Detail Information for IndEnz0002003701
IED ID IndEnz0002003701
Enzyme Type ID protease003701
Protein Name Astacin-like metalloendopeptidase
EC 3.4.-.-
Oocyte astacin
Ovastacin
Sperm acrosomal SLLP1-binding protein
Gene Name Astl Sas1b
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 MGIMGSLWPWILTMLSLLGLSMGAPSASRCSGVCSTSVPEGFTPEGSPVFQDKDIPAINQGLISEETPESSFLVEGDIIRPSPFRLLSVTNNKWPKGVGGFVEIPFLLSRKYDELSRRVIMDAFAEFERFTCIRFVAYHGQRDFVSILPMAGCFSGVGRSGGMQVVSLAPTCLRKGRGIVLHELMHVLGFWHEHSRADRDRYIQVNWNEILPGFEINFIKSRSTNMLVPYDYSSVMHYGRFAFSWRGQPTIIPLWTSSVHIGQRWNLSTSDITRVCRLYNCSRSVPDSHGRGFEAQSDGSSLTPASISRLQRLLEALSEESGSSAPSGSRTGGQSIAGLGNSQQGWEHPPQSTFSVGALARPPQMLADASKSGPGAGADSLSLEQFQLAQAPTVPLALFPEARDKPAPIQDAFERLAPLPGGCAPGSHIREVPRD
Enzyme Length 435
Uniprot Accession Number Q6HA09
Absorption
Active Site ACT_SITE 183; /evidence=ECO:0000255|PROSITE-ProRule:PRU01211
Activity Regulation ACTIVITY REGULATION: Inhibited by wide spectrum metalloproteinase inhibitor batimastat (BB-94). Also inhibited by EDTA (By similarity). {ECO:0000250|UniProtKB:Q6HA08}.
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number 3.4.-.-
Enzyme Function FUNCTION: Oocyte-specific oolemmal receptor involved in sperm and egg adhesion and fertilization. Plays a role in the polyspermy inhibition. Probably acts as a protease for the post-fertilization cleavage of ZP2. Cleaves the sperm-binding ZP2 at the surface of the zona pellucida after fertilization and cortical granule exocytosis, rendering the zona pellucida unable to support further sperm binding. {ECO:0000269|PubMed:22206759, ECO:0000269|PubMed:22472438}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (1); Alternative sequence (4); Chain (1); Compositional bias (1); Disulfide bond (2); Domain (1); Metal binding (3); Region (1); Sequence conflict (6); Signal peptide (1)
Keywords Alternative splicing;Cell membrane;Cytoplasm;Cytoplasmic vesicle;Disulfide bond;Fertilization;Hydrolase;Membrane;Metal-binding;Metalloprotease;Protease;Reference proteome;Signal;Zinc;Zymogen
Interact With
Induction INDUCTION: Up-regulated by superovulation. {ECO:0000269|PubMed:15087446}.
Subcellular Location SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22206759, ECO:0000269|PubMed:22472438}. Cell membrane {ECO:0000269|PubMed:22206759}. Cytoplasmic vesicle, secretory vesicle, Cortical granule {ECO:0000269|PubMed:22472438}. Note=Probably exocytosed from cortical granules during post-fertilization. Detected throughout the ooplasm of germinal vesicle stage oocytes in early bilaminar secondary follicles at postnatal (PN) day 3. Detected in the microvillar domain of the oolemma in arrested ovulated secondary oocytes and in the first polar body prior to fertilization. Upon fertilization, detected in the perivitelline space (PVS) and occasionally on the oolemma in 2-cell through morulae stages. Colocalizes with SPACA3 at the microvillar domain of the oolemma and in the perivitelline space (PVS). {ECO:0000269|PubMed:22472438}.
Modified Residue
Post Translational Modification
Signal Peptide SIGNAL 1..23; /evidence=ECO:0000255
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 10725249; 21267068; 21677750; 28114310; 28911209; 30122633;
Motif
Gene Encoded By
Mass 47,455
Kinetics
Metal Binding METAL 182; /note=Zinc; via tele nitrogen; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU01211; METAL 186; /note=Zinc; via tele nitrogen; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU01211; METAL 192; /note=Zinc; via tele nitrogen; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU01211
Rhea ID
Cross Reference Brenda