Sprouty (Spry) and Spred (Sprouty related EVH1 domain) proteins have been
identified as inhibitors of the Ras/mitogen-activated protein kinase (MAPK)
cascade, a pathway crucial for developmental processes initiated by activation
of various receptor tyrosine kinases [1,2]. These proteins share a conserved,
C-terminal cysteine-rich region, the SPR domain. This domain has been defined
as a novel cytosol to membrane translocation domain [1,2,3,4]. It has been
found to be a PtdIns(4,5)P2-binding domain that targets the proteins to a
cellular localization that maximizes their inhibitory potential [5,6]. It also
mediates homodimer formation of these proteins [1,5].
The SPR domain can occur in association with the WH1 domain (see <PDOC50229>)
(located in the N-terminal part of the proteins) in the Spred proteins.
We developed a profile that spans the entire SPR domain.
The SPR domain is also named Spry translocation domain (SpryTD).
July 2006 / First entry.
PROSITE method (with tools and information) covered by this documentation:
King J.A.J. Straffon A.F.L. D'Abaco G.M. Poon C.L.C. I S.T.T. Smith C.M. Buchert M. Corcoran N.M. Hall N.E. Callus B.A. Sarcevic B. Martin D. Lock P. Hovens C.M.
Distinct requirements for the Sprouty domain for functional activity of Spred proteins.
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