| IED ID | IndEnz0002016324 |
| Enzyme Type ID | protease016324 |
| Protein Name |
Matrix metalloproteinase-17 MMP-17 EC 3.4.24.- Membrane-type matrix metalloproteinase 4 MT-MMP 4 MTMMP4 Membrane-type-4 matrix metalloproteinase MT4-MMP MT4MMP |
| Gene Name | Mmp17 Mt4mmp |
| 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 | MGRRPRGPGSPRGPGPPRPGPGLPPLLLVLALAAHGGCAAPAPRAEDLSLGVEWLSRFGYLPPADPASGQLQTQEELSKAITAMQQFGGLETTGILDEATLALMKTPRCSLPDLPPGAQSRRKRQTPPPTKWSKRNLSWRVRTFPRDSPLGRDTVRALMYYALKVWSDITPLNFHEVAGNAADIQIDFSKADHNDGYPFDGPGGTVAHAFFPGDHHTAGDTHFDDDEPWTFRSSDAHGMDLFAVAVHEFGHAIGLSHVAAPSSIMQPYYQGPVGDPLRYGLPYEDRVRVWQLYGVRESVSPTAQLDTPEPEEPPLLPEPPNNRSSTPPQKDVPHRCTAHFDAVAQIRGEAFFFKGKYFWRLTRDRHLVSLQPAQMHRFWRGLPLHLDSVDAVYERTSDHKIVFFKGDRYWVFKDNNVEEGYPRPVSDFSLPPGGIDAVFSWAHNDRTYFFKDQLYWRYDDHTRRMDPGYPAQGPLWRGVPSMLDDAMRWSDGASYFFRGQEYWKVLDGELEAAPGYPQSTARDWLVCGEPLADAEDVGPGPQGRSGAQDGLAVCSCTSDAHRLALPSLLLLTPLLWGL |
| Enzyme Length | 578 |
| Uniprot Accession Number | Q9R0S3 |
| Absorption | |
| Active Site | ACT_SITE 248 |
| 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, such as fibrin. May be involved in the activation of membrane-bound precursors of growth factors or inflammatory mediators, such as tumor necrosis factor-alpha. May also be involved in tumoral process. Not obvious if able to proteolytically activate progelatinase A. Does not hydrolyze collagen types I, II, III, IV and V, gelatin, fibronectin, laminin, decorin nor alpha1-antitrypsin. {ECO:0000269|PubMed:10799478}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Compositional bias (1); Disulfide bond (1); Glycosylation (2); Lipidation (1); Metal binding (4); Motif (1); Mutagenesis (1); Propeptide (2); Region (3); Repeat (4); Sequence conflict (2); Signal peptide (1) |
| Keywords | Calcium;Cell membrane;Cleavage on pair of basic residues;Disulfide bond;Extracellular matrix;GPI-anchor;Glycoprotein;Hydrolase;Lipoprotein;Membrane;Metal-binding;Metalloprotease;Protease;Reference proteome;Repeat;Secreted;Signal;Zinc;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor; Extracellular side. Secreted, extracellular space, extracellular matrix. |
| Modified Residue | |
| Post Translational Modification | PTM: The precursor is cleaved by a furin endopeptidase. {ECO:0000250}. |
| Signal Peptide | SIGNAL 1..39; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 10640822; 12466851; 15142957; 15472464; 15734845; 15895410; 16141072; 16686598; 17825051; 19426156; 21267068; 21347258; 22407321; 23421805; 23431145; 25348153; 25794647; 25963716; 28926609; 29500407; 30208054; |
| Motif | MOTIF 107..114; /note=Cysteine switch; /evidence=ECO:0000250 |
| Gene Encoded By | |
| Mass | 64,333 |
| Kinetics | |
| Metal Binding | METAL 109; /note=Zinc; in inhibited form; /evidence=ECO:0000250; METAL 247; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; METAL 251; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; METAL 257; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095 |
| Rhea ID | |
| Cross Reference Brenda |