AMPDB_4057 | Pandinin-2

1 General Description

AMPDB ID: AMPDB_4057

Protein Names: Pandinin-2 (Pin2) (Non-disulfide-bridged peptide 3.1) (NDBP-3.1) (Non-disulfide-bridged peptide 4.1) (NDBP-4.1)

Protein Family: Non-disulfide-bridged peptide (NDBP) superfamily; Medium-length antimicrobial peptide (group 3) family

Gene Name: Nil

Source Organism: Pandinus imperator (Emperor scorpion)

Protein Length: 24 AA

Protein Existence: Evidence at protein level

2 Protein Sequence & Composition

FWGALAKGALKLIPSLFSSFSKKD

FASTA format

Counts of Amino Acids

'A': 3, 'R': 0, 'N': 0, 'D': 1, 'C': 0, 'Q': 0, 'E': 0, 'G': 2, 'H': 0, 'I': 1, 'L': 4, 'K': 4, 'M': 0, 'F': 3, 'P': 1, 'S': 4, 'T': 0, 'W': 1, 'Y': 0, 'V': 0

Frequencies of Amino Acids

'A': 12.5%, 'R': 0%, 'N': 0%, 'D': 4.17%, 'C': 0%, 'Q': 0%, 'E': 0%, 'G': 8.33%, 'H': 0%, 'I': 4.17%, 'L': 16.67%, 'K': 16.67%, 'M': 0%, 'F': 12.5%, 'P': 4.17%, 'S': 16.67%, 'T': 0%, 'W': 4.17%, 'Y': 0%, 'V': 0%

Missing Amino Acid(s)

C, E, H, M, N, Q, R, T, V, Y

Most Occurring Amino Acid(s)

K, L, S

Less Occurring Amino Acid(s)

D, I, P, 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	2612.11 Da	Computed by ProtParam module (biopython 1.79)
2.	Aliphatic Index	93.75	Computed by ProtParam module (biopython 1.79)
3.	Instability Index (Half Life)	2.425	Computed by ProtParam module (biopython 1.79)
4.	Hydrophobicity (GRAVY)	0.329	Computed by ProtParam module (biopython 1.79)
5.	Hydrophobic Moment	0.561	Computed by ProtParam module (biopython 1.79)
6.	Isoelectric Point	10.803	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	0.375, 0.292, 0.292 [Helix, Turn, Sheet]	Computed by ProtParam module (biopython 1.79)
9.	Aromaticity	0.167	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)

B.subtilis (Gram-positive), C.albicans, E.coli (Gram-negative), E.faecalis (Gram-positive), P.aeruginosa (Gram-negative), S.epidermidis (Gram-positive)

4.2 Antimicrobial Activity

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

4.3 Enzymatic Activity

4.4 Inhibitory Effect

4.5 Other Biological Activity

Cytolysis, Hemolytic, Non-ribosomal

Activity data manually curated from Literature and UniProt

5 Database Cross-references

5.1 Literature Database

Citation 1: Corzo G, Escoubas P, Villegas E, et al. Characterization of unique amphipathic antimicrobial peptides from venom of the scorpion Pandinus imperator. Biochem J. 2001;359(Pt 1):35-45. Published 2001 Oct 1. doi:10.1042/0264-6021:3590035

PMID: 11563967

Citation 2: Belokoneva OS, Satake H, Mal'tseva EL, et al. Pore formation of phospholipid membranes by the action of two hemolytic arachnid peptides of different size. Biochim Biophys Acta. 2004;1664(2):182-8. Published 2004 Aug 30. doi:10.1016/j.bbamem.2004.05.007

PMID: 15328050

Citation 3: Garcia F, Villegas E, Espino-Solis GP, et al. Antimicrobial peptides from arachnid venoms and their microbicidal activity in the presence of commercial antibiotics. J Antibiot (Tokyo). 2013;66(1):3-10. Published 2013 Jan. doi:10.1038/ja.2012.87

PMID: 23093034

Citation 4: Zeng XC, Corzo G, Hahin R, et al. Scorpion venom peptides without disulfide bridges. IUBMB Life. 2005;57(1):13-21. Published 2005 Jan. doi:10.1080/15216540500058899

PMID: 16036557

Citation 5: Almaaytah A, Albalas Q, Albalas Q. Scorpion venom peptides with no disulfide bridges: a review. Peptides. 2014;51:35-45. Published 2014 Jan. doi:10.1016/j.peptides.2013.10.021

PMID: 24184590

Citation 6: Nomura K, Corzo G, Nakajima T, et al. Orientation and pore-forming mechanism of a scorpion pore-forming peptide bound to magnetically oriented lipid bilayers. Biophys J. 2004;87(4):2497-507. Published 2004 Oct. doi:10.1529/biophysj.104.043513

PMID: 15298871

5.2 Protein Sequence Databases

5.3 3D Structure Databases

AlphaFoldDB: P83240

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: IPR012523

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

Download