{PDOC51488}
{PS51488; KBD}
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* KBD domain profile *
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The c-Kit-binding  domain (KBD) composed of about 50 amino acids is found in a
family of  membrane-bound molecules, Spreds, which contain an EVH1 domain (see
<PDOC50229>) in the N-terminus and a Sprouty-related cysteine rich region (SPR
domain) (see <PDOC51227>) in the C-terminus [1,2]:

 - Spred-1
 - Spred-2
 - Spred-3.  It  does  not possess a functional KBD domain, since the critical
   amino acid Arg was replaced with Gly.

Spred proteins  function  as  suppressors of the MAP kinase pathway in various
systems. Each member of the Spred family may have a selective function for the
regulation of the MAP kinase cascade [1,2].

The profile we developed covers the entire KBD domain.

-Sequences known to belong to this class detected by the profile: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.
-Last update: April 2010 / First entry.

[ 1] Wakioka T., Sasaki A., Kato R., Shouda T., Matsumoto A., Miyoshi K.,
     Tsuneoka M., Komiya S., Baron R., Yoshimura A.
     "Spred is a Sprouty-related suppressor of Ras signalling."
     Nature 412:647-651(2001).
     PubMed=11493923; DOI=10.1038/35088082
[ 2] Kato R., Nonami A., Taketomi T., Wakioka T., Kuroiwa A., Matsuda Y.,
     Yoshimura A.
     "Molecular cloning of mammalian Spred-3 which suppresses tyrosine
     kinase-mediated Erk activation."
     Biochem. Biophys. Res. Commun. 302:767-772(2003).
     PubMed=12646235

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