AMPDB_197 | Dermaseptin-B2

1 General Description

AMPDB ID: AMPDB_197

Protein Names: Dermaseptin-B2 (DRS-B2) (Adenoregulin) (Dermaseptin BII)

Protein Family: Frog skin active peptide (FSAP) family; Dermaseptin subfamily

Gene Name: ADR

Source Organism: Phyllomedusa bicolor (Two-colored leaf frog) (Rana bicolor)

Protein Length: 81 AA

Protein Existence: Evidence at protein level

2 Protein Sequence & Composition

MAFLKKSLFLVLFLGLVSLSICEEEKRENEDEEEQEDDEQSEMKRGLWSKIKEVGKEAAKAAAKAAGKAALGAVSEAVGEQ

FASTA format

Counts of Amino Acids

'A': 12, 'R': 2, 'N': 1, 'D': 3, 'C': 1, 'Q': 3, 'E': 15, 'G': 6, 'H': 0, 'I': 2, 'L': 9, 'K': 10, 'M': 2, 'F': 3, 'P': 0, 'S': 6, 'T': 0, 'W': 1, 'Y': 0, 'V': 5

Frequencies of Amino Acids

'A': 14.81%, 'R': 2.47%, 'N': 1.23%, 'D': 3.7%, 'C': 1.23%, 'Q': 3.7%, 'E': 18.52%, 'G': 7.41%, 'H': 0%, 'I': 2.47%, 'L': 11.11%, 'K': 12.35%, 'M': 2.47%, 'F': 3.7%, 'P': 0%, 'S': 7.41%, 'T': 0%, 'W': 1.23%, 'Y': 0%, 'V': 6.17%

Missing Amino Acid(s)

H, P, T, Y

Most Occurring Amino Acid(s)

Less Occurring Amino Acid(s)

C, N, W

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	8844.04 Da	Computed by ProtParam module (biopython 1.79)
2.	Aliphatic Index	85.679	Computed by ProtParam module (biopython 1.79)
3.	Instability Index (Half Life)	52.554	Computed by ProtParam module (biopython 1.79)
4.	Hydrophobicity (GRAVY)	-0.402	Computed by ProtParam module (biopython 1.79)
5.	Hydrophobic Moment	0.678	Computed by ProtParam module (biopython 1.79)
6.	Isoelectric Point	4.385	Computed by ProtParam module (biopython 1.79)
7.	Charge (at pH 7)	-6.039	Computed by ProtParam module (biopython 1.79)
8.	Secondary Structure Fraction	0.247, 0.16, 0.469 [Helix, Turn, Sheet]	Computed by ProtParam module (biopython 1.79)
9.	Aromaticity	0.049	Computed by ProtParam module (biopython 1.79)
10.	Molar Extinction Coefficient (cysteine\|cystine)	5500, 5500	Computed by ProtParam module (biopython 1.79)

4.1 Target Organism(s)

Gram Negative Bacteria and Gram Positive Bacteria

4.2 Antimicrobial Activity

Amphibian defense peptide, Antibiotic, Antimicrobial, Fungicide, Anti-protozoal, Anti-gram-negative, Anti-gram-Positive

4.3 Enzymatic Activity

4.4 Inhibitory Effect

4.5 Other Biological Activity

Cytotoxin, Hemolytic, Synergistic peptide, Non-ribosomal

Activity data manually curated from Literature and UniProt

5 Database Cross-references

5.1 Literature Database

Citation 1: Amiche M, Ducancel F, Lajeunesse E, et al. Molecular cloning of a cDNA encoding the precursor of adenoregulin from frog skin. Relationships with the vertebrate defensive peptides, dermaseptins. Biochem Biophys Res Commun. 1993;191(3):983-90. Published 1993 Mar 31. doi:10.1006/bbrc.1993.1314

PMID: 8466537

Citation 2: Daly JW, Caceres J, Moni RW, et al. Frog secretions and hunting magic in the upper Amazon: identification of a peptide that interacts with an adenosine receptor. Proc Natl Acad Sci U S A. 1992;89(22):10960-3. Published 1992 Nov 15. doi:10.1073/pnas.89.22.10960

PMID: 1438301

Citation 3: Shin Y, Moni RW, Lueders JE, et al. Effects of the amphiphilic peptides mastoparan and adenoregulin on receptor binding, G proteins, phosphoinositide breakdown, cyclic AMP generation, and calcium influx. Cell Mol Neurobiol. 1994;14(2):133-57. Published 1994 Apr. doi:10.1007/BF02090781

PMID: 7842473

Citation 4: Mor A, Nicolas P, Nicolas P. Isolation and structure of novel defensive peptides from frog skin. Eur J Biochem. 1994;219(1-2):145-54. Published 1994 Jan 15. doi:10.1111/j.1432-1033.1994.tb19924.x

PMID: 8306981

Citation 5: Moni RW, Romero FS, Daly JW, et al. The amphiphilic peptide adenoregulin enhances agonist binding to A1-adenosine receptors and [35S]GTP gamma S to brain membranes. Cell Mol Neurobiol. 1995;15(4):465-93. Published 1995 Aug. doi:10.1007/BF02071881

PMID: 8565049

Citation 6: Vanhoye D, Bruston F, Nicolas P, et al. Antimicrobial peptides from hylid and ranin frogs originated from a 150-million-year-old ancestral precursor with a conserved signal peptide but a hypermutable antimicrobial domain. Eur J Biochem. 2003;270(9):2068-81. Published 2003 May. doi:10.1046/j.1432-1033.2003.03584.x

PMID: 12709067

Citation 7: Cao W, Zhou Y, Ma Y, et al. Expression and purification of antimicrobial peptide adenoregulin with C-amidated terminus in Escherichia coli. Protein Expr Purif. 2005;40(2):404-10. Published 2005 Apr. doi:10.1016/j.pep.2004.12.007

PMID: 15766883

Citation 8: Lequin O, Ladram A, Chabbert L, et al. Dermaseptin S9, an alpha-helical antimicrobial peptide with a hydrophobic core and cationic termini. Biochemistry. 2006;45(2):468-80. Published 2006 Jan 17. doi:10.1021/bi051711i

PMID: 16401077

Citation 9: Auvynet C, El Amri C, Lacombe C, et al. Structural requirements for antimicrobial versus chemoattractant activities for dermaseptin S9. FEBS J. 2008;275(16):4134-51. Published 2008 Aug. doi:10.1111/j.1742-4658.2008.06554.x

PMID: 18637027

Citation 10: Amiche M, Ladram A, Nicolas P, et al. A consistent nomenclature of antimicrobial peptides isolated from frogs of the subfamily Phyllomedusinae. Peptides. 2008;29(11):2074-82. Published 2008 Nov. doi:10.1016/j.peptides.2008.06.017

PMID: 18644413

Citation 11: Galanth C, Abbassi F, Lequin O, et al. Mechanism of antibacterial action of dermaseptin B2: interplay between helix-hinge-helix structure and membrane curvature strain. Biochemistry. 2009;48(2):313-27. Published 2009 Jan 20. doi:10.1021/bi802025a

PMID: 19113844

5.2 Protein Sequence Databases

5.3 3D Structure Databases

AlphaFoldDB: P31107

5.4 Nucleotide Sequence Databases

Sl. no.	Accession(s)	Access Link(s)
1.	X70278	GenBank \|\| EMBL

RefSeq: Not found

5.5 Protein-Protein Interaction Databases

STRING: Not found

IntAct: Not found

BioGRID: Not found

5.6 Ligand Databases

BindingDB: Not found

DrugBank: Not found

ChEMBL: Not found

5.7 Family & Domain Databases

InterPro: IPR022731, IPR004275

PANTHER: Not found

PROSITE: Not found

5.8 Genome Annotation Databases

Ensembl: Not found

5.9 Phylogenomic Databases

GeneTree: Not found

5.10 Enzyme & Pathway Databases

BRENDA: Not found

BioCyc: Not found

5.11 Protein-RNA Interaction Databases

RNAct: Not found

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