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.