALL39, the human counterpart of the PR-39 animal peptide antibiotic found in pig intestine. FALL39, named for the first 4 N-terminal amino acids (phe-ala-leu-leu) and the total number of residues (39), is a peptide predicted to contain an amphipathic alpha helix. FALL39 lacks cysteine, making it different from all other previously isolated human peptide antibiotics of the defensin family, each of which contain 3 disulfide bridges. Agerberth et al. (1995) chemically synthesized the FALL39 peptide from the predicted amino acid sequence and showed it to be antibacterial. Zanetti et al. (1993) reported that a number of antibacterial peptides from different mammals contained a conserved pro-region very similar to cathelin, a cysteine protease inhibitor isolated from pig leukocytes. Agerberth et al. (1995) showed that prepro-FALL39 encodes a cathelin-like precursor protein consisting of 170 amino acids. By RNA blot analysis, they found that the gene for FALL39 is expressed mainly in bone marrow and testis, tissues that are not often sites of infection. Interestingly, other species (e.g., bull and Drosophila) express antibacterial proteins in reproductive organs as well. With resistance to classic antibiotics becoming a clinical problem, Agerberth et al. (1995) suggested that the peptide FALL39 (or even a fragment, such as the amphipathic alpha helix) has the potential to become an antibacterial drug. Larrick et al. (1996) independently cloned the human CAP18 gene from a human genomic phage library. Sequence analysis revealed that, like several other genes expressed late in polymorphonuclear leukocyte development, the CAP18 gene does not contain typical TATA box or CCAAT sequences. Western, Northern, and RT-PCR analysis showed that CAP18 is produced specifically in granulocytes. The family of CAP18 proteins share a similar overall structure: signal sequence, conserved N-terminal protein sequence of unknown function, and a C-terminal antimicrobial domain.
GENE STRUCTURE
Gudmundsson et al. (1996) characterized and sequenced the complete human FALL39 gene. It is a compact gene of 1,963 bp with 4 exons. Exons 1-3 encode for a signal sequence and the cathelin region. Exon 4 contains the information for the mature antibacterial peptide. Their results suggested that FALL39 is the only member of the cathelin gene family present in the human genome. Potential binding sites for acute-phase-response factors were identified in the promoter and in intron 2. Anti-(FALL39) IgG located the peptide in granulocytes ...
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Subscribe to this protein entry history
Feb. 2, 2018: Protein entry updated
Automatic update: Uniprot description updated
Dec. 19, 2017: Protein entry updated
Automatic update: Uniprot description updated
Nov. 23, 2017: Protein entry updated
Automatic update: Uniprot description updated
March 25, 2017: Additional information
No protein expression data in P. Mayeux work for CAMP
March 16, 2016: Protein entry updated
Automatic update: OMIM entry 600474 was added.
Jan. 24, 2016: Protein entry updated
Automatic update: model status changed