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Primary Information | |
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| BoMiProt ID | Bomi114 |
| Protein Name | Cathelicidin-3 |
| Organism | Bos taurus |
| Uniprot ID | P19661 |
| Milk Fraction | Whey |
| 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, Phosphorylation | |
| CATH | Matched CATH superfamily 1.20.1270.10 2.60.34.10 |
| 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 |
| PDB ID | 4JWC, 4JWD, 5F8K, 5HAU, |
| 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. |