Frizzled cysteine-rich domain superfamily
IPR036790
Definition
This entry represents the frizzled domain superfamily. 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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