************************************************************
* Cereal trypsin/alpha-amylase inhibitors family signature *
************************************************************

The seeds  of cereals contain  numerous  serine  proteases  and  alpha-amylase
inhibitors. These inhibitors can be grouped into families  based on structural
similarities. The cereal trypsin/alpha-amylase inhibitor family [1,2] consists
of proteins of about 120 amino acids  which  contain 10 cysteine residues, all
of which  are  involved  in  disulfide  bonds.  Some of  these  inhibitors are
specific to trypsin, others to alpha-amylase, and a few are bifunctional.  The
schematic representation of the structure of these inhibitors is shown below:

                       +----------------------------+
           +----------+|   +-+                      |
    *******|****      ||   | |                      |
  xxCxxxxxxCxxxCxxxxxxCCxxxCxCxxxxxxxxxxxxxCxxxxxxxxCxxxxxxxCxxxx
    |          |                           |                |
    |          +---------------------------+                |
    +-------------------------------------------------------+

'C': conserved cysteine involved in a disulfide bond.
'*': position of the pattern.

This family of proteins also includes a number of seed allergenic protein from
rice [3].

-Consensus pattern: C-x(10)-L-x(2)-C-x(2)-[LIVMFY](2)-x(3,4)-C
                    [The three C's are involved in disulfide bonds]
-Sequences known to belong to this class detected by the pattern: ALL.
-Other sequence(s) detected in SWISS-PROT: Drosophila Notch, human uromodulin,
 human complement receptor 2 and Trypanosoma leucine repeat protein ESAG-8.
-Last update: June 1994 / Text revised.

[ 1] Gautier M.-F., Alary R., Joudirer P.
     Plant Mol. Biol. 14:313-322(1990).
[ 2] Garcia-Olmedo F., Salcedo G., Sanchez-Monge R., Gomez L., Royo J.,
     Carbonero P.
     (In) Oxford Surveys of Plant Molecular and Cell Biology, Miflin B., Ed.,
     vol. 4, pp. 275-334, Oxford University Press, Oxford, (1987).
[ 3] Adachi T., Izumi H., Yamada T., Tanaka K., Takeuchi S., Nakamura R.,
     Matsuda T.
     Plant Mol. Biol. 21:239-248(1993).