AMPDB_264 | Potassium channel toxin kappa-KTx 1.2

1 General Description

AMPDB ID: AMPDB_264

Protein Names: Potassium channel toxin kappa-KTx 1.2 (Kappa-hefutoxin 2) (Kappa-HfTx2) [Cleaved into: Potassium channel toxin kappa-KTx 1.1 (Kappa-hefutoxin 1) (Kappa-HfTx1)]

Protein Family: Short scorpion toxin superfamily; Potassium channel inhibitor kappa-KTx family; Kappa-KTx 1 subfamily

Gene Name: Nil

Source Organism: Chersonesometrus fulvipes (Indian black scorpion) (Heterometrus fulvipes)

Protein Length: 23 AA

Protein Existence: Evidence at protein level

2 Protein Sequence & Composition

GHACYRNCWREGNDEETCKERCG

FASTA format

Counts of Amino Acids

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

Frequencies of Amino Acids

'A': 4.35%, 'R': 13.04%, 'N': 8.7%, 'D': 4.35%, 'C': 17.39%, 'Q': 0%, 'E': 17.39%, 'G': 13.04%, 'H': 4.35%, 'I': 0%, 'L': 0%, 'K': 4.35%, 'M': 0%, 'F': 0%, 'P': 0%, 'S': 0%, 'T': 4.35%, 'W': 4.35%, 'Y': 4.35%, 'V': 0%

Missing Amino Acid(s)

F, I, L, M, P, Q, S, V

Most Occurring Amino Acid(s)

C, E

Less Occurring Amino Acid(s)

A, D, H, K, T, W, Y

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	2716.94 Da	Computed by ProtParam module (biopython 1.79)
2.	Aliphatic Index	4.348	Computed by ProtParam module (biopython 1.79)
3.	Instability Index (Half Life)	46.209	Computed by ProtParam module (biopython 1.79)
4.	Hydrophobicity (GRAVY)	-1.626	Computed by ProtParam module (biopython 1.79)
5.	Hydrophobic Moment	0.639	Computed by ProtParam module (biopython 1.79)
6.	Isoelectric Point	5.659	Computed by ProtParam module (biopython 1.79)
7.	Charge (at pH 7)	-1.153	Computed by ProtParam module (biopython 1.79)
8.	Secondary Structure Fraction	0.087, 0.217, 0.217 [Helix, Turn, Sheet]	Computed by ProtParam module (biopython 1.79)
9.	Aromaticity	0.087	Computed by ProtParam module (biopython 1.79)
10.	Molar Extinction Coefficient (cysteine\|cystine)	6990, 7240	Computed by ProtParam module (biopython 1.79)

4.1 Target Organism(s)

4.2 Antimicrobial Activity

Antimicrobial, Fungicide

4.3 Enzymatic Activity

4.4 Inhibitory Effect

4.5 Other Biological Activity

Toxin, Non-hemolytic, Non-ribosomal

Activity data manually curated from Literature and UniProt

5 Database Cross-references

5.1 Literature Database

Citation 1: Srinivasan KN, Sivaraja V, Huys I, et al. kappa-Hefutoxin1, a novel toxin from the scorpion Heterometrus fulvipes with unique structure and function. Importance of the functional diad in potassium channel selectivity. J Biol Chem. 2002;277(33):30040-7. Published 2002 Aug 16. doi:10.1074/jbc.M111258200

PMID: 12034709

Citation 2: Peigneur S, Yamaguchi Y, Goto H, et al. Synthesis and characterization of amino acid deletion analogs of Îº-hefutoxin 1, a scorpion toxin on potassium channels. Toxicon. 2013;71:25-30. Published 2013 Sep. doi:10.1016/j.toxicon.2013.05.010

PMID: 23726856

Citation 3: Moreels L, Peigneur S, Yamaguchi Y, et al. Expanding the pharmacological profile of Îº-hefutoxin 1 and analogues: A focus on the inhibitory effect on the oncogenic channel K(v)10.1. Peptides. 2017;98:43-50. Published 2017 Dec. doi:10.1016/j.peptides.2016.08.008

PMID: 27578329

Citation 4: Nirthanan S, Pil J, Abdel-Mottaleb Y, et al. Assignment of voltage-gated potassium channel blocking activity to kappa-KTx1.3, a non-toxic homologue of kappa-hefutoxin-1, from Heterometrus spinifer venom. Biochem Pharmacol. 2005;69(4):669-78. Published 2005 Feb 15. doi:10.1016/j.bcp.2004.10.018

PMID: 15670585

Citation 5: Correnti CE, Gewe MM, Mehlin C, et al. Screening, large-scale production and structure-based classification of cystine-dense peptides. Nat Struct Mol Biol. 2018;25(3):270-278. Published 2018 Mar. doi:10.1038/s41594-018-0033-9

PMID: 29483648

5.2 Protein Sequence Databases

5.3 3D Structure Databases

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

AlphaFoldDB: P82851

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: IPR012630

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