PROSITE documentation PDOC60021
Huwentoxin-1 family signature


The spider venoms often contain many active peptides such as neurotoxins, lectins, inhibitors to enzyme, etc. These peptides are very important for spider's hunting and defending. During the long history of spider evolution, the peptides evolved into different structures and functions. Despite their different biological functions the following peptides appear to have evolved from the same ancestors and belong to the huwentoxin-1 family [1]:

  • Ornithoctonus huwena (Chinese bird spider) (Selenocosmia huwena) huwentoxin-I (HWTX-I), a 33 amino acid peptide, which can block the N-type high-voltage activated calcium channels [2].
  • Ornithoctonus huwena (Chinese bird spider) (Selenocosmia huwena) huwentoxin-IIIa (HWTX-IIIa).
  • Ornithoctonus huwena (Chinese bird spider) (Selenocosmia huwena) huwentoxin-IV (HWTX-IV), a 35 amino acid peptide, which is an inhibitor of tetrodotoxin (TTX) sensitive voltage-gated sodium channel [3].
  • Ornithoctonus huwena (Chinese bird spider) (Selenocosmia huwena) huwentoxin-V (HWTX-V), a 35 amino acid insecticidal toxin which can reversibly paralyze in insects [4].
  • Ornithoctonus huwena (Chinese bird spider) (Selenocosmia huwena) huwenlectin-I (SHL-I), a 32 amino acid peptide with haemagglutination activity but almost no neurotoxin activity.
  • Selenocosmia hainana Hainantoxin-I (HNTX-I), Hainantoxin-III (HNTX-III), Hainantoxin-IV (HNTX-IV) and Hainantoxin-V (HNTX-V) [5].
  • Brachypelma smithii (Mexican red knee tarantula) Venom protein 5.
  • Grammostola spatulata (Chilean rose tarantula) voltage sensor toxin 1.

Peptides of the huwentoxin type I family contain 6 cysteine residues involved in three disulfide bonds. The three disulfide bridges have been assigned as C1-C4, C2-C5 and C3-C6. HWTX-I adopts a compact structure consisting of a small triple-stranded antiparallel β-sheet and five β-turns (see <PDB:1QK6>) [6].

We developed a pattern for huwentoxin-1 family proteins, which have a [C-C-CC-C-C] cysteine arrangement. The three-dimensional structure of huwentoxin-1 family proteins possess a knottin scafold (see <PDOC60004>) [E1].

Expert(s) to contact by email:

Ramakumar S.

Last update:

August 2005 / First entry.


Technical section

PROSITE method (with tools and information) covered by this documentation:

HWTX_1, PS60021; Huwentoxin-1 family signature  (PATTERN)


1AuthorsDiao J. Lin Y. Tang J. Liang S.-P.
TitlecDNA sequence analysis of seven peptide toxins from the spider Selenocosmia huwena.
SourceToxicon 42:715-723(2003).
PubMed ID14757201

2AuthorsLiang S.-P. Zhang D.Y. Pan X. Chen Q. Zhou P.A.
TitleProperties and amino acid sequence of huwentoxin-I, a neurotoxin purified from the venom of the Chinese bird spider Selenocosmia huwena.
SourceToxicon 31:969-978(1993).
PubMed ID8212049

3AuthorsLiu Z. Dai J. Chen Z. Hu W. Xiao Y. Liang S.-P.
TitleIsolation and characterization of hainantoxin-IV, a novel antagonist of tetrodotoxin-sensitive sodium channels from the Chinese bird spider Selenocosmia hainana.
SourceCell. Mol. Life Sci. 60:972-978(2003).
PubMed ID12827284

4AuthorsZhang P.F. Chen P. Hu W.-J. Liang S.-P.
TitleHuwentoxin-V, a novel insecticidal peptide toxin from the spider Selenocosmia huwena, and a natural mutant of the toxin: indicates the key amino acid residues related to the biological activity.
SourceToxicon 42:15-20(2003).
PubMed ID12893056

5AuthorsXiao Y.-C. Liang S.-P.
TitlePurification and characterization of Hainantoxin-V, a tetrodotoxin-sensitive sodium channel inhibitor from the venom of the spider Selenocosmia hainana.
SourceToxicon 41:643-650(2003).
PubMed ID12727268

6AuthorsQu Y. Liang S. Ding J. Liu X. Zhang R. Gu X.
TitleProton nuclear magnetic resonance studies on huwentoxin-I from the venom of the spider Selenocosmia huwena: 2. Three-dimensional structure in solution.
SourceJ. Protein Chem. 16:565-574(1997).
PubMed ID9263120


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