|PROSITE documentation PDOC00180 [for PROSITE entry PS00203]|
Metallothioneins (MT) [1,2,3] are small proteins which bind heavy metals such as zinc, copper, cadmium, nickel, etc., through clusters of thiolate bonds. MT's occur throughout the animal kingdom and are also found in higher plants, fungi and some prokaryotes. On the basis of structural relationships MT's have been subdivided into three classes. Class I includes mammalian MT's as well as MT's from crustacean and molluscs, but with clearly related primary structure. Class II groups together MT's from various species such as sea urchins, fungi, insects and cyanobacteria which display none or only very distant correspondence to class I MT's. Class III MT's are atypical polypeptides containing γ-glutamylcysteinyl units.
Vertebrate class I MT's are proteins of 60 to 68 amino acid residues, 20 of these residues are cysteines that bind to 7 bivalent metal ions. As a signature pattern we chose a region that spans 19 residues and which contains seven of the metal-binding cysteines, this region is located in the N-terminal section of class-I MT's.Note:
This signature pattern is not meant to detect invertebrate class-I MT's whose sequence is highly divergent from that of vertebrate's.Expert(s) to contact by email:
May 2004 / Text revised.
PROSITE method (with tools and information) covered by this documentation:
|Source||Annu. Rev. Biochem. 55:913-951(1986).|
|2||Authors||Kagi J.H.R. Schaffer A.|
|Title||Biochemistry of metallothionein.|
|Source||Thesis, 1996, University of Zurich.|