AMPDB_194 | Kappa-stichotoxin-She3a

AMPDB_194 | Kappa-stichotoxin-She3a

PEPTIDE SUMMARY

Kappa-stichotoxin-She3a

1 General Description

AMPDB ID: AMPDB_194

Protein Names: Kappa-stichotoxin-She3a (Kappa-SHTX-She3a) (Potassium channel toxin ShK)

Protein Family: Sea anemone type 1 potassium channel toxin family; Type 1a subfamily

Gene Name: Nil

Source Organism: Stichodactyla helianthus (Sun anemone) (Stoichactis helianthus)

Protein Length: 35 AA

Protein Existence: Evidence at protein level

2 Protein Sequence & Composition

2.1 Sequence

RSCIDTIPKSRCTAFQCKHSMKYRLSFCRKTCGTC

2.2 Composition

Counts of Amino Acids

'A': 1, 'R': 4, 'N': 0, 'D': 1, 'C': 6, 'Q': 1, 'E': 0, 'G': 1, 'H': 1, 'I': 2, 'L': 1, 'K': 4, 'M': 1, 'F': 2, 'P': 1, 'S': 4, 'T': 4, 'W': 0, 'Y': 1, 'V': 0

Frequencies of Amino Acids

'A': 2.86%, 'R': 11.43%, 'N': 0%, 'D': 2.86%, 'C': 17.14%, 'Q': 2.86%, 'E': 0%, 'G': 2.86%, 'H': 2.86%, 'I': 5.71%, 'L': 2.86%, 'K': 11.43%, 'M': 2.86%, 'F': 5.71%, 'P': 2.86%, 'S': 11.43%, 'T': 11.43%, 'W': 0%, 'Y': 2.86%, 'V': 0%

Missing Amino Acid(s)

E, N, V, W

Most Occurring Amino Acid(s)

C

Less Occurring Amino Acid(s)

A, D, G, H, L, M, P, Q, Y

Hydrophobic Amino Acid(s) Count

9

Hydrophilic Amino Acid(s) Count

26

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	4060.84 Da	Computed by ProtParam module (biopython 1.79)
2.	Aliphatic Index	36.286	Computed by ProtParam module (biopython 1.79)
3.	Instability Index (Half Life)	31.871	Computed by ProtParam module (biopython 1.79)
4.	Hydrophobicity (GRAVY)	-0.457	Computed by ProtParam module (biopython 1.79)
5.	Hydrophobic Moment	0.406	Computed by ProtParam module (biopython 1.79)
6.	Isoelectric Point	9.624	Computed by ProtParam module (biopython 1.79)
7.	Charge (at pH 7)	6.715	Computed by ProtParam module (biopython 1.79)
8.	Secondary Structure Fraction	0.171, 0.171, 0.086 [Helix, Turn, Sheet]	Computed by ProtParam module (biopython 1.79)
9.	Aromaticity	0.086	Computed by ProtParam module (biopython 1.79)
10.	Molar Extinction Coefficient (cysteine\|cystine)	1490, 1865	Computed by ProtParam module (biopython 1.79)

4 Activity Details

4.1 Target Organism(s)

B.subtilis (Gram-positive), P.aeruginosa (Gram-negative), S.aureus (Gram-positive), S.typhimurium

4.2 Antimicrobial Activity

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

4.3 Enzymatic Activity

Not found

4.4 Inhibitory Effect

Not found

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

5.1.1 PubMed

Citation 1: CastaÃ±eda O, Sotolongo V, Amor AM, et al. Characterization of a potassium channel toxin from the Caribbean Sea anemone Stichodactyla helianthus. Toxicon. 1995;33(5):603-13. Published 1995 May. doi:10.1016/0041-0101(95)00013-c

PMID: 7660365

Citation 2: Pennington MW, Byrnes ME, Zaydenberg I, et al. Chemical synthesis and characterization of ShK toxin: a potent potassium channel inhibitor from a sea anemone. Int J Pept Protein Res. 1995;46(5):354-8. Published 1995 Nov. doi:10.1111/j.1399-3011.1995.tb01068.x

PMID: 8567178

Citation 3: Pennington MW, Mahnir VM, Krafte DS, et al. Identification of three separate binding sites on SHK toxin, a potent inhibitor of voltage-dependent potassium channels in human T-lymphocytes and rat brain. Biochem Biophys Res Commun. 1996;219(3):696-701. Published 1996 Feb 27. doi:10.1006/bbrc.1996.0297

PMID: 8645244

Citation 4: Rauer H, Pennington M, Cahalan M, et al. Structural conservation of the pores of calcium-activated and voltage-gated potassium channels determined by a sea anemone toxin. J Biol Chem. 1999;274(31):21885-92. Published 1999 Jul 30. doi:10.1074/jbc.274.31.21885

PMID: 10419508

Citation 5: Beeton C, Pennington MW, Wulff H, et al. Targeting effector memory T cells with a selective peptide inhibitor of Kv1.3 channels for therapy of autoimmune diseases. Mol Pharmacol. 2005;67(4):1369-81. Published 2005 Apr. doi:10.1124/mol.104.008193

PMID: 15665253

Citation 6: Oliveira JS, Fuentes-Silva D, King GF, et al. Development of a rational nomenclature for naming peptide and protein toxins from sea anemones. Toxicon. 2012;60(4):539-50. Published 2012 Sep 15. doi:10.1016/j.toxicon.2012.05.020

PMID: 22683676

Citation 7: Kim CH, Lee YJ, Go HJ, et al. Defensin-neurotoxin dyad in a basally branching metazoan sea anemone. FEBS J. 2017;284(19):3320-3338. Published 2017 Oct. doi:10.1111/febs.14194

PMID: 28796463

Citation 8: Chi V, Pennington MW, Norton RS, et al. Development of a sea anemone toxin as an immunomodulator for therapy of autoimmune diseases. Toxicon. 2012;59(4):529-46. Published 2012 Mar 15. doi:10.1016/j.toxicon.2011.07.016

PMID: 21867724

Citation 9: Prentis PJ, Pavasovic A, Norton RS, et al. Sea Anemones: Quiet Achievers in the Field of Peptide Toxins. Toxins (Basel). 2018;10(1). Published 2018 Jan 8. doi:10.3390/toxins10010036

PMID: 29316700

Citation 10: Tudor JE, Pallaghy PK, Pennington MW, et al. Solution structure of ShK toxin, a novel potassium channel inhibitor from a sea anemone. Nat Struct Biol. 1996;3(4):317-20. Published 1996 Apr. doi:10.1038/nsb0496-317

PMID: 8599755

Citation 11: Kalman K, Pennington MW, Lanigan MD, et al. ShK-Dap22, a potent Kv1.3-specific immunosuppressive polypeptide. J Biol Chem. 1998;273(49):32697-707. Published 1998 Dec 4. doi:10.1074/jbc.273.49.32697

PMID: 9830012

Citation 12: Pennington MW, Lanigan MD, Kalman K, et al. Role of disulfide bonds in the structure and potassium channel blocking activity of ShK toxin. Biochemistry. 1999;38(44):14549-58. Published 1999 Nov 2. doi:10.1021/bi991282m

PMID: 10545177

Citation 13: Pennington MW, Beeton C, Galea CA, et al. Engineering a stable and selective peptide blocker of the Kv1.3 channel in T lymphocytes. Mol Pharmacol. 2009;75(4):762-73. Published 2009 Apr. doi:10.1124/mol.108.052704

PMID: 19122005

Citation 14: Dang B, Kubota T, Mandal K, et al. Native chemical ligation at Asx-Cys, Glx-Cys: chemical synthesis and high-resolution X-ray structure of ShK toxin by racemic protein crystallography. J Am Chem Soc. 2013;135(32):11911-9. Published 2013 Aug 14. doi:10.1021/ja4046795

PMID: 23919482

Citation 15: Murray JK, Qian YX, Liu B, et al. Pharmaceutical Optimization of Peptide Toxins for Ion Channel Targets: Potent, Selective, and Long-Lived Antagonists of Kv1.3. J Med Chem. 2015;58(17):6784-802. Published 2015 Sep 10. doi:10.1021/acs.jmedchem.5b00495

PMID: 26288216

Citation 16: Dang B, Shen R, Kubota T, et al. Inversion of the Side-Chain Stereochemistry of Indvidual Thr or Ile Residues in a Protein Molecule: Impact on the Folding, Stability, and Structure of the ShK Toxin. Angew Chem Int Ed Engl. 2017;56(12):3324-3328. Published 2017 Mar 13. doi:10.1002/anie.201612398

PMID: 28194851

5.2 Protein Sequence Databases

UniProt: P29187

5.3 3D Structure Databases

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

AlphaFoldDB: P29187

5.4 Nucleotide Sequence Databases

No entries found in GenBank or EMBL

CCDS: Not found

RefSeq: Not found

5.5 Protein-Protein Interaction Databases

STRING: Not found

IntAct: Not found

MINT: Not found

DIP: Not found

BioGRID: Not found

5.6 Ligand Databases

BindingDB: Not found

DrugBank: Not found

ChEMBL: Not found

5.7 Family & Domain Databases

InterPro: IPR003582

PANTHER: Not found

PROSITE: PS51670

5.8 Genome Annotation Databases

Ensembl: Not found

KEGG: 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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