CFC domain
Protein domain
title: "CFC domain" type: doc version: 1 created: 2026-02-28 author: "Wikipedia contributors" status: active scope: public tags: ["protein-domains"] description: "Protein domain" topic_path: "general/protein-domains" source: "https://en.wikipedia.org/wiki/CFC_domain" license: "CC BY-SA 4.0" wikipedia_page_id: 0 wikipedia_revision_id: 0
::summary Protein domain ::
::data[format=table title="Infobox protein family"]
| Field | Value |
|---|---|
| Symbol | CFC |
| Name | CFC |
| image | PDB 2j5h EBI.jpg |
| caption | nmr analysis of mouse cripto cfc domain |
| Pfam | PF09443 |
| InterPro | IPR019011 |
| :: |
| Symbol = CFC | Name = CFC | image = PDB 2j5h EBI.jpg | width = | caption = nmr analysis of mouse cripto cfc domain | Pfam = PF09443 | Pfam_clan = | InterPro = IPR019011 | SMART = | PROSITE = | MEROPS = | SCOP = | TCDB = | OPM family = | OPM protein = | CAZy = | CDD = In molecular biology, the CFC domain (Cripto_Frl-1_Cryptic domain) is a protein domain found at the C-terminus of a number of proteins including Cripto (or teratocarcinoma-derived growth factor). It is 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 CFC domain appears to play a crucial role in the tumourigenic activity of Cripto proteins, as it is through the CFC domain that Cripto interferes with the onco-suppressive activity of Activins, either by blocking the Activin receptor ALK4 or by antagonising proteins of the TGF-beta family.
References
References
- (September 2003). "The CRIPTO/FRL-1/CRYPTIC (CFC) domain of human Cripto. Functional and structural insights through disulfide structure analysis". Eur. J. Biochem..
- (November 2006). "Solution structure of mouse Cripto CFC domain and its inactive variant Trp107Ala". J. Med. Chem..
- (March 2009). "Structural insights into the interaction between the Cripto CFC domain and the ALK4 receptor". J. Pept. Sci..
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