AMPDB_295 | Defensin alpha 5

1 General Description

AMPDB ID: AMPDB_295

Protein Names: Defensin alpha 5 (Defensin-5) (HD5(20-94)) [Cleaved into: HD5(23-94); HD5(29-94); HD5(56-94); HD5(63-94)]

Protein Family: Alpha-defensin family

Gene Name: DEFA5 DEF5

Source Organism: Homo sapiens (Human)

Protein Length: 94 AA

Protein Existence: Evidence at protein level

2 Protein Sequence & Composition

MRTIAILAAILLVALQAQAESLQERADEATTQKQSGEDNQDLAISFAGNGLSALRTSGSQARATCYCRTGRCATRESLSGVCEISGRLYRLCCR

FASTA format

Counts of Amino Acids

'A': 14, 'R': 10, 'N': 2, 'D': 3, 'C': 6, 'Q': 7, 'E': 6, 'G': 7, 'H': 0, 'I': 5, 'L': 11, 'K': 1, 'M': 1, 'F': 1, 'P': 0, 'S': 9, 'T': 7, 'W': 0, 'Y': 2, 'V': 2

Frequencies of Amino Acids

'A': 14.89%, 'R': 10.64%, 'N': 2.13%, 'D': 3.19%, 'C': 6.38%, 'Q': 7.45%, 'E': 6.38%, 'G': 7.45%, 'H': 0%, 'I': 5.32%, 'L': 11.7%, 'K': 1.06%, 'M': 1.06%, 'F': 1.06%, 'P': 0%, 'S': 9.57%, 'T': 7.45%, 'W': 0%, 'Y': 2.13%, 'V': 2.13%

Missing Amino Acid(s)

H, P, W

Most Occurring Amino Acid(s)

Less Occurring Amino Acid(s)

F, K, M

Hydrophobic Amino Acid(s) Count

Hydrophilic Amino Acid(s) Count

Basic Amino Acid(s) Count

Acidic Amino Acid(s) Count

Modified Amino Acid(s) Count

Modified Amino Acid(s) Frequencies

Computed by biopython (version 1.79) & proteinAnalysis (version 1)

3 Physicochemical Properties

Sl. No.	Properties	Values	Reference
1.	Molecular Mass	10071.4 Da	Computed by ProtParam module (biopython 1.79)
2.	Aliphatic Index	87.447	Computed by ProtParam module (biopython 1.79)
3.	Instability Index (Half Life)	35.197	Computed by ProtParam module (biopython 1.79)
4.	Hydrophobicity (GRAVY)	-0.126	Computed by ProtParam module (biopython 1.79)
5.	Hydrophobic Moment	0.712	Computed by ProtParam module (biopython 1.79)
6.	Isoelectric Point	8.109	Computed by ProtParam module (biopython 1.79)
7.	Charge (at pH 7)	1.636	Computed by ProtParam module (biopython 1.79)
8.	Secondary Structure Fraction	0.223, 0.191, 0.34 [Helix, Turn, Sheet]	Computed by ProtParam module (biopython 1.79)
9.	Aromaticity	0.032	Computed by ProtParam module (biopython 1.79)
10.	Molar Extinction Coefficient (cysteine\|cystine)	2980, 3355	Computed by ProtParam module (biopython 1.79)

4.1 Target Organism(s)

B.adolescentis (Gram-positive), B.anthracis (Gram-positive), B.breve (Gram-positive), B.cereus (Gram-positive), B.longum (Gram-positive), E.coli (Gram-negative), E.faecium (Gram-positive), L.acidophilus (Gram-positive), L.fermentum (Gram-positive), L.monocytogenes (Gram-positive), P.aeruginosa (Gram-negative), S.aureus (Gram-positive), S.flexneri (Gram-negative), S.thermophilus (Gram-positive), S.typhimurium

4.2 Antimicrobial Activity

Antibiotic, Antimicrobial, Defensin, Fungicide, Anti-gram-negative, Anti-gram-Positive

4.3 Enzymatic Activity

4.4 Inhibitory Effect

4.5 Other Biological Activity

Non-hemolytic, Non-ribosomal

Activity data manually curated from Literature and UniProt

5 Database Cross-references

5.1 Literature Database

Citation 1: Jones DE, Bevins CL, Bevins CL. Paneth cells of the human small intestine express an antimicrobial peptide gene. J Biol Chem. 1992;267(32):23216-25. Published 1992 Nov 15. doi:

PMID: 1429669

Citation 2: Nusbaum C, Mikkelsen TS, Zody MC, et al. DNA sequence and analysis of human chromosome 8. Nature. 2006;439(7074):331-5. Published 2006 Jan 19. doi:10.1038/nature04406

PMID: 16421571

Citation 3: 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 4: Ghosh D, Porter E, Shen B, et al. Paneth cell trypsin is the processing enzyme for human defensin-5. Nat Immunol. 2002;3(6):583-90. Published 2002 Jun. doi:10.1038/ni797

PMID: 12021776

Citation 5: Quayle AJ, Porter EM, Nussbaum AA, et al. Gene expression, immunolocalization, and secretion of human defensin-5 in human female reproductive tract. Am J Pathol. 1998;152(5):1247-58. Published 1998 May. doi:

PMID: 9588893

Citation 6: Salzman NH, Ghosh D, Huttner KM, et al. Protection against enteric salmonellosis in transgenic mice expressing a human intestinal defensin. Nature. 2003;422(6931):522-6. Published 2003 Apr 3. doi:10.1038/nature01520

PMID: 12660734

Citation 7: 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 8: Spencer JD, Hains DS, Porter E, et al. Human alpha defensin 5 expression in the human kidney and urinary tract. PLoS One. 2012;7(2):e31712. Published 2012. doi:10.1371/journal.pone.0031712

PMID: 22359618

Citation 9: Schroeder BO, Ehmann D, Precht JC, et al. Paneth cell Î±-defensin 6 (HD-6) is an antimicrobial peptide. Mucosal Immunol. 2015;8(3):661-71. Published 2015 May. doi:10.1038/mi.2014.100

PMID: 25354318

Citation 10: Ehmann D, Wendler J, Koeninger L, et al. Paneth cell Î±-defensins HD-5 and HD-6 display differential degradation into active antimicrobial fragments. Proc Natl Acad Sci U S A. 2019;116(9):3746-3751. Published 2019 Feb 26. doi:10.1073/pnas.1817376116

PMID: 30808760

Citation 11: Szyk A, Wu Z, Tucker K, et al. Crystal structures of human alpha-defensins HNP4, HD5, and HD6. Protein Sci. 2006;15(12):2749-60. Published 2006 Dec. doi:10.1110/ps.062336606

PMID: 17088326

Citation 12: de Leeuw E, Rajabi M, Zou G, et al. Selective arginines are important for the antibacterial activity and host cell interaction of human alpha-defensin 5. FEBS Lett. 2009;583(15):2507-12. Published 2009 Aug 6. doi:10.1016/j.febslet.2009.06.051

PMID: 19589339

Citation 13: Wommack AJ, Robson SA, Wanniarachchi YA, et al. NMR solution structure and condition-dependent oligomerization of the antimicrobial peptide human defensin 5. Biochemistry. 2012;51(48):9624-37. Published 2012 Dec 4. doi:10.1021/bi301255u

PMID: 23163963

Citation 14: Rajabi M, Ericksen B, Wu X, et al. Functional determinants of human enteric Î±-defensin HD5: crucial role for hydrophobicity at dimer interface. J Biol Chem. 2012;287(26):21615-27. Published 2012 Jun 22. doi:10.1074/jbc.M112.367995

PMID: 22573326

Citation 15: Wang C, Shen M, Gohain N, et al. Design of a potent antibiotic peptide based on the active region of human defensin 5. J Med Chem. 2015;58(7):3083-93. Published 2015 Apr 9. doi:10.1021/jm501824a

PMID: 25782105

Citation 16: Xu D, Liao C, Zhang B, et al. Human Enteric Î±-Defensin 5 Promotes Shigella Infection by Enhancing Bacterial Adhesion and Invasion. Immunity. 2018;48(6):1233-1244.e6. Published 2018 Jun 19. doi:10.1016/j.immuni.2018.04.014

PMID: 29858013

5.2 Protein Sequence Databases

5.3 3D Structure Databases

	Sl. no.	PDB ID	Method	Resolution	Access Links	3D View

AlphaFoldDB: Q01523

5.4 Nucleotide Sequence Databases

Sl. no.	Accession(s)	Access Link(s)
1.	M97925	GenBank \|\| EMBL
2.	AF238378	GenBank \|\| EMBL
3.	CH471153	GenBank \|\| EMBL
4.	BC069690	GenBank \|\| EMBL
5.	BC107079	GenBank \|\| EMBL

CCDS: CCDS5963.1

RefSeq: NP_066290.1

5.5 Protein-Protein Interaction Databases

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

Ensembl: ENSGT00940000153268

5.9 Phylogenomic Databases

GeneTree: ENSGT00940000153268

5.10 Enzyme & Pathway Databases

BRENDA: Not found

BioCyc: Not found

5.11 Protein-RNA Interaction Databases

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