Frizzled domain
IPR020067
Definition
The frizzled (fz) domain is an extracellular domain of about 120 amino acids.It was first identified in the alpha-1 chain of type XVIII collagen and in members of the Frizzled family of seven transmembrane (7TM) proteins which act as receptors for secreted Wingless (Wg)/Wnt glycoproteins PMID:7876242. In addition to these proteins, one or two copies of the fz domain are also found [[cite:PMID:9637908], [cite:PMID:9637909], [cite:PMID:10082384], [cite:PMID:9852758], [cite:PMID:10329693]] in: The Frzb family; secreted frizzled-like proteins. Smoothened; another 7TM receptor involved in hedgehog signaling. Carboxpeptidase Z (CPZ). Transmembrane serine protease corin (atrial natriuretic peptide-converting enzyme). Two receptor tyrosine kinases (RTKs) subfamilies, the Ror family and the muscle-specific kinase (MuSK) family. As the fz domain contains 10 cysteines which are largely conserved, it has also been called cysteine-rich domain (CRD) PMID:7876242. The fz domain also contains several other highly conserved residues, for example, a basic amino acid follows C6, and a conserved proline residues lies four residues C-terminal to C9 PMID:9852758. The crystal structure of a fz domain shows that it is predominantly α-helical with all cysteines forming disulphide bonds. In addition to helical regions, two short β-strands at the N terminus form a minimal β-sheet with the second β sheet passing through a knot created by disulphide bonds PMID:11452312. Several fz domains have been shown to be both necessary and sufficient for Wg/Wnt ligand binding, strongly suggesting that the fz domain is a Wg/Wnt interacting domain [[cite:PMID:8717036], [cite:PMID:9326585]].
23 human proteins with this domain
Each is a reviewed human protein in the Seroatlas serome and a potential autoantibody target; this domain groups them into one antibody-relevant category. Every entry links to its own record.
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