PROSITE documentation PDOC51862
BetaSPN-type cysteine-stabilized alpha/beta (CS-alpha/beta) domain profile


Scorpion venoms are complex mixture of peptides with a variety of pharmacological functions. These toxin peptides include ion channel modulators, antibacterial peptides, and protease inhibitors. Scorpion toxins targeting various ion channels share a cysteine-stabilized α/β (CS-α/β) structure, which can be divided into two types: short-chain toxins of 2342 amino acid residues with 3 or 4 disulfide bridges, which are commonly potassium channel blockers, and long-chain toxins of 5378 amino acids, which are mostly modulators of sodium channels.

In addition to the classic short-chain toxins such as α-KTxs, which are specific for potassium channels, long-chain toxins with unique structure and function, which were named β-KTxs and scorpine-like peptides, were identified from the scorpion families Buthidae, Scorpionidae and Caraboctonidae. Peptides of the βSPN (β-KTxs and scorpines) family, which are 5975 amino acid residues in length, display various antimicrobial, cytolytic, and potassium channel-blocking activities. βSPN family full-length mature peptides contain two structural domains that confer them bi-functionality: the amphipathic α-helical N-terminal domain has cytolytic or antimicrobial activity, while the three-disulfid bridged C-terminal domain with the consensus CS-α/β motif has K(+) channel blocking activity. Sequence analysis revealed that the βSPN family can be divided into three distinct groups: (1) β-KTx-like peptides from buthids; (2) Scorpine-like peptides from Scorpionidae and Caraboctonidae species, including scorpine, Opiscorpines 14, HgeScplp1, HgeScplp2 and Heteroscorpine 1; (3) heterogeneous peptides similar to BmTXKβ of buthids and iurids [1,2,3,4,5].

The βSPN-type CS-α/β domain is more closely related to invertebrate defensins, antimicrobial peptides involved in the innate immune response of several invertebrate groups (see <PDOC00356>), than to the classical scorpion toxins. Its structure shows an α helix along with one β sheet stabilized by three disulfide bridges, folding into a CS-α/β motif (see <PDB:5IPO>). The connectivity between the ordinal numbered cysteines is C1-C4, C2-C5, and C3-C6 [5].

The profile we developed covers the entire βSPN-type CS-α/β domain.

Last update:

April 2018 / First entry.


Technical section

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

BSPN_CSAB, PS51862; BetaSPN-type cysteine-stabilized alpha/beta (CS-alpha/beta) domain profile  (MATRIX)


1AuthorsDiego-Garcia E. Schwartz E.F. D'Suze G. Gonzalez S.A.R. Batista C.V.F. Garcia B.I. de la Vega R.C. Possani L.D.
TitleWide phylogenetic distribution of Scorpine and long-chain beta-KTx-like peptides in scorpion venoms: identification of 'orphan' components.
SourcePeptides 28:31-37(2007).
PubMed ID17141373

2AuthorsFeng J. Yu C. Wang M. Li Z. Wu Y. Cao Z. Li W. He X. Han S.
TitleExpression and characterization of a novel scorpine-like peptide Ev37, from the scorpion Euscorpiops validus.
SourceProtein Expr. Purif. 88:127-133(2013).
PubMed ID23262394

3AuthorsLuna-Martinez K. Jimenez-Vargas J.M. Possani L.D.
TitleScorpine-Like Peptides. Single Cell Biology 5(2016).

4AuthorsZhu S. Gao B. Aumelas A. del Carmen Rodriguez M. Lanz-Mendoza H. Peigneur S. Diego-Garcia E. Martin-Eauclaire M.-F. Tytgat J. Possani L.D.
TitleMeuTXKbeta1, a scorpion venom-derived two-domain potassium channel toxin-like peptide with cytolytic activity.
SourceBiochim. Biophys. Acta 1804:872-883(2010).
PubMed ID20045493

5AuthorsFlores-Solis D. Toledano Y. Rodriguez-Lima O. Cano-Sanchez P. Ramirez-Cordero B.E. Landa A. Rodriguez de la Vega R.C. Del Rio-Portilla F.
TitleSolution structure and antiparasitic activity of scorpine-like peptides from Hoffmannihadrurus gertschi.
SourceFEBS Lett. 590:2286-2296(2016).
PubMed ID27314815

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