PROSITE documentation PDOC00244Plant thionins signature
Thionins are small, basic, plant proteins generally toxic to animal cells [1]. They seem to exert their toxic effect at the level of the cell membrane but their exact function is not known. They consist of a polypeptide chain of forty five to fifty amino acids with three to four internal disulfide bonds. They are found in seeds but also in the cell wall of leaves [2]. Thionins are processed from larger precursor proteins [3]. Crambin [4], a hydrophobic plant seed protein, also belongs to this family. The pattern we developed to detect this family of proteins includes three of the six cysteine residues involved in disulfide bonds.
+-----------------------------------+ |+----------------------------+ | || | | xxCCxxxxxxxxxxxCxxxxxxxxxCxxxCxxCxxxxxCxxxxxxxx ************** | | | +---------+
'C': conserved cysteine involved in a disulfide bond. '*': position of the pattern.Note:
The proteins from the γ-thionin family are not related to the above proteins and are described in a separate section.
Last update:May 2004 / Text revised.
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PROSITE method (with tools and information) covered by this documentation:
1 | Authors | Vernon L.P. Evett G.E. Zeikus R.D. Gray W.R. |
Title | A toxic thionin from Pyrularia pubera: purification, properties, and amino acid sequence. | |
Source | Arch. Biochem. Biophys. 238:18-29(1985). | |
PubMed ID | 3985614 |
2 | Authors | Bohlmann H. Clausen S. Behnke S. Giese H. Hiller C. Reimann-Phillip U. Schrader G. Barkholt V. Apel K. |
Source | EMBO J. 7:1559-1565(1988). |
3 | Authors | Bohlmann H. Apel K. |
Source | Mol. Gen. Genet. 207:446-454(1987). |
4 | Authors | Teeter M.M. Mazer J.A. L'Italien J.J. |
Title | Primary structure of the hydrophobic plant protein crambin. | |
Source | Biochemistry 20:5437-5443(1981). | |
PubMed ID | 6895315 |
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