PROSITE documentation PDOC00597Germin family signature
Germins and germin-like proteins [1,2] are a family of hexameric ubiquitous plant glycoproteins. They are not restricted to germinating grains as initially sought and thereof called 'germins', but they exist in all organs and developmental stages. All are at least partly associated with the extracellular matrix.
A wide range of function has been uncovered for germins and germin-like proteins: some act as oxalate oxidases (EC 1.2.3.4) or as superoxide dismutase (EC 1.15.1.1), while others seems to be structural proteins or receptors for auxins or proteins.
Germins and germin-like proteins are highly similar to slime mold spherulins 1a and 1b which are proteins that accumulate specifically during spherulation, a process induced by various forms of environmental stress which leads to encystment and dormancy.
As a signature pattern we selected the best conserved region: 14 amino acids located in the central section of these proteins. This region contains three residues most probably implicated in the binding of a manganese ion [3].
Last update:May 2004 / Text revised.
-------------------------------------------------------------------------------
PROSITE method (with tools and information) covered by this documentation:
1 | Authors | Lane B.G. |
Title | Oxalate, germin, and the extracellular matrix of higher plants. | |
Source | FASEB J. 8:294-301(1994). | |
PubMed ID | 8143935 |
2 | Authors | Bernier F. Berna A. |
Source | Plant Physiol. Biochem. 39:545-554(2001). |
3 | Authors | Gane P.J. Dunwell J.M. Warwicker J. |
Title | Modeling based on the structure of vicilins predicts a histidine cluster in the active site of oxalate oxidase. | |
Source | J. Mol. Evol. 46:488-493(1998). | |
PubMed ID | 9541544 |
PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see prosite_license.html.
View entry in original PROSITE document format
View entry in raw text format (no links)