AMPDB_76 | Defensin beta 4A
PEPTIDE SUMMARY
Defensin beta 4A
1 General Description
AMPDB ID: AMPDB_76
Protein Names: Defensin beta 4A (Beta-defensin 2) (BD-2) (hBD-2) (Defensin; beta 2) (Skin-antimicrobial peptide 1) (SAP1)
Protein Family: Beta-defensin family; LAP TAP subfamily
Gene Name: DEFB4A DEFB102 DEFB2 DEFB4; DEFB4B
Source Organism: Homo sapiens (Human)
Protein Length: 64 AA
Protein Existence: Evidence at protein level
2 Protein Sequence & Composition
2.1 Sequence
MRVLYLLFSFLFIFLMPLPGVFGGIGDPVTCLKSGAICHPVFCPRRYKQIGTCGLPGTKCCKKP
FASTA format
2.2 Composition
Counts of Amino Acids
'A': 1, 'R': 3, 'N': 0, 'D': 1, 'C': 6, 'Q': 1, 'E': 0, 'G': 8, 'H': 1, 'I': 4, 'L': 8, 'K': 5, 'M': 2, 'F': 6, 'P': 7, 'S': 2, 'T': 3, 'W': 0, 'Y': 2, 'V': 4
Frequencies of Amino Acids
'A': 1.56%, 'R': 4.69%, 'N': 0%, 'D': 1.56%, 'C': 9.38%, 'Q': 1.56%, 'E': 0%, 'G': 12.5%, 'H': 1.56%, 'I': 6.25%, 'L': 12.5%, 'K': 7.81%, 'M': 3.13%, 'F': 9.38%, 'P': 10.94%, 'S': 3.13%, 'T': 4.69%, 'W': 0%, 'Y': 3.13%, 'V': 6.25%
Missing Amino Acid(s)
E, N, W
Most Occurring Amino Acid(s)
G, L
Less Occurring Amino Acid(s)
A, D, H, Q
Hydrophobic Amino Acid(s) Count
40
Hydrophilic Amino Acid(s) Count
24
Basic Amino Acid(s) Count
1
Acidic Amino Acid(s) Count
9
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 7037.66 Da Computed by ProtParam module (biopython 1.79)
2. Aliphatic Index 92.813 Computed by ProtParam module (biopython 1.79)
3. Instability Index (Half Life) 41.316 Computed by ProtParam module (biopython 1.79)
4. Hydrophobicity (GRAVY) 0.605 Computed by ProtParam module (biopython 1.79)
5. Hydrophobic Moment 0.52 Computed by ProtParam module (biopython 1.79)
6. Isoelectric Point 9.506 Computed by ProtParam module (biopython 1.79)
7. Charge (at pH 7) 6.714 Computed by ProtParam module (biopython 1.79)
8. Secondary Structure Fraction 0.375, 0.266, 0.172 [Helix, Turn, Sheet] Computed by ProtParam module (biopython 1.79)
9. Aromaticity 0.125 Computed by ProtParam module (biopython 1.79)
10. Molar Extinction Coefficient (cysteine|cystine) 2980, 3355 Computed by ProtParam module (biopython 1.79)
4 Activity Details
4.1 Target Organism(s)
C.albicans
4.2 Antimicrobial Activity
Antibiotic, Antimicrobial, Defensin, Anti-candida
4.3 Enzymatic Activity
Not found
4.4 Inhibitory Effect
Not found
4.5 Other Biological Activity
Chemotaxis, 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: Harder J, Bartels J, Christophers E, et al. A peptide antibiotic from human skin. Nature. 1997;387(6636):861. Published 1997 Jun 26. doi:10.1038/43088
PMID: 9202117
Citation 2: Liu L, Wang L, Jia HP, et al. Structure and mapping of the human beta-defensin HBD-2 gene and its expression at sites of inflammation. Gene. 1998;222(2):237-44. Published 1998 Nov 19. doi:10.1016/s0378-1119(98)00480-6
PMID: 9831658
Citation 3: Diamond G, Kaiser V, Rhodes J, et al. Transcriptional regulation of beta-defensin gene expression in tracheal epithelial cells. Infect Immun. 2000;68(1):113-9. Published 2000 Jan. doi:10.1128/IAI.68.1.113-119.2000
PMID: 10603376
Citation 4: Harder J, Meyer-Hoffert U, Teran LM, et al. Mucoid Pseudomonas aeruginosa, TNF-alpha, and IL-1beta, but not IL-6, induce human beta-defensin-2 in respiratory epithelia. Am J Respir Cell Mol Biol. 2000;22(6):714-21. Published 2000 Jun. doi:10.1165/ajrcmb.22.6.4023
PMID: 10837369
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: Yang D, Chertov O, Bykovskaia SN, et al. Beta-defensins: linking innate and adaptive immunity through dendritic and T cell CCR6. Science. 1999;286(5439):525-8. Published 1999 Oct 15. doi:10.1126/science.286.5439.525
PMID: 10521347
Citation 7: Klüver E, Schulz A, Forssmann WG, et al. Chemical synthesis of beta-defensins and LEAP-1/hepcidin. J Pept Res. 2002;59(6):241-8. Published 2002 Jun. doi:10.1034/j.1399-3011.2002.00980.x
PMID: 12010514
Citation 8: Röhrl J, Yang D, Oppenheim JJ, et al. Specific binding and chemotactic activity of mBD4 and its functional orthologue hBD2 to CCR6-expressing cells. J Biol Chem. 2010;285(10):7028-34. Published 2010 Mar 5. doi:10.1074/jbc.M109.091090
PMID: 20068036
Citation 9: Hoover DM, Rajashankar KR, Blumenthal R, et al. The structure of human beta-defensin-2 shows evidence of higher order oligomerization. J Biol Chem. 2000;275(42):32911-8. Published 2000 Oct 20. doi:10.1074/jbc.M006098200
PMID: 10906336
Citation 10: Sawai MV, Jia HP, Liu L, et al. The NMR structure of human beta-defensin-2 reveals a novel alpha-helical segment. Biochemistry. 2001;40(13):3810-6. Published 2001 Apr 3. doi:10.1021/bi002519d
PMID: 11300761
Citation 11: Bauer F, Schweimer K, Klüver E, et al. Structure determination of human and murine beta-defensins reveals structural conservation in the absence of significant sequence similarity. Protein Sci. 2001;10(12):2470-9. Published 2001 Dec. doi:10.1110/ps.24401
PMID: 11714914
Citation 12: Järvå M, Phan TK, Lay FT, et al. Human β-defensin 2 kills Candida albicans through phosphatidylinositol 4,5-bisphosphate-mediated membrane permeabilization. Sci Adv. 2018;4(7):eaat0979. Published 2018 Jul. doi:10.1126/sciadv.aat0979
PMID: 30050988
5.2 Protein Sequence Databases
UniProt: O15263
5.3 3D Structure Databases
Sl. no. PDB ID Method Resolution Access Links 3D View
AlphaFoldDB: O15263
5.4 Nucleotide Sequence Databases
Sl. no. Accession(s) Access Link(s)
1. Z71389 GenBank || EMBL
2. AF040153 GenBank || EMBL
3. AF071216 GenBank || EMBL
4. AJ000152 GenBank || EMBL
5. BC069285 GenBank || EMBL
6. BC093983 GenBank || EMBL
7. BC093985 GenBank || EMBL
5.5 Protein-Protein Interaction Databases
IntAct: O15263
MINT: Not found
DIP: Not found
BioGRID: 108037
5.6 Ligand Databases
BindingDB: Not found
DrugBank: Not found
ChEMBL: Not found
5.7 Family & Domain Databases
InterPro: IPR006080, IPR001855
PANTHER: Not found
PROSITE: Not found
5.8 Genome Annotation Databases
5.9 Phylogenomic Databases
5.10 Enzyme & Pathway Databases
BRENDA: Not found
BioCyc: Not found
5.11 Protein-RNA Interaction Databases
RNAct: O15263




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