| IED ID | IndEnz0002010210 |
| Enzyme Type ID | protease010210 |
| Protein Name |
Spermosin EC 3.4.21.99 Cleaved into: Spermosin L1 light chain; Spermosin L2 light chain; Spermosin heavy chain |
| Gene Name | |
| Organism | Halocynthia roretzi (Sea squirt) (Cynthia roretzi) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Tunicata Ascidiacea Stolidobranchia Pyuridae Halocynthia Halocynthia roretzi (Sea squirt) (Cynthia roretzi) |
| Enzyme Sequence | MAAINVIFISGAIALFALTGSCSESTNPFTNKPYATQNPYSPPQTNQPTKRPYQPGPAPTPAPYIPQKTNPPTKRPLNPTPSPTAKPPSENSESENSEGPVLIEEDHFTVDANFKCGIPPVEPDLKKGKIVGGAEAVPNSWPYAAAFGTYDISGGKLEVSQMCGSTIITPRHALTAAHCFMMDPDIDQTYYIFMGLHDETTYKGVRPNKIVGVRYHPKTNVFTDDPWLVYDFAILTLRKKVIANFAWNYACLPQPKKIPPEGTICWSVGWGVTQNTGGDNVLKQVAIDLVSEKRCKEEYRSTITSKSTICGGTTPGQDTCQGDSGGPLFCKEDGKWYLQGIVSYGPSVCGSGPMAAYAAVAYNLEWLCCYMPNLPSCEDIECDESGEN |
| Enzyme Length | 388 |
| Uniprot Accession Number | Q966V2 |
| Absorption | |
| Active Site | ACT_SITE 178; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:Q9CR35; ACT_SITE 231; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:Q9CR35; ACT_SITE 324; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:Q9CR35 |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by peptidyl-argininals wth Pro in the P2 position, diisopropyl fluorophosphate, phenylmethanesulfonyl fluoride, leupeptin, antipain, soybean trypsin inhibitor, aprotinin, ovomucoid, valyl-prolyl-arginyl-chloromethane, glycyl-valyl-arginyl-chloromethane, p-aminobenzamidine, benzamidine, zinc chloride and mercuric chloride. {ECO:0000269|PubMed:6365918, ECO:0000269|PubMed:6381175, ECO:0000269|PubMed:8914083}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Hydrolyzes arginyl bonds, preferably with Pro in the P2 position.; EC=3.4.21.99; Evidence={ECO:0000269|PubMed:6365918, ECO:0000269|PubMed:8914083}; |
| DNA Binding | |
| EC Number | 3.4.21.99 |
| Enzyme Function | FUNCTION: Trypsin-like protease with a narrow substrate specificity. Preferentially hydrolyzes substrates with Pro in the P2 position and Val in the P3 position. Plays a role in fertilization. {ECO:0000269|PubMed:6365918, ECO:0000269|PubMed:8670234, ECO:0000269|PubMed:8914083}. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.5-9.0. {ECO:0000269|PubMed:6365918}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (3); Compositional bias (2); Disulfide bond (5); Domain (1); Region (1); Signal peptide (1) |
| Keywords | Direct protein sequencing;Disulfide bond;Hydrolase;Protease;Secreted;Serine protease;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:8670234}. Note=Localized on the sperm head. Released into the surrounding seawater in response to the sperm reaction, a large proportion remains associated with the sperm cell surface. {ECO:0000269|PubMed:8670234}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..22; /evidence=ECO:0000269|PubMed:11856325 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 42,145 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=145 uM for Boc-Val-Pro-Arg-MCA {ECO:0000269|PubMed:6365918}; |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.4.21.99; |