| IED ID | IndEnz0002003866 |
| Enzyme Type ID | protease003866 |
| Protein Name |
Mast cell protease 4 mMCP-4 EC 3.4.21.- MSMCP Myonase Serosal mast cell protease |
| Gene Name | Mcpt4 |
| 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 | MQALLFLMALLLPSGAGAEEIIGGVESRPHSRPYMAHLEITTERGFTATCGGFLITRQFVMTAAHCSGREITVTLGAHDVSKTESTQQKIKVEKQIVHPKYNFYSNLHDIMLLKLQKKAKETPSVNVIPLPRPSDFIKPGKMCRAAGWGRTGVTEPTSDTLREVKLRIMDKEACKNYWHYDYNLQVCVGSPRKKRSAYKGDSGGPLLCAGVAHGIVSYGRGDAKPPAVFTRISSYVPWINRVIKGE |
| Enzyme Length | 246 |
| Uniprot Accession Number | P21812 |
| Absorption | |
| Active Site | ACT_SITE 65; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 109; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 202; /note=Charge relay system; /evidence=ECO:0000250 |
| Activity Regulation | ACTIVITY REGULATION: Completely inhibited by serine protease inhibitors such as chymostatin, diisopropylfluorophosphate and phenylmethylsulfonyl fluoride, but not by p-tosyl-L-phenylalanine chloromethyl ketone, p-tosyl-L-lysine chloromethyl ketone, pepstatin, E-64, EDTA or o-phenanthroline. Also inhibited by lima bean trypsin inhibitor, soy bean trypsin inhibitor and human plasma alpha1-antichymotrypsin. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.21.- |
| Enzyme Function | FUNCTION: Has chymotrypsin-like activity. Hydrolyzes the amide bonds of synthetic substrates having Tyr and Phe residues at the P1 position. Preferentially hydrolyzes the 'Tyr-4-|-Ile-5' bond of angiotensin I and the 'Phe-20-|-Ala-21' bond of amyloid beta-protein, and is less active towards the 'Phe-8-|-His-9' bond of angiotensin I and the 'Phe-4-|-Ala-5' and 'Tyr-10-|-Glu-11' bonds of amyloid beta-protein. Involved in thrombin regulation and fibronectin processing. {ECO:0000269|PubMed:12900518, ECO:0000269|PubMed:9538257}. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 9 at high salt concentrations.; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Disulfide bond (3); Domain (1); Erroneous initiation (1); Natural variant (3); Propeptide (1); Signal peptide (1) |
| Keywords | Direct protein sequencing;Disulfide bond;Hydrolase;Protease;Reference proteome;Serine protease;Signal;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..18 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 10466726; 10737774; 12204111; 1372640; 14578624; 15173164; 15615702; 16141072; 16807745; 16807746; 1688433; 18376408; 19010978; 19720934; 19841188; 1995638; 20018751; 20530261; 20864640; 21076070; 21267068; 21880713; 21926462; 22232213; 22901752; 23193170; 23235745; 23515052; 23596057; 23624557; 23975861; 24075853; 24257755; 24453258; 24523504; 24814421; 26976326; 27274047; 27936149; 27939674; 28916188; 30571485; 30639224; 30742008; 30842526; 31248979; 31866111; 33154104; 7959952; 8098710; 9360993; 9541598; 9626500; |
| Motif | |
| Gene Encoded By | |
| Mass | 27,204 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.4.21.39; |