{PDOC51376}
{PS51376; DBB}
{BEGIN}
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* DBB domain profile *
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The following  proteins  share  a  number  of  distinct parts, namely, ankyrin
repeats (see  <PDOC50088>),  a coiled coil, and a stretch of approximately 140
amino acid residues upstream of the ankyrin repeats, which has been called the
Dof/BCAP/BANK (DBB) domain [1,2]:

 - Drosophila  Downstream-of-EGF  receptor  (Dof), a protein essential for the
   morphogenesis of  both  the mesoderm and the tracheae. It has been proposed
   to mediate the transmission of a signal from an activated receptor to other
   components of the cell, including the MAP kinase cascade.
 - Vertebrate BANK and BCAP proteins that function in B-cell signaling.

These proteins  are  involved in signaling; however, unlike Dof, BANK and BCAP
are not  implicated in FGF signaling but appear to have undergone rapid change
during the   course  of  evolution  to  acquire  a  novel  function  with  the
development of the immune system in higher vertebrates.

The DBB domain in both Dof and BCAP is required to mediate self-association in
yeast cells,  indicating  that  this  domain  may  have a more general role in
mediating protein-protein interactions [1].

The profile we developed covers the entire DBB domain.

-Sequences known to belong to this class detected by the profile: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.
-Last update: April 2008 / First entry.

[ 1] Battersby A., Csiszar A., Leptin M., Wilson R.
     "Isolation of proteins that interact with the signal transduction
     molecule Dof and identification of a functional domain conserved
     between Dof and vertebrate BCAP."
     J. Mol. Biol. 329:479-493(2003).
     PubMed=12767830
[ 2] Wilson R., Battersby A., Csiszar A., Vogelsang E., Leptin M.
     "A functional domain of Dof that is required for fibroblast growth
     factor signaling."
     Mol. Cell. Biol. 24:2263-2276(2004).
     PubMed=14993266

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