Search by BoMiProt ID - Bomi114

Primary Information

BoMiProt ID Bomi114
Protein Name Cathelicidin-3
Organism Bos taurus
Uniprot IDP19661
Milk FractionWhey
Ref Sequence ID NP_776426.1
Aminoacid Length 190
Molecular Weight 21567
FASTA Sequence Download
Gene Name CATHL3
Gene ID 281037
Protein Existence Status Reviewed: Experimental evidence at protein level

Secondary Information

Presence in other biological fluids/tissue/cells bovine neutrophil
Protein Function antimicrobial activity against Gram-negative bacteria; internalized into the cell where it inactivates intracellular targets; micropinocytosis; has cytolytic activity, involving membrane disruption and necrosis of host mammalian cells; In terms of fungicidal activity, Bac7 is active against Cryptococcus neoformans, which infects the lungs and central nervous system; displays activity against several Chlamydia strains; inhibit biofilms; prevents bacterial metabolism, likely disrupting biofilm formation
Biochemical Properties proline-rich peptides; positively charged peptides and make up 4% of total neutrophil proteins; linear peptide that is structurally comparable to Bac5; highly cationic (+11), and so is more hydrophobic than Bac5
Significance in milk initial response of the mammary epithelium to microbial infection
Site(s) of PTM(s)

N-glycosylation, O-glycosylation,
CATH Matched CATH superfamily
Predicted Disorder Regions 1-7,63-78,84-101,112-148,154-190
DisProt Annotation
TM Helix Prediction 1TMH; (13-31)
Significance of PTMs Antimicrobial peptides and upregulated in mastitis
Bibliography 1. Donati, M., Di Francesco, A., Gennaro, R., Benincasa, M., Magnino, S., Pignanelli, S., Shurdhi, A., Moroni, A., Mazzoni, C., Merialdi, G., Baldelli, R., and Cevenini, R. (2007) Sensitivity of Chlamydia suis to cathelicidin peptides. Vet. Microbiol. 123, 269–273.
2. Pompilio, A., Scocchi, M., Pomponio, S., Guida, F., Di Primio, A., Fiscarelli, E., Gennaro, R., and Di Bonaventura, G. (2011) Antibacterial and anti-biofilm effects of cathelicidin peptides against pathogens isolated from cystic fibrosis patients. Peptides 32, 1807–1814. >br/> 3.Tomasinsig, L., Benincasa, M., Scocchi, M., Skerlavaj, B., Tossi, A., Zanetti, M., and Gennaro, R. (2010) Role of Cathelicidin Peptides in Bovine Host Defense and Healing. Probiotics Antimicrob. Proteins 2, 12–20.
4. Frank, R. W., Gennaro, R., Schneider, K., Przybylski, M., and Romeo, D. (1990) Amino acid sequences of two proline-rich bactenecins. Antimicrobial peptides of bovine neutrophils. J. Biol. Chem. 265, 18871–18874.
5. Pelillo, C., Benincasa, M., Scocchi, M., Gennaro, R., Tossi, A., and Pacor, S. (2014) Cellular internalization and cytotoxicity of the antimicrobial proline-rich peptide Bac7(1-35) in monocytes/macrophages, and its activity against phagocytosed Salmonella typhimurium. Protein Pept. Lett. 21, 382–390.