SMART: Pfam domain Fz

The domain within your query sequence starts at position 327 and ends at position 458; the E-value for the Fz domain shown below is 1.1e-27.

CAQYRGEVCDAVLAKDALVFFNTSYRDPEDAQELLIHTAWNELKAVSPLCRPAAEALLCN
HLFQECSPGVVPTPMPICREYCLAVKELFCAKEWQAMEGKAHRGLYRSGMHLLPVPECSK
LPSMHRDPTACT

Fz

PFAM accession number:	PF01392
Interpro abstract (IPR020067):	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 [ (PUBMED:7876242) ]. In addition to these proteins, one or two copies of the fz domain are also found [ (PUBMED:9637908) (PUBMED:9637909) (PUBMED:10082384) (PUBMED:9852758) (PUBMED: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) [ (PUBMED: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 [ (PUBMED:9852758) ]. The crystal structure of a fz domain shows that it is predominantly alpha-helical with all cysteines forming disulphide bonds. In addition to helical regions, two short beta-strands at the N terminus form a minimal beta-sheet with the second beta sheet passing through a knot created by disulphide bonds [ (PUBMED: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 [ (PUBMED:8717036) (PUBMED:9326585) ].
GO function:	protein binding (GO:0005515)

PFAM accession number:

PF01392

Interpro abstract (IPR020067):

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 [ (PUBMED:7876242) ]. In addition to these proteins, one or two copies of the fz domain are also found [ (PUBMED:9637908) (PUBMED:9637909) (PUBMED:10082384) (PUBMED:9852758) (PUBMED: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) [ (PUBMED: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 [ (PUBMED:9852758) ]. The crystal structure of a fz domain shows that it is predominantly alpha-helical with all cysteines forming disulphide bonds. In addition to helical regions, two short beta-strands at the N terminus form a minimal beta-sheet with the second beta sheet passing through a knot created by disulphide bonds [ (PUBMED: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 [ (PUBMED:8717036) (PUBMED:9326585) ].

GO function:

protein binding (GO:0005515)

This is a PFAM domain. For full annotation and more information, please see the PFAM entry Fz