InterPro : IPR019011

Name  Cryptic/Cripto, CFC domain Short Name  Cryptic/Cripto_CFC-dom
Type  Domain Description  This entry represents the CFC domain found in the membrane protein Cripto (or teratocarcinoma-derived growth factor), a protein over expressed in many tumours [, ]and structurally similar to the C-terminal extracellular portions of Jagged 1 and Jagged 2 []. CFC is approx 40-residues long, compacted by three internal disulphide bridges, and binds Alk4 via a hydrophobic patch. CFC is structurally homologous to the VWFC-like domain []. The protein Cripto is the founding member of the extra-cellular EGF-CFC growth factors, which are composed of two adjacent cysteine-rich domains: the EGF-like and the CFC domains. Members of the EGF-CFC family play key roles in embryonic development and are also implicated in tumourigenesis []. The Cripto protein could play a role in the determination of the epiblastic cells that subsequently give rise to the mesoderm. Although both the EGF and CFC domains are involved in the tumourigenic activity of Crispto proteins, the CFC domain appears to play a crucial role, as it is through the CFC domain that Crispto interferes with the onco-suppressive activity of Activins, either by blocking the Activin receptor ALK4 or by antagonising proteins of the TGF-beta family []. The Cryptic protein is involved in the correct establishment of the left-right axis. May play a role in mesoderm and/or neural patterning during gastrulation.
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Sequence Features

GO Displayer

Proteins

InterPro protein domain ID --> Contigs

 

Other

0 Child Features

0 Contains

2 Found In

Id Name Short Name Type
IPR017047 Teratocarcinoma-derived growth factor Cripto Cripto_growth_factor Family
IPR017436 Cripto-related protein 3 Cripto-rel_3 Family

0 Parent Features

3 Publications

First Author Title Year Journal Volume Pages
Calvanese L Solution structure of mouse Cripto CFC domain and its inactive variant Trp107Ala. 2006 J Med Chem 49 7054-62
Foley SF The CRIPTO/FRL-1/CRYPTIC (CFC) domain of human Cripto. Functional and structural insights through disulfide structure analysis. 2003 Eur J Biochem 270 3610-8
Calvanese L Structural insights into the interaction between the Cripto CFC domain and the ALK4 receptor. 2009 J Pept Sci 15 175-83



To cite PlanMine, please refer to the following publication:

Rozanski, A., Moon, H., Brandl, H., Martín-Durán, J. M., Grohme, M., Hüttner, K., Bartscherer, K., Henry, I., & Rink, J. C.
PlanMine 3.0—improvements to a mineable resource of flatworm biology and biodiversity
Nucleic Acids Research, gky1070. doi:10.1093/nar/gky1070 (2018)