| IED ID | IndEnz0002012690 |
| Enzyme Type ID | protease012690 |
| Protein Name |
Zona pellucida sperm-binding protein 2 Zona pellucida glycoprotein 2 Zp-2 Zona pellucida protein A Cleaved into: Processed zona pellucida sperm-binding protein 2 |
| Gene Name | Zp2 Zp-2 Zpa |
| Organism | Mus musculus (Mouse) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Glires (Rodents and rabbits) Rodentia Myomorpha (mice and others) Muroidea Muridae Murinae Mus Mus Mus musculus (Mouse) |
| Enzyme Sequence | MARWQRKASVSSPCGRSIYRFLSLLFTLVTSVNSVSLPQSENPAFPGTLICDKDEVRIEFSSRFDMEKWNPSVVDTLGSEILNCTYALDLERFVLKFPYETCTIKVVGGYQVNIRVGDTTTDVRYKDDMYHFFCPAIQAETHEISEIVVCRRDLISFSFPQLFSRLADENQNVSEMGWIVKIGNGTRAHILPLKDAIVQGFNLLIDSQKVTLHVPANATGIVHYVQESSYLYTVQLELLFSTTGQKIVFSSHAICAPDLSVACNATHMTLTIPEFPGKLESVDFGQWSIPEDQWHANGIDKEATNGLRLNFRKSLLKTKPSEKCPFYQFYLSSLKLTFYFQGNMLSTVIDPECHCESPVSIDELCAQDGFMDFEVYSHQTKPALNLDTLLVGNSSCQPIFKVQSVGLARFHIPLNGCGTRQKFEGDKVIYENEIHALWENPPSNIVFRNSEFRMTVRCYYIRDSMLLNAHVKGHPSPEAFVKPGPLVLVLQTYPDQSYQRPYRKDEYPLVRYLRQPIYMEVKVLSRNDPNIKLVLDDCWATSSEDPASAPQWQIVMDGCEYELDNYRTTFHPAGSSAAHSGHYQRFDVKTFAFVSEARGLSSLIYFHCSALICNQVSLDSPLCSVTCPASLRSKREANKEDTMTVSLPGPILLLSDVSSSKGVDPSSSEITKDIIAKDIASKTLGAVAALVGSAVILGFICYLYKKRTIRFNH |
| Enzyme Length | 713 |
| Uniprot Accession Number | P20239 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: Component of the zona pellucida, an extracellular matrix surrounding oocytes which mediates sperm binding, induction of the acrosome reaction and prevents post-fertilization polyspermy. The zona pellucida is composed of 3 to 4 glycoproteins, ZP1, ZP2, ZP3, and ZP4. ZP2 may act as a secondary sperm receptor. {ECO:0000269|PubMed:22472438}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Beta strand (18); Chain (2); Disulfide bond (7); Domain (1); Glycosylation (7); Helix (5); Mutagenesis (1); Propeptide (1); Region (1); Signal peptide (1); Site (2); Topological domain (2); Transmembrane (1); Turn (2) |
| Keywords | 3D-structure;Cell membrane;Cleavage on pair of basic residues;Direct protein sequencing;Disulfide bond;Extracellular matrix;Fertilization;Glycoprotein;Membrane;Receptor;Reference proteome;Secreted;Signal;Transmembrane;Transmembrane helix |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: [Processed zona pellucida sperm-binding protein 2]: Zona pellucida {ECO:0000269|PubMed:12799386, ECO:0000269|PubMed:17559063, ECO:0000269|PubMed:22472438, ECO:0000269|PubMed:3845123}.; SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22472438}; Single-pass type I membrane protein {ECO:0000255}. |
| Modified Residue | |
| Post Translational Modification | PTM: Proteolytically cleaved before the transmembrane segment to yield the secreted ectodomain incorporated in the zona pellucida. {ECO:0000269|PubMed:22472438, ECO:0000269|PubMed:26811476}.; PTM: Proteolytically cleaved in the N-terminal part by the metalloendopeptidase ASTL exocytosed from cortical granules after fertilization, yielding a N-terminal peptide of about 30 kDa which remains covalently attached to the C-terminal peptide via disulfide bond(s). This cleavage may play an important role in the post-fertilization block to polyspermy. Additional proteolytically cleavage of the N-terminal peptide of 30 kDa occurs in one-cell and two-cell embryos. {ECO:0000269|PubMed:22472438}.; PTM: N-glycosylated. {ECO:0000269|PubMed:12799386}.; PTM: O-glycosylated; contains sulfate-substituted glycans. {ECO:0000269|PubMed:12799386}. |
| Signal Peptide | SIGNAL 1..34; /evidence="ECO:0000269|PubMed:12799386, ECO:0000269|PubMed:1690843" |
| Structure 3D | X-ray crystallography (2) |
| Cross Reference PDB | 5BUP; 5II6; |
| Mapped Pubmed ID | 10441734; 10533707; 10729725; 10793136; 11023867; 11245577; 11389548; 11739644; 11906903; 12852850; 15317747; 15326356; 15970507; 16141072; 16416028; 16690745; 1673105; 17047254; 17926344; 18354036; 19014927; 19052627; 1968044; 20616279; 20970175; 20979237; 21378311; 22685254; 22734000; 2320565; 23417405; 24357321; 24934154; 26160904; 26267271; 27065194; 27193969; 28619824; 28646452; 30122633; 31598710; 31657143; 32212159; 32558204; 6793422; 6819087; 6928658; 7487932; 7512897; 7601475; 7607680; 7635043; 7774957; 7822321; 7841460; 7896292; 7920633; 8344459; 8385033; 8390964; 8570653; 8575777; 8636124; 8747928; 8833147; 9237231; 9988213; |
| Motif | |
| Gene Encoded By | |
| Mass | 80,210 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |