{PDOC00619}
{PS00771; BARWIN_1}
{PS00772; BARWIN_2}
{PS51174; BARWIN_3}
{BEGIN}
****************************************
* Barwin domain signatures and profile *
****************************************

Barwin [1] is a barley seed protein of 125 residues that binds weakly a chitin
analog. It contains six cysteines involved in disulfide bonds, as shown in the
following schematic representation.

                              +---------------+
                              |    *****      |                ****
    xxxxxxxxxxxxxxxCxxxxxxxxxxCxxxxCxCxxxxxxxxCxxxxxxxxxxxxxxxxxxCx
                   |               | |                           |
                   +---------------+ +---------------------------+

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

Barwin is closely related to the following proteins:

 - Hevein, a wound-induced protein found in the latex of rubber trees.
 - HEL, an Arabidopsis thaliana hevein-like protein [2].
 - Win1 and win2, two wound-induced proteins from potato.
 - Pathogenesis-related protein 4 from tobacco.

Hevein and the win1/2 proteins consist  of an N-terminal chitin-binding domain
followed by  a  barwin-like C-terminal domain of ~122 residues. Barwin and its
related proteins could be involved in a defense mechanism in plants [1].

The dominating structural feature of the barwin domain is a well-defined four-
stranded antiparallel beta-sheet, two parallel beta-sheets packed antiparallel
to each other and four short alpha-helices (see <PDB:1BW3>) [3].

As signature  patterns,  we selected two highly conserved regions that contain
some of  the  cysteines.  We  also  developed a profile that covers the entire
barwin domain.

-Consensus pattern: C-G-[KR]-C-L-x-V-x-N
                    [The 2 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: NONE.

-Consensus pattern: V-[DN]-Y-[EQD]-F-V-[DN]-C
                    [C is involved in a disulfide bond]
-Sequences known to belong to this class detected by the pattern: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.

-Sequences known to belong to this class detected by the profile: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.

-Last update: December 2005 / Text revised; profile added.

[ 1] Svensson B., Svendsen I., Hoejrup P., Roepstorff P., Ludvigsen S.,
     Poulsen F.M.
     "Primary structure of barwin: a barley seed protein closely related to
     the C-terminal domain of proteins encoded by wound-induced plant
     genes."
     Biochemistry 31:8767-8770(1992).
     PubMed=1390663;
[ 2] Potter S., Uknes S., Lawton K., Winter A.M., Chandler D.,
     Dimaio J., Novitzky R., Ward E., Ryals J.
     "Regulation of a hevein-like gene in Arabidopsis."
     Mol. Plant Microbe Interact. 6:680-685(1993).
     PubMed=8118053;
[ 3] Ludvigsen S., Poulsen F.M.
     "Three-dimensional structure in solution of barwin, a protein from
     barley seed."
     Biochemistry 31:8783-8789(1992).
     PubMed=1390665

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