| IED ID | IndEnz0002006530 |
| Enzyme Type ID | protease006530 |
| Protein Name |
Matrix metalloproteinase-24 MMP-24 EC 3.4.24.- Matrix metalloproteinase-21 MMP-21 Membrane-type matrix metalloproteinase 5 MT-MMP 5 MTMMP5 Membrane-type-5 matrix metalloproteinase MT5-MMP MT5MMP Cleaved into: Processed matrix metalloproteinase-24 |
| Gene Name | Mmp24 Mmp21 Mt5mmp |
| 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 | MPRSRGGRAAPGQASRWSGWRAPGRLLPLLPALCCLAAAAGAGKPAGADAPFAGQNWLKSYGYLLPYESRASALHSGKALQSAVSTMQQFYGIPVTGVLDQTTIEWMKKPRCGVPDHPHLSRRRRNKRYALTGQKWRQKHITYSIHNYTPKVGELDTRKAIRQAFDVWQKVTPLTFEEVPYHEIKSDRKEADIMIFFASGFHGDSSPFDGEGGFLAHAYFPGPGIGGDTHFDSDEPWTLGNANHDGNDLFLVAVHELGHALGLEHSNDPSAIMAPFYQYMETHNFKLPQDDLQGIQKIYGPPAEPLEPTRPLPTLPVRRIHSPSERKHERHPRPPRPPLGDRPSTPGAKPNICDGNFNTVALFRGEMFVFKDRWFWRLRNNRVQEGYPMQIEQFWKGLPARIDAAYERADGRFVFFKGDKYWVFKEVTVEPGYPHSLGELGSCLPREGIDTALRWEPVGKTYFFKGERYWRYSEERRATDPGYPKPITVWKGIPQAPQGAFISKEGYYTYFYKGRDYWKFDNQKLSVEPGYPRNILRDWMGCKQKEVERRKERRLPQDDVDIMVTIDDVPGSVNAVAVVVPCTLSLCLLVLLYTIFQFKNKAGPQPVTYYKRPVQEWV |
| Enzyme Length | 618 |
| Uniprot Accession Number | Q9R0S2 |
| Absorption | |
| Active Site | ACT_SITE 256; /evidence="ECO:0000255|PROSITE-ProRule:PRU10095, ECO:0000269|PubMed:10085137" |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.24.- |
| Enzyme Function | FUNCTION: Metalloprotease that mediates cleavage of N-cadherin (CDH2) and acts as a regulator of neuro-immune interactions and neural stem cell quiescence (PubMed:19805319, PubMed:24952463). Involved in cell-cell interactions between nociceptive neurites and mast cells, possibly by mediating cleavage of CDH2, thereby acting as a mediator of peripheral thermal nociception and inflammatory hyperalgesia (PubMed:19805319). Key regulator of neural stem cells quiescence by mediating cleavage of CDH2, affecting CDH2-mediated anchorage of neural stem cells to ependymocytes in the adult subependymal zone, leading to modulate their quiescence (PubMed:24952463). May play a role in axonal growth (PubMed:11714638). Able to activate progelatinase A. May also be a proteoglycanase involved in degradation of proteoglycans, such as dermatan sulfate and chondroitin sulfate proteoglycans. Cleaves partially fibronectin, but not collagen type I, nor laminin (PubMed:10622708). {ECO:0000269|PubMed:10622708, ECO:0000269|PubMed:11714638, ECO:0000269|PubMed:19805319, ECO:0000269|PubMed:24952463}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (2); Compositional bias (1); Disulfide bond (1); Metal binding (4); Motif (2); Mutagenesis (3); Propeptide (1); Region (1); Repeat (4); Sequence conflict (9); Signal peptide (1); Site (1); Topological domain (2); Transmembrane (1) |
| Keywords | Calcium;Cell adhesion;Cell membrane;Cleavage on pair of basic residues;Disulfide bond;Extracellular matrix;Golgi apparatus;Hydrolase;Membrane;Metal-binding;Metalloprotease;Protease;Reference proteome;Repeat;Secreted;Signal;Transmembrane;Transmembrane helix;Zinc;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: [Matrix metalloproteinase-24]: Cell membrane; Single-pass type I membrane protein. Golgi apparatus, trans-Golgi network membrane; Single-pass type I membrane protein. Note=Recycled back to the plasma membrane through the trans-Golgi network via interaction with APBA3. {ECO:0000269|PubMed:14990567}.; SUBCELLULAR LOCATION: [Processed matrix metalloproteinase-24]: Secreted, extracellular space, extracellular matrix. Note=Also shed from cell surface as soluble proteinase, by a proteolytic cleavage. {ECO:0000269|PubMed:11470782}. |
| Modified Residue | |
| Post Translational Modification | PTM: Cleaved by a furin endopeptidase in the trans-Golgi network. |
| Signal Peptide | SIGNAL 1..41; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 10471807; 10640822; 10725249; 10949577; 11217851; 12466851; 14741353; 15734845; 16495457; 16602821; 17114464; 18799693; 21267068; 23421805; 24718611; 25794647; 26202697; 26322584; 28119565; 29196321; |
| Motif | MOTIF 110..117; /note=Cysteine switch; /evidence=ECO:0000250; MOTIF 616..618; /note=PDZ-binding |
| Gene Encoded By | |
| Mass | 70,460 |
| Kinetics | |
| Metal Binding | METAL 112; /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 |