*********************** * ZP domain signature * *********************** A domain of about 260 amino acid residues has been recognized [1] in a number of receptor-like eukaryotic glycoproteins; these proteins are listed below. - Sperm receptor proteins ZP2 and ZP3. Along with protein ZP1, proteins ZP2 and ZP3 are responsible for sperm-adhesion to the zona pellucida. ZP3 first binds to specific sperm proteins, thus mediating sperm contacts with the oocyte. ZP2 acts a second sperm receptor reinforcing the interactions. ZP1 cross-links the polymers formed by ZP2 and ZP3. - Glycoprotein GP2, the major component of pancreatic secretory granule membranes. - TGF-beta receptor type III (also known as betaglycan). This protein is a proteoglycan that binds to TGF-beta and that could be involved in capturing and retaining TGF-beta for presentation to the signalling receptors. - Uromodulin (also known as Tamm-Horsfall urinary glycoprotein). The function of this protein, which is the most abundant protein in human urine, is not yet clear. All of the above proteins are mosaic proteins composed of various domains, but they all consist of a large extracellular region followed by either a transmembrane region and a very short cytoplasmic region or by a GPI-anchor. The domain which is common to these proteins, and that we call 'ZP', is found in the C-terminal section of the extracellular region. The ZP domain contains eight conserved cysteines that are probably involved in disulfide bonds. As a signature pattern for this domain we selected a region, in the central part of the ZP domain, that contains two of the conserved cysteines. -Consensus pattern: [LIVMFYW]-x(7)-[STADN]-x(3)-[LIVMFYW]-x-[LIVMFYW]-x- [LIVMFYW]-x(2)-C-[LIVMFYW]-x-[ST]-[PS]-x(2,4)-[DN]-x- [STADN]-x(6)-[LIVM](2)-x(3,4)-C [The two C's are probably involved in disulfide bonds] -Sequences known to belong to this class detected by the pattern: ALL. -Other sequence(s) detected in SWISS-PROT: NONE. -Expert(s) to contact by email: Bork P. bork@embl-heidelberg.de -Last update: June 1992 / First entry. [ 1] Bork P., Sander C. FEBS Lett. 300:237-240(1992).