Atrial natriuretic peptide (ANP) is a cardiac hormone essential for the regulation of blood pressure. In cardiac myocytes, ANP is synthesized as a precursor, pro-ANP, which is converted to biologically active ANP by the serine peptidase corin []. This entry represents the atrial natriuretic peptide-converting enzyme corin, which is a type II transmembrane serine protease that belongs to MEROPS peptidase family S1A (clan PA(S)), which is abundantly expressed in the heart. Other serine proteases such as thrombin and kallikrein had previously also been shown to cleave pro-ANP in vitro, but corin has now been shown to be the endogenous pro-ANP convertase in cardiomyocytes []. For corin to cleave its substrate, pro-ANP, it should be catalytically active and located in close proximity []. Corin is highly sequence specific. Corin-mediated pro-ANP activation may play a role in regulating blood pressure [].N-Glycosylation may influence the subcellular localization and biological activity of corin and tunicamycin treatment also significantly reduces corin activity [].Corin in involved in promoting trophoblast invasion and spiral artery remodelling in pregnancy. Mutations in the corin gene cause pre-eclampsia/eclampsia 5 (PEE5) [].
The cysteine-rich domain (CRD) is an essential component of corin, a type II transmembrane serine protease which functions as the convertase of the pro-atrial natriuretic peptide (pro-ANP) in the heart []. Corin contains two CRDs in its extracellular region, which play an important role in recognition of the physiological substrate, pro-ANP. This entry represents the first (N-terminal) CRD [].
The cysteine-rich domain (CRD) is an essential component of corin, a type II transmembrane serine protease which functions as the convertase of the pro-atrial natriuretic peptide (pro-ANP) in the heart []. Corin contains two CRDs in its extracellular region, which play an important role in recognition of the physiological substrate, pro-ANP. This entry represents the second (C-terminal) CRD [].
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 []. In addition to these proteins, one or two copies of the fz domain are also found [, , , , ]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) []. 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 []. 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 beta sheet passing through a knot created by disulphide bonds [].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 [, ].
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 []. In addition to these proteins, one or two copies of the fz domain are also found [, , , , ]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) []. 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 []. 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 beta sheet passing through a knot created by disulphide bonds [].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 [, ].
