AMPDB_357 | M-theraphotoxin-Gr1a

1 General Description

AMPDB ID: AMPDB_357

Protein Names: M-theraphotoxin-Gr1a (M-TRTX-Gr1a) (GsMTx-4) (GsMTx4) (MTx4) (GsMTx-IV)

Protein Family: Neurotoxin 10 (Hwtx-1) family; 52 (MTx4) subfamily

Gene Name: Nil

Source Organism: Grammostola rosea (Chilean rose tarantula) (Grammostola spatulata)

Protein Length: 82 AA

Protein Existence: Evidence at protein level

2 Protein Sequence & Composition

MKTSVVFVIAGLALLSVVCYASELKEQSSVNEVLSTIFHFEQPEERGCLEFWWKCNPNDDKCCRPKLKCSKLFKLCNFSFGK

FASTA format

Counts of Amino Acids

'A': 3, 'R': 2, 'N': 4, 'D': 2, 'C': 7, 'Q': 2, 'E': 7, 'G': 3, 'H': 1, 'I': 2, 'L': 9, 'K': 9, 'M': 1, 'F': 7, 'P': 3, 'S': 8, 'T': 2, 'W': 2, 'Y': 1, 'V': 7

Frequencies of Amino Acids

'A': 3.66%, 'R': 2.44%, 'N': 4.88%, 'D': 2.44%, 'C': 8.54%, 'Q': 2.44%, 'E': 8.54%, 'G': 3.66%, 'H': 1.22%, 'I': 2.44%, 'L': 10.98%, 'K': 10.98%, 'M': 1.22%, 'F': 8.54%, 'P': 3.66%, 'S': 9.76%, 'T': 2.44%, 'W': 2.44%, 'Y': 1.22%, 'V': 8.54%

Missing Amino Acid(s)

No Amino Acid(s) are missing in this protein

Most Occurring Amino Acid(s)

K, L

Less Occurring Amino Acid(s)

H, M, 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	9400.02 Da	Computed by ProtParam module (biopython 1.79)
2.	Aliphatic Index	80.732	Computed by ProtParam module (biopython 1.79)
3.	Instability Index (Half Life)	27.096	Computed by ProtParam module (biopython 1.79)
4.	Hydrophobicity (GRAVY)	0.004	Computed by ProtParam module (biopython 1.79)
5.	Hydrophobic Moment	0.517	Computed by ProtParam module (biopython 1.79)
6.	Isoelectric Point	8.036	Computed by ProtParam module (biopython 1.79)
7.	Charge (at pH 7)	1.665	Computed by ProtParam module (biopython 1.79)
8.	Secondary Structure Fraction	0.341, 0.22, 0.244 [Helix, Turn, Sheet]	Computed by ProtParam module (biopython 1.79)
9.	Aromaticity	0.122	Computed by ProtParam module (biopython 1.79)
10.	Molar Extinction Coefficient (cysteine\|cystine)	12490, 12865	Computed by ProtParam module (biopython 1.79)

4.1 Target Organism(s)

Aeropyrum pernix, B.subtilis (Gram-positive), E.coli (Gram-negative), P.aeruginosa (Gram-negative), S.aureus (Gram-positive), S.epidermidis (Gram-positive), S.typhimurium

4.2 Antimicrobial Activity

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

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: Ostrow KL, Mammoser A, Suchyna T, et al. cDNA sequence and in vitro folding of GsMTx4, a specific peptide inhibitor of mechanosensitive channels. Toxicon. 2003;42(3):263-74. Published 2003 Sep. doi:10.1016/s0041-0101(03)00141-7

PMID: 14559077

Citation 2: Ono S, Kimura T, Kubo T, et al. Characterization of voltage-dependent calcium channel blocking peptides from the venom of the tarantula Grammostola rosea. Toxicon. 2011;58(3):265-76. Published 2011 Sep 1. doi:10.1016/j.toxicon.2011.06.006

PMID: 21740921

Citation 3: Suchyna TM, Johnson JH, Hamer K, et al. Identification of a peptide toxin from Grammostola spatulata spider venom that blocks cation-selective stretch-activated channels. J Gen Physiol. 2000;115(5):583-98. Published 2000 May. doi:10.1085/jgp.115.5.583

PMID: 10779316

Citation 4: Oswald RE, Suchyna TM, McFeeters R, et al. Solution structure of peptide toxins that block mechanosensitive ion channels. J Biol Chem. 2002;277(37):34443-50. Published 2002 Sep 13. doi:10.1074/jbc.M202715200

PMID: 12082099

Citation 5: Redaelli E, Cassulini RR, Silva DF, et al. Target promiscuity and heterogeneous effects of tarantula venom peptides affecting Na+ and K+ ion channels. J Biol Chem. 2010;285(6):4130-4142. Published 2010 Feb 5. doi:10.1074/jbc.M109.054718

PMID: 19955179

Citation 6: Bode F, Sachs F, Franz MR, et al. Tarantula peptide inhibits atrial fibrillation. Nature. 2001;409(6816):35-6. Published 2001 Jan 4. doi:10.1038/35051165

PMID: 11343101

Citation 7: Ruta V, MacKinnon R, MacKinnon R. Localization of the voltage-sensor toxin receptor on KvAP. Biochemistry. 2004;43(31):10071-9. Published 2004 Aug 10. doi:10.1021/bi049463y

PMID: 15287735

Citation 8: Suchyna TM, Tape SE, Koeppe RE 2nd, et al. Bilayer-dependent inhibition of mechanosensitive channels by neuroactive peptide enantiomers. Nature. 2004;430(6996):235-40. Published 2004 Jul 8. doi:10.1038/nature02743

PMID: 15241420

Citation 9: Jung HJ, Kim PI, Lee SK, et al. Lipid membrane interaction and antimicrobial activity of GsMTx-4, an inhibitor of mechanosensitive channel. Biochem Biophys Res Commun. 2006;340(2):633-8. Published 2006 Feb 10. doi:10.1016/j.bbrc.2005.12.046

PMID: 16376854

Citation 10: Fang J, Iwasa KH, Iwasa KH. Effects of tarantula toxin GsMTx4 on the membrane motor of outer hair cells. Neurosci Lett. 2006;404(1-2):213-6. Published 2006 Aug 14. doi:10.1016/j.neulet.2006.05.059

PMID: 16797839

Citation 11: Nishizawa M, Nishizawa K, Nishizawa K. Molecular dynamics simulations of a stretch-activated channel inhibitor GsMTx4 with lipid membranes: two binding modes and effects of lipid structure. Biophys J. 2007;92(12):4233-43. Published 2007 Jun 15. doi:10.1529/biophysj.106.101071

PMID: 17384064

Citation 12: Posokhov YO, Gottlieb PA, Morales MJ, et al. Is lipid bilayer binding a common property of inhibitor cysteine knot ion-channel blockers? Biophys J. 2007;93(4):L20-2. Published 2007 Aug 15. doi:10.1529/biophysj.107.112375

PMID: 17573432

Citation 13: Agwa AJ, Peigneur S, Chow CY, et al. Gating modifier toxins isolated from spider venom: Modulation of voltage-gated sodium channels and the role of lipid membranes. J Biol Chem. 2018;293(23):9041-9052. Published 2018 Jun 8. doi:10.1074/jbc.RA118.002553

PMID: 29703751

Citation 14: Pan NC, Zhang T, Hu S, et al. Fast desensitization of acetylcholine receptors induced by a spider toxin. Channels (Austin). 2021;15(1):507-515. Published 2021 Dec. doi:10.1080/19336950.2021.1961459

PMID: 34374321

5.2 Protein Sequence Databases

5.3 3D Structure Databases

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

AlphaFoldDB: Q7YT39

5.4 Nucleotide Sequence Databases

Sl. no.	Accession(s)	Access Link(s)
1.	AY316118	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: IPR011696

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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