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PROSITE documentation PDOC00577

ZP domain signature and profile

Description:

The zona pellucida (ZP) domain is a protein polymerization module of ~260 amino acid module, which is found at the C-terminus of many secreted eukaryotic glycoproteins that play fundamental roles in development, hearing, immunity, and cancer [1,2,3,4]:

  • 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 as a second sperm receptor reinforcing the interactions. ZP1 cross-links the polymers formed by ZP2 and ZP3.
  • Zona pellucida sperm-binding protein B (ZP-B) (also known as ZP-X in rabbit and ZP-3 α in pig).
  • Glycoprotein GP2, the major component of pancreatic secretory granule membranes.
  • TGF-β receptor type III (also known as βglycan). This protein is a proteoglycan that binds to TGF-β and could be involved in capturing and retaining TGF-β for presentation to the signalling receptors.
  • Uromodulin (also known as Tamm-Horsfall urinary glycoprotein). The function of this protein, which is the most abundant in human urine, is not yet clear.
  • Chicken β-tectorin, a major glycoprotein of avian tectorial membrane.

Most ZP domain proteins are synthesized as precursors with carboxy-terminal transmembrane domains or glycosyl phosphatidylinositol (GPI) anchors [2].

The ZP domain contains eight strictly conserved cysteines, which form disulfide bridges. The disulfide bonds within the ZP domains are divided into two groups, suggesting that the ZP domain consists of two subdomains. In addition to the conserved cysteines, only a few aromatic or hydrophobic amino acids are absolutely invariant, probably as a result of structural rather than functional constraints [1,3,4].

The profile we developed covers the entire ZP domain.

Note:

Endoglins are reported to contain a region of homology with the N- terminal third of the ZP domain [5]. This truncated version of the ZP domain is not recognized by the profile.

Expert(s) to contact by email:

Bork P.

Last update:

December 2004 / Pattern and text revised.

Technical section:

PROSITE methods (with tools and information) covered by this documentation:

ZP_2, PS51034; ZP domain profile  (MATRIX)
Sequences known to belong to this class detected by the profile: ALL
Other sequence(s) detected in Swiss-Prot: NONE.
• Domain architecture view of Swiss-Prot proteins matching PS51034
PS51034
• Retrieve an alignment of Swiss-Prot true positive hits:
  Clustal format, color, condensed view  / Clustal format, color  / Clustal format, plain text  / Fasta format
• Retrieve the sequence logo from the alignment
• Taxonomic tree view of all Swiss-Prot/TrEMBL entries matching PS51034
• Retrieve a list of all Swiss-Prot/TrEMBL entries matching PS51034
• Scan Swiss-Prot/TrEMBL entries against PS51034
• view ligand binding statistics
Matching PDB structures: 3D4C 3D4G 3EF7 3NK3 ... [ALL]
ZP_1, PS00682; ZP domain signature  (PATTERN)
Consensus pattern: [LIVMFYW]-x(7)-[STAPDNLR]-x(3)-[LIVMFYW]-x-[LIVMFYW]-x-[LIVMFYW]-x(2)-C-[LIVMFYW]-x-[STA]-[PSLT]-x(2,4)-[DENSG]-x-[STADNQLFM]-x(6)-[LIVM](2)-x(3,4)-C
The 2 C's may be involved in disulfide bonds
Sequences known to belong to this class detected by the pattern: ALL
Other sequence(s) detected in Swiss-Prot: NONE.
• Retrieve an alignment of Swiss-Prot true positive hits:
  Clustal format, color, condensed view  / Clustal format, color  / Clustal format, plain text  / Fasta format
• Retrieve the sequence logo from the alignment
• Taxonomic tree view of all Swiss-Prot/TrEMBL entries matching PS00682
• Retrieve a list of all Swiss-Prot/TrEMBL entries matching PS00682
• Scan Swiss-Prot/TrEMBL entries against PS00682
• view ligand binding statistics
Matching PDB structures: 3NK3 3NK4 3QW9 [ALL]

References:

1 AuthorsBork P., Sander C.
TitleA large domain common to sperm receptors (Zp2 and Zp3) and TGF-beta type III receptor.
SourceFEBS Lett. 300:237-240(1992).
PubMed ID1313375
2 AuthorsJovine L., Qi H., Williams Z., Litscher E., Wassarman P.M.
TitleThe ZP domain is a conserved module for polymerization of extracellular proteins.
SourceNat. Cell Biol. 4:457-461(2002).
PubMed ID12021773
DOI10.1038/ncb802
3 AuthorsYonezawa N., Nakano M.
TitleIdentification of the carboxyl termini of porcine zona pellucida glycoproteins ZPB and ZPC.
SourceBiochem. Biophys. Res. Commun. 307:877-882(2003).
PubMed ID12878193
4 AuthorsJovine L., Qi H., Williams Z., Litscher E.S., Wassarman P.M.
TitleA duplicated motif controls assembly of zona pellucida domain proteins.
SourceProc. Natl. Acad. Sci. U.S.A. 101:5922-5927(2004).
PubMed ID15079052
DOI10.1073/pnas.0401600101
5 AuthorsGe A.Z., Butcher E.C.
TitleCloning and expression of a cDNA encoding mouse endoglin, an endothelial cell TGF-beta ligand.
SourceGene 138:201-206(1994).
PubMed ID8125301

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