|SMART accession number:||SM00467|
|Description:||Aa approx. 30 amino acid motif that precedes the kinase domain in types I and II TGF beta receptors. Mutation of two or more of the serines or threonines in the TTSGSGSG of TGF-beta type I receptor impairs phosphorylation and signaling activity.|
|Interpro abstract (IPR003605):|
Transforming growth factor beta (TGF-beta) is a member of a large family of secreted growth factors of central importance in eukaryotic development and homeostasis. Members of this family, which includes the activins, inhibins and bone morphogenic proteins (BMPs), bind to receptors that consist of two transmembrane serine/threonine (Ser/Thr) kinases called the type I and type II receptors. Type II activates Type I upon formation of the ligand receptor complex by multiply phosphorylating the GS domain, a short (~30 residues), highly conserved regulatory sequence just N-terminal to the kinase domain on the cytoplasmic side of the receptor. The GS domain is found only in the type I receptor family and is named for the TTSGSGSG sequence at its core. At least three, and perhaps four to five of the serines and threonines in the GS domain, must be phosphorylated to fully activate TbetaR-1 [(PUBMED:11583628)].
The GS domain forms a helix-loop-helix structure in which the sites of activating phosphorylation are situated in a loop known as the GS loop. One key role for phosphorylation is to block the adoption of an inactivating configuration by the GS domain [(PUBMED:10025408)].
|GO process:||protein phosphorylation (GO:0006468)|
|GO component:||membrane (GO:0016020)|
|GO function:||transmembrane receptor protein serine/threonine kinase activity (GO:0004675), ATP binding (GO:0005524)|
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