| IED ID | IndEnz0002010525 |
| Enzyme Type ID | protease010525 |
| Protein Name |
Mastin EC 3.4.21.- Mast cell protease 3 DMP MCP-3 dMCP-3 Mastocytoma protease |
| Gene Name | |
| Organism | Canis lupus familiaris (Dog) (Canis familiaris) |
| 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 Laurasiatheria Carnivora Caniformia Canidae (dog coyote wolf fox) Canis Canis lupus (Gray wolf) Canis lupus familiaris (Dog) (Canis familiaris) |
| Enzyme Sequence | MLWLLVLTAPWLGGSVPISPDPGLRHEQVGIVGGCKVPARRYPWQVSLRFHGMGSGQWQHICGGSLIHPQWVLTAAHCVELEGLEAATLRVQVGQLRLYDHDQLCNVTEIIRHPNFNMSWYGWDSADIALLKLEAPLTLSEDVNLVSLPSPSLIVPPGMLCWVTGWGDIADHTPLPPPYHLQEVEVPIVGNRECNCHYQTILEQDDEVIKQDMLCAGSEGHDSCQMDSGGPLVCRWKCTWIQVGVVSWGYGCGYNLPGVYARVTSYVSWIHQHIPLSPGP |
| Enzyme Length | 280 |
| Uniprot Accession Number | P19236 |
| Absorption | |
| Active Site | ACT_SITE 77; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 127; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 228; /note=Charge relay system; /evidence=ECO:0000250 |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by leupeptin and bis(5-amidino-2-benzimidazolyl)methane (BABIM). {ECO:0000269|PubMed:7768912}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.21.- |
| Enzyme Function | FUNCTION: Trypsin-like serine protease. Has a preference for extended substrates with basic residues at the P1 position; Arg is preferred over Lys. Active towards calcitonin gene-related peptide and gelatin. Not active towards substance P, vasoactive intestinal peptide, type I collagen or azocasein. {ECO:0000269|PubMed:15708374}. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.0-8.5.; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Disulfide bond (4); Domain (1); Glycosylation (2); Propeptide (1); Sequence conflict (3); Signal peptide (1) |
| Keywords | Cytoplasm;Direct protein sequencing;Disulfide bond;Glycoprotein;Hydrolase;Protease;Reference proteome;Serine protease;Signal;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:8144904}. |
| Modified Residue | |
| Post Translational Modification | PTM: N-glycosylated. {ECO:0000269|PubMed:7768912}. |
| Signal Peptide | SIGNAL 1..15; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 31,025 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |