General Information of HIF (ID: HIFM0094)
HIF Name
Eosinophil cationic protein
HIF Synonym(s)
RNase 3, ECP, Eosinophil Cationic Protein
HIF Classification
Antimicrobial peptide (AMP)
Molecular Function
Antibiotic; Antimicrobial; Endonuclease; Hydrolase; Nuclease
Description RNase 3 has been identified in humans. It forms the first line of host defense against pathogenic infections and are a key component of the ancient innate immune system. [1]
Pfam Pancreatic ribonuclease (PF00074 )
Pathway Asthma (hsa05310 )
Sequence Click here to download the HIF sequence in FASTA format
External Links
Uniprot ID
ECP_HUMAN
APD ID
AP02103
Microbe Species (MIC) Regulated by This HIF
         Acinetobacter baumannii (gamma-proteobacteria) MIC00016
             Description The RNase 3 showed >10 bactericidal activity against Acinetobacter baumannii when the hemolytic activity of 11.2+0.1M or 11.2-0.1M and the peptide size reduction of 48%. [2]
         Candida albicans (budding yeasts) MIC00317
             Description The RNase 3H15A has max membrane depolarization 67.271.13 on Candida albicans(p<0.05). [2]
         Corynebacteriales (actinobacteria) MIC00842
             Description The RNase 3 were indeed able to totally inhibit mycobacterial growth in a low micromolar range, showing MIC100s from 10 to 20 M. [2]
         Enterococcus faecium (firmicutes) MIC00549
             Description The RNase 3 showed >10 bactericidal activity against Enterococcus faecium when the hemolytic activity of 11.2+0.1M or 11.2-0.1M and the peptide size reduction of 48%. [2]
         Escherichia coli (enterobacteria) MIC00516
             Description The RNase 3 showed bactericidal activity against Escherichia coli when the hemolytic activity of 11.2M. [2]
         Micrococcus luteus (actinobacteria) MIC00824
             Description The RNase 3 showed >10 bactericidal activity against Micrococcus luteus when the hemolytic activity of 11.2+0.1M or 11.2-0.1M and the peptide size reduction of 48%. [2]
         Mycolicibacterium vaccae (actinobacteria) MIC01786
             Description RNase 3 has bacterial viability of 55.1 0.6 on Mycobacterium vaccae. [3]
         Pseudomonas sp. (gamma-proteobacteria) MIC01053
             Description The RNase 3 showed >10 bactericidal activity against Pseudomonas sp. when the hemolytic activity of 11.2+0.1M or 11.2-0.1M and the peptide size reduction of 48%. [2]
         Staphylococcus aureus (firmicutes) MIC01208
             Description The RNase 3 showed >10 bactericidal activity against Staphylococcus aureus when the hemolytic activity of 11.2+0.1M or 11.2-0.1M and the peptide size reduction of 48%. [2]
References
1 Antimicrobial peptides and the skin immune defense system.J Allergy Clin Immunol. 2008 Aug;122(2):261-6. doi: 10.1016/j.jaci.2008.03.027. Epub 2008 Apr 25.
2 Exploring the mechanisms of action of human secretory RNase 3 and RNase 7 against Candida albicans.Microbiologyopen. 2016 Oct;5(5):830-845. doi: 10.1002/mbo3.373. Epub 2016 Jun 8.
3 Two human host defense ribonucleases against mycobacteria, the eosinophil cationic protein (RNase 3) and RNase 7.Antimicrob Agents Chemother. 2013 Aug;57(8):3797-805. doi: 10.1128/AAC.00428-13. Epub 2013 May 28.

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