Zona pellucida-like domain

Last updated
Zona pellucida-like domain
Identifiers
SymbolZona_pellucida
Pfam PF00100
InterPro IPR001507
SMART SM00241
PROSITE PDOC00577
Membranome 146
Available protein structures:
Pfam   structures / ECOD  
PDB RCSB PDB; PDBe; PDBj
PDBsum structure summary

The zona pellucida-like domain (ZP domain / ZP-like domain / ZP module) [1] [2] is a large protein region of about 260 amino acids. It has been recognised in a variety of receptor-like eukaryotic glycoproteins. [1] All of these molecules are mosaic proteins with a large extracellular region composed of various domains, often followed by either a transmembrane domain and a short cytoplasmic region or by a GPI-anchor. [2]

Functional and crystallographic studies revealed that the "ZP domain" region common to all these proteins is a protein polymerization module that consists of two distinct but structurally related immunoglobulin-like domains, ZP-N and ZP-C, separated by an interdomain linker (ITD). [3] [4] [5] [6] [7] [8] [9] The ZP module is located in the C-terminal portion of the extracellular region and – with the exception of non-polymeric family member ENG [10] – contains 8 or 10 conserved Cys residues involved in disulfide bonds. [4] [5] [8] The ZP-C domain contains a EHP/IHP motif that controls polymerization. [11]

The first 3D structure of a homopolymeric ZP module protein filament, native human uromodulin (UMOD), was determined by cryo-EM. [12] [13]

Additional copies of isolated ZP-N domains are found in the N-terminal region of egg coat protein subunits involved in fertilization in both vertebrates and invertebrates, with the human zona pellucida components ZP1, ZP2 and ZP4 being the best understood. [4] [14] The mollusc "vitelline envelope receptor for egg lysin" (VERL, Q8WR62 ) is found in the vitelline envelope of mollusc eggs and consists of 22 VERL repeats followed by a ZP module. Structural work from 2017 demonstrated that VERL repeats are also ZP-N domains. [15]

Examples

Humans genes encoding proteins containing this domain include:

Related Research Articles

<span class="mw-page-title-main">Zona pellucida</span> Glycoprotein layer surrounding the plasma membrane of mammalian oocytes

The zona pellucida is the specialized area surrounding mammalian oocytes (eggs). It is also known as an egg coat. The zona pellucida is essential for oocyte growth and fertilization.

<span class="mw-page-title-main">Acrosin</span> Mammalian protein found in Homo sapiens

Acrosin is a digestive enzyme that acts as a protease. In humans, acrosin is encoded by the ACR gene. Acrosin is released from the acrosome of spermatozoa as a consequence of the acrosome reaction. It aids in the penetration of the Zona Pellucida.

<span class="mw-page-title-main">Human fertilization</span> Union of a human egg and sperm

Human fertilization is the union of an egg and sperm, occurring primarily in the ampulla of the fallopian tube. The result of this union leads to the production of a fertilized egg called a zygote, initiating embryonic development. Scientists discovered the dynamics of human fertilization in the 19th century.

The vitelline membrane or vitelline envelope is a structure surrounding the outer surface of the plasma membrane of an ovum or, in some animals, the extracellular yolk and the oolemma. It is composed mostly of protein fibers, with protein receptors needed for sperm binding which, in turn, are bound to sperm plasma membrane receptors. The species-specificity between these receptors contributes to prevention of breeding between different species. It is called zona pellucida in mammals. Between the vitelline membrane and the oolemma is a fluid-filled perivitelline space.

<span class="mw-page-title-main">Uromodulin</span> Mammalian protein found in Homo sapiens

Uromodulin (UMOD), also known as Tamm–Horsfall protein (THP), is a zona pellucida-like domain-containing glycoprotein that in humans is encoded by the UMOD gene. Uromodulin is the most abundant protein excreted in ordinary urine.

<span class="mw-page-title-main">Endoglin</span> Protein-coding gene in the species Homo sapiens

Endoglin (ENG) is a type I membrane glycoprotein located on cell surfaces and is part of the TGF beta receptor complex. It is also commonly referred to as CD105, END, FLJ41744, HHT1, ORW and ORW1. It has a crucial role in angiogenesis, therefore, making it an important protein for tumor growth, survival and metastasis of cancer cells to other locations in the body.

Sialyl-Lewis <sup>X</sup> Chemical compound

Sialyl LewisX (sLeX), also known as cluster of differentiation 15s (CD15s) or stage-specific embryonic antigen 1 (SSEA-1), is a tetrasaccharide carbohydrate which is usually attached to O-glycans on the surface of cells. It is known to play a vital role in cell-to-cell recognition processes. It is also the means by which an egg attracts sperm; first, to stick to it, then bond with it and eventually form a zygote.

<span class="mw-page-title-main">TGF alpha</span> Protein

Transforming growth factor alpha (TGF-α) is a protein that in humans is encoded by the TGFA gene. As a member of the epidermal growth factor (EGF) family, TGF-α is a mitogenic polypeptide. The protein becomes activated when binding to receptors capable of protein kinase activity for cellular signaling.

<span class="mw-page-title-main">ZP3</span> Protein-coding gene in the species Homo sapiens

Zona pellucida sperm-binding protein 3, also known as zona pellucida glycoprotein 3 (Zp-3) or the sperm receptor, is a ZP module-containing protein that in humans is encoded by the ZP3 gene. ZP3 is the glycoprotein in the zona pellucida most important for inducting the acrosome reaction of sperm cells at the beginning of fertilization.

<span class="mw-page-title-main">ZP2</span> Protein-coding gene in the species Homo sapiens

Zona pellucida sperm-binding protein 2 is a protein that in humans is encoded by the ZP2 gene.

<span class="mw-page-title-main">ZP4</span> Protein-coding gene in the species Homo sapiens

Zona pellucida sperm-binding protein 4, ZP-4 or avilesine, named after its discoverer Manuel Avilés Sánchez is a protein that in humans is encoded by the ZP4 gene.

<span class="mw-page-title-main">Alae (nematode anatomy)</span>

The alae is a protruding ridge that forms longitudinally on many nematodes. In the Caenorhabditis elegans nematode they are present in the L1, dauer and adult stages. The alae are most pronounced during the dauer larval stage and not present in the L2, and L3 C. elegans stages.

<span class="mw-page-title-main">FIGLA</span> Protein-coding gene in the species Homo sapiens

Folliculogenesis-specific basic helix-loop-helix, also known as factor in the germline alpha (FIGalpha) or transcription factor FIGa, is a protein that in humans is encoded by the FIGLA gene. The FIGLA gene is a germ cell-specific transcription factor preferentially expressed in oocytes that can be found on human chromosome 2p13.3.

WH1 domains, also known as EVH1 domains, are evolutionary conserved protein domains found on WASP (VASP) proteins, which are often involved in actin polymerization.

Egg lysin is a Mullusca protein that creates a hole in the envelope of the egg thereby allowing the sperm to pass through the envelope and fuse with the egg.

Zona pellucida sperm-binding protein 1 is a protein that cross-links ZP2 and ZP3. Aberrant ZP1 results in sequestration of ZP3 in the cytoplasm, thereby preventing the formation of the zona pellucida around the oocyte.

<span class="mw-page-title-main">Juno (protein)</span> Protein-coding gene in the species Homo sapiens

Juno also known as folate receptor 4, folate receptor delta or IZUMO1R is a protein that in humans is encoded by the FOLR4 gene. Juno is a member of the folate receptor family and is GPI-anchored to the plasmalemma of the mammalian egg cell that recognizes its sperm-riding counterpart, IZUMO1, and facilitates fertilization. The protein was named after Juno, the Roman goddess of fertility and marriage.

<span class="mw-page-title-main">Beta-sandwich</span> Two opposing antiparallel beta sheets that commonly occur in proteins

Beta-sandwich or β-sandwich domains consisting of 80 to 350 amino acids occur commonly in proteins. They are characterized by two opposing antiparallel beta sheets (β-sheets). The number of strands found in such domains may differ from one protein to another. β-sandwich domains are subdivided in a variety of different folds. The immunoglobulin-type fold found in antibodies (Ig-fold) consists of a sandwich arrangement of 7-9 antiparallel β-strands arranged in two β-sheets with a Greek-key topology. The Greek-key topology is also found in Human Transthyretin. The jelly-roll topology is found in carbohydrate binding proteins such as concanavalin A and various lectins, in the collagen binding domain of Staphylococcus aureus Adhesin and in modules that bind fibronectin as found in Tenascin. The L-type lectin domain is a variation of the jelly roll fold. The C2 domain in its typical version (PKC-C2) is a β-sandwich composed of 8 beta-strands (β-strands).

The transforming growth factor beta (TGFβ) receptors are a family of serine/threonine kinase receptors involved in TGF beta signaling pathway. These receptors bind growth factor and cytokine signaling proteins in the TGF-beta family such as TGFβs, bone morphogenetic proteins (BMPs), growth differentiation factors (GDFs), activin and inhibin, myostatin, anti-Müllerian hormone (AMH), and NODAL.

Paul Michael Wassarman is an American biologist who has been Professor in the Dept. of Cell, Developmental, and Regenerative Biology at the Icahn School of Medicine at Mount Sinai since 1996. His laboratory identified and characterised proteins that make up the zona pellucida (ZP) of mammalian eggs and determined their role in fertilisation.

References

  1. 1 2 Bork P, Sander C (1992). "A large domain common to sperm receptors (Zp2 and Zp3) and TGF-beta type III receptor". FEBS Lett. 300 (3): 237–40. doi: 10.1016/0014-5793(92)80853-9 . PMID   1313375. S2CID   38778076.
  2. 1 2 Jovine L, Darie CC, Litscher ES, Wassarman PM (2005). "Zona pellucida domain proteins". Annu. Rev. Biochem. 74: 83–114. doi:10.1146/annurev.biochem.74.082803.133039. PMID   15952882.
  3. ↑ Jovine L, Qi H, Williams Z, Litscher E, Wassarman PM (2002). "The ZP domain is a conserved module for polymerization of extracellular proteins". Nat. Cell Biol. 4 (6): 457–61. doi:10.1038/ncb802. PMID   12021773. S2CID   11575790.
  4. 1 2 3 Monné M, Han L, Schwend T, Burendahl S, Jovine L (2008). "Crystal structure of the ZP-N domain of ZP3 reveals the core fold of animal egg coats". Nature. 456 (7222): 653–7. Bibcode:2008Natur.456..653M. doi:10.1038/nature07599. hdl: 11563/8930 . PMID   19052627. S2CID   4430083. PDB: 3D4C, 3D4G, 3EF7 ​
  5. 1 2 Han L, Monné M, Okumura, H, Schwend, T, Cherry, AL, Flot, D, Matsuda, T, Jovine, L (2010). "Insights into egg coat assembly and egg-sperm interaction from the X-ray structure of full-length ZP3". Cell. 143 (3): 404–15. doi: 10.1016/j.cell.2010.09.041 . hdl: 11563/8931 . PMID   20970175. S2CID   18583237. PDB: 3NK3, 3NK4 ​
  6. ↑ Lin SJ, Hu Y, Zhu J, Woodruff TK, Jardetzky TS (2011). "Structure of betaglycan zona pellucida (ZP)-C domain provides insights into ZP-mediated protein polymerization and TGF-beta binding". Proc Natl Acad Sci U S A. 108 (13): 5232–6. Bibcode:2011PNAS..108.5232L. doi: 10.1073/pnas.1010689108 . PMC   3069177 . PMID   21402931. PDB: 3QW9 ​
  7. ↑ Diestel U, Resch M, Meinhardt K, Weiler S, Hellmann TV, Mueller TD, Nickel J, Eichler J, Muller YA (2013). "Identification of a Novel TGF-β-Binding Site in the Zona Pellucida C-terminal (ZP-C) Domain of TGF-β-Receptor-3 (TGFR-3)". PLOS ONE. 8 (6): e67214. Bibcode:2013PLoSO...867214D. doi: 10.1371/journal.pone.0067214 . PMC   3695229 . PMID   23826237. PDB: 4AJV ​
  8. 1 2 Bokhove M, Nishimura K, Brunati M, Han L, de Sanctis D, Rampoldi L, Jovine L (2016). "A structured interdomain linker directs self-polymerization of human uromodulin". Proc. Natl. Acad. Sci. U.S.A. 113 (6): 1552–1557. Bibcode:2016PNAS..113.1552B. doi: 10.1073/pnas.1519803113 . PMC   4760807 . PMID   26811476. PDB: 4WRN, 5BUP ​
  9. ↑ Bokhove M, Jovine L (2018). "Structure of Zona Pellucida Module Proteins". Curr. Top. Dev. Biol. Current Topics in Developmental Biology. 130: 413–442. doi:10.1016/bs.ctdb.2018.02.007. ISBN   9780128098028. PMID   29853186.
  10. ↑ Saito T, Bokhove M, Croci R, Zamora-Caballero S, Han L, Letarte M, de Sanctis D, Jovine L (2017). "Structural Basis of the Human Endoglin-BMP9 Interaction: Insights into BMP Signaling and HHT1". Cell Reports. 19 (9): 1917–1928. doi:10.1016/j.celrep.2017.05.011. PMC   5464963 . PMID   28564608. PDB: 5HZV ​
  11. ↑ Jovine L, Qi H, Williams Z, Litscher ES, Wassarman PM (2004). "A duplicated motif controls assembly of zona pellucida domain proteins". Proc. Natl. Acad. Sci. U.S.A. 101 (16): 5922–7. Bibcode:2004PNAS..101.5922J. doi: 10.1073/pnas.0401600101 . PMC   395899 . PMID   15079052.
  12. ↑ Stsiapanava A, Xu C, Brunati M, Zamora-Caballero S, Schaeffer C, Bokhove M, Han L, Hebert H, Carroni M, Yasumasu S, Rampoldi L, Wu B, Jovine L (2020). "Cryo-EM structure of native human uromodulin, a zona pellucida module polymer". EMBO J. 39 (24): e106807. doi: 10.15252/embj.2020106807 . PMC   7737619 . PMID   33196145. bioRxiv   10.1101/2020.05.28.119206 PDB: 6TQK, 6TQL ​
  13. ↑ Stsiapanava A, Xu C, Nishio S, Han L, Yamakawa N, Carroni M, Tunyasuvunakool K, Jumper J, de Sanctis D, Wu B, Jovine L (2022). "Structure of the decoy module of human glycoprotein 2 and uromodulin and its interaction with bacterial adhesin FimH". Nat. Struct. Mol. Biol. 29 (3): 190–193. doi: 10.1038/s41594-022-00729-3 . PMC   8930769 . PMID   35273390. PDB: 7PFP, 7Q3N ​
  14. ↑ Callebaut I, Mornon JP, Monget P (2007). "Isolated ZP-N domains constitute the N-terminal extensions of Zona Pellucida proteins". Bioinformatics. 23 (15): 1871–1874. doi: 10.1093/bioinformatics/btm265 . PMID   17510169.
  15. ↑ Raj I, Sadat Al Hosseini H, Dioguardi E, Nishimura K, Han L, Villa A, de Sanctis D, Jovine L (2017). "Structural Basis of Egg Coat-Sperm Recognition at Fertilization". Cell. 169 (7): 1315–1326. doi:10.1016/j.cell.2017.05.033. PMC   5480393 . PMID   28622512. PDB: 5II4, 5II5, 5II6, 5MR2, 5IIC, 5IIA, 5IIB, 5MR3 ​
This article incorporates text from the public domain Pfam and InterPro: IPR001507


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