AMPDB_230 | Neutrophil defensin 3
PEPTIDE SUMMARY
Neutrophil defensin 3
1 General Description
AMPDB ID: AMPDB_230
Protein Names: Neutrophil defensin 3 (Defensin; alpha 3) (HNP-3) (HP-3) (HP3) [Cleaved into: HP 3-56; Neutrophil defensin 2 (HNP-2) (HP-2) (HP2)]
Protein Family: Alpha-defensin family
Gene Name: DEFA3 DEF3
Source Organism: Homo sapiens (Human)
Protein Length: 94 AA
Protein Existence: Evidence at protein level
2 Protein Sequence & Composition
2.1 Sequence
MRTLAILAAILLVALQAQAEPLQARADEVAAAPEQIAADIPEVVVSLAWDESLAPKHPGSRKNMDCYCRIPACIAGERRYGTCIYQGRLWAFCC
FASTA format
2.2 Composition
Counts of Amino Acids
'A': 18, 'R': 7, 'N': 1, 'D': 4, 'C': 6, 'Q': 5, 'E': 6, 'G': 4, 'H': 1, 'I': 7, 'L': 9, 'K': 2, 'M': 2, 'F': 1, 'P': 6, 'S': 3, 'T': 2, 'W': 2, 'Y': 3, 'V': 5
Frequencies of Amino Acids
'A': 19.15%, 'R': 7.45%, 'N': 1.06%, 'D': 4.26%, 'C': 6.38%, 'Q': 5.32%, 'E': 6.38%, 'G': 4.26%, 'H': 1.06%, 'I': 7.45%, 'L': 9.57%, 'K': 2.13%, 'M': 2.13%, 'F': 1.06%, 'P': 6.38%, 'S': 3.19%, 'T': 2.13%, 'W': 2.13%, 'Y': 3.19%, 'V': 5.32%
Missing Amino Acid(s)
No Amino Acid(s) are missing in this protein
Most Occurring Amino Acid(s)
A
Less Occurring Amino Acid(s)
F, H, N
Hydrophobic Amino Acid(s) Count
54
Hydrophilic Amino Acid(s) Count
40
Basic Amino Acid(s) Count
10
Acidic Amino Acid(s) Count
10
Modified Amino Acid(s) Count
0
Modified Amino Acid(s) Frequencies
0
Computed by biopython (version 1.79) & proteinAnalysis (version 1)
3 Physicochemical Properties
Sl. No. Properties Values Reference
1. Molecular Mass 10245 Da Computed by ProtParam module (biopython 1.79)
2. Aliphatic Index 100.957 Computed by ProtParam module (biopython 1.79)
3. Instability Index (Half Life) 43.718 Computed by ProtParam module (biopython 1.79)
4. Hydrophobicity (GRAVY) 0.229 Computed by ProtParam module (biopython 1.79)
5. Hydrophobic Moment 0.577 Computed by ProtParam module (biopython 1.79)
6. Isoelectric Point 5.791 Computed by ProtParam module (biopython 1.79)
7. Charge (at pH 7) -1.274 Computed by ProtParam module (biopython 1.79)
8. Secondary Structure Fraction 0.287, 0.149, 0.372 [Helix, Turn, Sheet] Computed by ProtParam module (biopython 1.79)
9. Aromaticity 0.064 Computed by ProtParam module (biopython 1.79)
10. Molar Extinction Coefficient (cysteine|cystine) 15470, 15845 Computed by ProtParam module (biopython 1.79)
4 Activity Details
4.1 Target Organism(s)
Clostridium difficile (Gram-positive), Staphylococcus aureus (Gram-positive)
4.2 Antimicrobial Activity
Antibiotic, Antimicrobial, Defensin, Fungicide, Anti-HSV, Anti-gram-Positive
4.3 Enzymatic Activity
Not found
4.4 Inhibitory Effect
Not found
4.5 Other Biological Activity
Cytotoxin, Non-hemolytic, Non-ribosomal
Activity data manually curated from Literature and UniProt
5 Database Cross-references
5.1 Literature Database
5.1.1 PubMed
Citation 1: Daher KA, Lehrer RI, Ganz T, et al. Isolation and characterization of human defensin cDNA clones. Proc Natl Acad Sci U S A. 1988;85(19):7327-31. Published 1988 Oct. doi:10.1073/pnas.85.19.7327
PMID: 3174637
Citation 2: Wiedemann LM, Francis GE, Lamb RF, et al. Differentiation stage-specific expression of a gene during granulopoiesis. Leukemia. 1989;3(3):227-34. Published 1989 Mar. doi:
PMID: 2918759
Citation 3: Linzmeier R, Michaelson D, Liu L, et al. The structure of neutrophil defensin genes. FEBS Lett. 1993;321(2-3):267-73. Published 1993 Apr 26. doi:10.1016/0014-5793(93)80122-b
PMID: 8477861
Citation 4: Linzmeier R, Michaelson D, Liu L, et al. The structure of neutrophil defensin genes. FEBS Lett. 1993;326(1-3):299-300. Published 1993 Jul 12. doi:10.1016/0014-5793(93)81813-f
PMID: 8325384
Citation 5: Gerhard DS, Wagner L, Feingold EA, et al. The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004;14(10B):2121-7. Published 2004 Oct. doi:10.1101/gr.2596504
PMID: 15489334
Citation 6: Selsted ME, Harwig SS, Ganz T, et al. Primary structures of three human neutrophil defensins. J Clin Invest. 1985;76(4):1436-9. Published 1985 Oct. doi:10.1172/JCI112121
PMID: 4056036
Citation 7: Selsted ME, Harwig SS, Harwig SS. Determination of the disulfide array in the human defensin HNP-2. A covalently cyclized peptide. J Biol Chem. 1989;264(7):4003-7. Published 1989 Mar 5. doi:
PMID: 2917986
Citation 8: Valore EV, Ganz T, Ganz T. Posttranslational processing of defensins in immature human myeloid cells. Blood. 1992;79(6):1538-44. Published 1992 Mar 15. doi:
PMID: 1339298
Citation 9: Ericksen B, Wu Z, Lu W, et al. Antibacterial activity and specificity of the six human {alpha}-defensins. Antimicrob Agents Chemother. 2005;49(1):269-75. Published 2005 Jan. doi:10.1128/AAC.49.1.269-275.2005
PMID: 15616305
Citation 10: Kim C, Gajendran N, Mittrücker HW, et al. Human alpha-defensins neutralize anthrax lethal toxin and protect against its fatal consequences. Proc Natl Acad Sci U S A. 2005;102(13):4830-5. Published 2005 Mar 29. doi:10.1073/pnas.0500508102
PMID: 15772169
Citation 11: Hazrati E, Galen B, Lu W, et al. Human alpha- and beta-defensins block multiple steps in herpes simplex virus infection. J Immunol. 2006;177(12):8658-66. Published 2006 Dec 15. doi:10.4049/jimmunol.177.12.8658
PMID: 17142766
Citation 12: Giesemann T, Guttenberg G, Aktories K, et al. Human alpha-defensins inhibit Clostridium difficile toxin B. Gastroenterology. 2008;134(7):2049-58. Published 2008 Jun. doi:10.1053/j.gastro.2008.03.008
PMID: 18435932
Citation 13: Cardot-Martin E, Casalegno JS, Badiou C, et al. α-Defensins partially protect human neutrophils against Panton-Valentine leukocidin produced by Staphylococcus aureus. Lett Appl Microbiol. 2015;61(2):158-64. Published 2015 Aug. doi:10.1111/lam.12438
PMID: 25963798
Citation 14: Liu X, Chen Q, Luo Y, et al. Plasma levels of alarmin HNPs 1-3 associate with lung dysfunction after cardiac surgery in children. BMC Pulm Med. 2017;17(1):218. Published 2017 Dec 28. doi:10.1186/s12890-017-0558-4
PMID: 29282039
Citation 15: Hill CP, Yee J, Selsted ME, et al. Crystal structure of defensin HNP-3, an amphiphilic dimer: mechanisms of membrane permeabilization. Science. 1991;251(5000):1481-5. Published 1991 Mar 22. doi:10.1126/science.2006422
PMID: 2006422
Citation 16: Xie C, Prahl A, Ericksen B, et al. Reconstruction of the conserved beta-bulge in mammalian defensins using D-amino acids. J Biol Chem. 2005;280(38):32921-9. Published 2005 Sep 23. doi:10.1074/jbc.M503084200
PMID: 15894545
Citation 17: Zou G, de Leeuw E, Li C, et al. Toward understanding the cationicity of defensins. Arg and Lys versus their noncoded analogs. J Biol Chem. 2007;282(27):19653-65. Published 2007 Jul 6. doi:10.1074/jbc.M611003200
PMID: 17452329
5.2 Protein Sequence Databases
UniProt: P59666
5.3 3D Structure Databases
Sl. no. PDB ID Method Resolution Access Links 3D View
AlphaFoldDB: P59666
5.4 Nucleotide Sequence Databases
Sl. no. Accession(s) Access Link(s)
1. M21131 GenBank || EMBL
2. M23281 GenBank || EMBL
3. L12691 GenBank || EMBL
4. X13621 GenBank || EMBL
5. BC027917 GenBank || EMBL
RefSeq: NP_005208.1
5.5 Protein-Protein Interaction Databases
IntAct: P59666
MINT: Not found
DIP: Not found
BioGRID: Not found
5.6 Ligand Databases
BindingDB: Not found
DrugBank: Not found
ChEMBL: Not found
5.7 Family & Domain Databases
PANTHER: PTHR11876
PROSITE: PS00269
5.8 Genome Annotation Databases
KEGG: hsa:1668
5.9 Phylogenomic Databases
5.10 Enzyme & Pathway Databases
BRENDA: Not found
BioCyc: Not found
5.11 Protein-RNA Interaction Databases
RNAct: P59666




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