| IED ID | IndEnz0002002699 |
| Enzyme Type ID | protease002699 |
| Protein Name |
Matrix metalloproteinase-15 MMP-15 EC 3.4.24.- Membrane-type matrix metalloproteinase 2 MT-MMP 2 MTMMP2 Membrane-type-2 matrix metalloproteinase MT2-MMP MT2MMP |
| Gene Name | Mmp15 |
| 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 | MGSDRSALGRPGCTGSCLSSRASLLPLLLVLLDCLGHGTASKDAEVYAAENWLRLYGYLPQPSRHMSTMRSAQILASALAEMQSFYGIPVTGVLDEETKTWMKRPRCGVPDQFGVHVKANLRRRRKRYTLTGKAWNNYHLTFSIQNYTEKLGWYNSMEAVRRAFQVWEQVTPLVFQEVSYDDIRLRRRAEADIMVLFASGFHGDSSPFDGVGGFLAHAYFPGPGLGGDTHFDADEPWTFSSTDLHGISLFLVAVHELGHALGLEHSSNPSAIMAPFYQWMDTDNFQLPEDDLRGIQQLYGSPDGKPQPTRPLPTVRPRRPGRPDHQPPRPPQPPHPGGKPERPPKPGPPPQPRATERPDQYGPNICDGNFDTVAVLRGEMFVFKGRWFWRVRHNRVLDNYPMPIGHFWRGLPGNISAAYERQDGHFVFFKGNRYWLFREANLEPGYPQPLSSYGTDIPYDRIDTAIWWEPTGHTFFFQADRYWRFNEETQHGDPGYPKPISVWQGIPTSPKGAFLSNDAAYTYFYKGTKYWKFNNERLRMEPGHPKSILRDFMGCQEHVEPRSRWPDVARPPFNPNGGAEPEADGDSKEENAGDKDEGSRVVVQMEEVVRTVNVVMVLVPLLLLLCILGLAFALVQMQRKGAPRMLLYCKRSLQEWV |
| Enzyme Length | 657 |
| Uniprot Accession Number | O54732 |
| Absorption | |
| Active Site | ACT_SITE 256; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.24.- |
| Enzyme Function | FUNCTION: Endopeptidase that degrades various components of the extracellular matrix. May activate progelatinase A. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Compositional bias (2); Disulfide bond (1); Glycosylation (2); Metal binding (4); Motif (1); Propeptide (1); Region (2); Repeat (4); Signal peptide (1); Topological domain (2); Transmembrane (1) |
| Keywords | Calcium;Cleavage on pair of basic residues;Disulfide bond;Glycoprotein;Hydrolase;Membrane;Metal-binding;Metalloprotease;Protease;Reference proteome;Repeat;Signal;Transmembrane;Transmembrane helix;Zinc;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}; Extracellular side {ECO:0000305}. |
| Modified Residue | |
| Post Translational Modification | PTM: The precursor is cleaved by a furin endopeptidase. {ECO:0000250}. |
| Signal Peptide | SIGNAL 1..36; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 10949577; 11217851; 12466851; 14681479; 15734845; 15895410; 16093645; 16113801; 16602821; 19538736; 19915148; 20858856; 21267068; 21677750; 21920357; 22008794; 22967998; 23421805; 24194600; 25794647; 27626380; 27633994; 29196321; 29329412; 30269950; 31600777; 31609468; 9048885; 9653660; |
| Motif | MOTIF 105..112; /note=Cysteine switch; /evidence=ECO:0000250 |
| Gene Encoded By | |
| Mass | 74,666 |
| Kinetics | |
| Metal Binding | METAL 107; /note=Zinc; in inhibited form; /evidence=ECO:0000250; METAL 255; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; METAL 259; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; METAL 265; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095 |
| Rhea ID | |
| Cross Reference Brenda | 3.4.24.B5; |