AMPDB_124 | Anoplin

1 General Description

AMPDB ID: AMPDB_124

Protein Names: Anoplin (ANP) (As-183)

Protein Family: Nil

Gene Name: Nil

Source Organism: Anoplius samariensis (Solitary wasp)

Protein Length: 10 AA

Protein Existence: Evidence at protein level

2 Protein Sequence & Composition

GLLKRIKTLL

FASTA format

Counts of Amino Acids

'A': 0, 'R': 1, 'N': 0, 'D': 0, 'C': 0, 'Q': 0, 'E': 0, 'G': 1, 'H': 0, 'I': 1, 'L': 4, 'K': 2, 'M': 0, 'F': 0, 'P': 0, 'S': 0, 'T': 1, 'W': 0, 'Y': 0, 'V': 0

Frequencies of Amino Acids

'A': 0%, 'R': 10%, 'N': 0%, 'D': 0%, 'C': 0%, 'Q': 0%, 'E': 0%, 'G': 10%, 'H': 0%, 'I': 10%, 'L': 40%, 'K': 20%, 'M': 0%, 'F': 0%, 'P': 0%, 'S': 0%, 'T': 10%, 'W': 0%, 'Y': 0%, 'V': 0%

Missing Amino Acid(s)

A, C, D, E, F, H, M, N, P, Q, S, V, W, Y

Most Occurring Amino Acid(s)

Less Occurring Amino Acid(s)

G, I, R, T

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	1154.5 Da	Computed by ProtParam module (biopython 1.79)
2.	Aliphatic Index	195	Computed by ProtParam module (biopython 1.79)
3.	Instability Index (Half Life)	24.62	Computed by ProtParam module (biopython 1.79)
4.	Hydrophobicity (GRAVY)	0.63	Computed by ProtParam module (biopython 1.79)
5.	Hydrophobic Moment	0.586	Computed by ProtParam module (biopython 1.79)
6.	Isoelectric Point	11.823	Computed by ProtParam module (biopython 1.79)
7.	Charge (at pH 7)	2.997	Computed by ProtParam module (biopython 1.79)
8.	Secondary Structure Fraction	0.5, 0.1, 0.4 [Helix, Turn, Sheet]	Computed by ProtParam module (biopython 1.79)
9.	Aromaticity	0	Computed by ProtParam module (biopython 1.79)
10.	Molar Extinction Coefficient (cysteine\|cystine)	0, 0	Computed by ProtParam module (biopython 1.79)

4.1 Target Organism(s)

Gram Negative Bacteria and Gram Positive Bacteria

4.2 Antimicrobial Activity

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

4.3 Enzymatic Activity

4.4 Inhibitory Effect

4.5 Other Biological Activity

Hemolytic, Non-ribosomal

Activity data manually curated from Literature and UniProt

5 Database Cross-references

5.1 Literature Database

Citation 1: Hisada M, Konno K, Itagaki Y, et al. Advantages of using nested collision induced dissociation/post-source decay with matrix-assisted laser desorption/ionization time-of-flight mass spectrometry: sequencing of novel peptides from wasp venom. Rapid Commun Mass Spectrom. 2000;14(19):1828-34. Published 2000. doi:10.1002/1097-0231(20001015)14:19<1828::AID-RCM101>3.0.CO;2-G

PMID: 11006592

Citation 2: Konno K, Hisada M, Fontana R, et al. Anoplin, a novel antimicrobial peptide from the venom of the solitary wasp Anoplius samariensis. Biochim Biophys Acta. 2001;1550(1):70-80. Published 2001 Nov 26. doi:10.1016/s0167-4838(01)00271-0

PMID: 11738089

Citation 3: Ifrah D, Doisy X, Ryge TS, et al. Structure-activity relationship study of anoplin. J Pept Sci. 2005;11(2):113-21. Published 2005 Feb. doi:10.1002/psc.598

PMID: 15635634

Citation 4: Dos Santos Cabrera MP, Arcisio-Miranda M, Broggio Costa ST, et al. Study of the mechanism of action of anoplin, a helical antimicrobial decapeptide with ion channel-like activity, and the role of the amidated C-terminus. J Pept Sci. 2008;14(6):661-9. Published 2008 Jun. doi:10.1002/psc.960

PMID: 17994639

Citation 5: JindÅichovÃ¡ B, BurketovÃ¡ L, NovotnÃ¡ Z, et al. Novel properties of antimicrobial peptide anoplin. Biochem Biophys Res Commun. 2014;444(4):520-4. Published 2014 Feb 21. doi:10.1016/j.bbrc.2014.01.097

PMID: 24472551

Citation 6: Konno K, Kazuma K, Nihei K, et al. Peptide Toxins in Solitary Wasp Venoms. Toxins (Basel). 2016;8(4):114. Published 2016 Apr 18. doi:10.3390/toxins8040114

PMID: 27096870

Citation 7: UggerhÃ¸j LE, Poulsen TJ, Munk JK, et al. Rational design of alpha-helical antimicrobial peptides: do's and don'ts. Chembiochem. 2015;16(2):242-53. Published 2015 Jan 19. doi:10.1002/cbic.201402581

PMID: 25530580

5.2 Protein Sequence Databases

5.3 3D Structure Databases

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

AlphaFoldDB: P0C005

5.4 Nucleotide Sequence Databases

No entries found in GenBank or 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: Not found

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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