Summary: Transforming growth factor beta type I GS-motif
Transforming growth factor beta type I GS-motif Provide feedback
This motif is found in the transforming growth factor beta (TGF-beta) type I which regulates cell growth and differentiation. The name of the GS motif comes from its highly conserved GSGSGLP signature in the cytoplasmic juxtamembrane region immediately preceding the protein's kinase domain. Point mutations in the GS motif modify the signaling ability of the type I receptor .
Feng XH, Derynck R; , EMBO J 1997;16:3912-3923.: A kinase subdomain of transforming growth factor-beta (TGF-beta) type I receptor determines the TGF-beta intracellular signaling specificity. PUBMED:9233801 EPMC:9233801
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This tab holds annotation information from the InterPro database.
InterPro entry 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].
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|Cellular component||membrane (GO:0016020)|
|Molecular function||ATP binding (GO:0005524)|
|transmembrane receptor protein serine/threonine kinase activity (GO:0004675)|
|Biological process||protein phosphorylation (GO:0006468)|
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Curation and family details
|Seed source:||Pfam-B_630 (release 18.0)|
|Number in seed:||27|
|Number in full:||927|
|Average length of the domain:||27.40 aa|
|Average identity of full alignment:||69 %|
|Average coverage of the sequence by the domain:||5.57 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 80369284 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||8|
|Download:||download the raw HMM for this family|
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For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the TGF_beta_GS domain has been found. There are 74 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.
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