| IED ID | IndEnz0002006318 |
| Enzyme Type ID | protease006318 |
| Protein Name |
Matrix metalloproteinase-16 MMP-16 EC 3.4.24.- Membrane-type matrix metalloproteinase 3 MT-MMP 3 MTMMP3 Membrane-type-3 matrix metalloproteinase MT3-MMP MT3MMP |
| Gene Name | Mmp16 |
| Organism | Rattus norvegicus (Rat) |
| 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 Rattus Rattus norvegicus (Rat) |
| Enzyme Sequence | MILLAFSSGRRLDFVHRSGVFFFQTLLWILCATVCGTEQYFNVEVWLQKYGYLPPTDPRMSVLRSAETMQSALAAMQQFYGINMTGKVDRNTIDWMKKPRCGVPDQTRGSSKFNIRRKRYALTGQKWQHKHITYSIKNVTPKVGDPETRRAIRRAFDVWQNVTPLTFEEVPYSELENGKRDVDITIIFASGFHGDRSPFDGEGGFLAHAYFPGPGIGGDTHFDSDEPWTLGNPNHDGNDLFLVAVHELGHALGLEHSNDPTAIMAPFYQYMETDNFKLPNDDLQGIQKIYGPPDKIPPPTRPLPTVPPHRSVPPADPRKNDRPKPPRPPTGRPSYPGAKPNICDGNFNTLAILRREMFVFKDQWFWRVRNNRVMDGYPMQITYFWRGLPPSIDAVYENSDGNFVFFKGNKYWVFKDTTLQPGYPHDLITLGNGIPPHGIDSAIWWEDVGKTYFFKGDRYWRYSEEMKTMDPGYPKPITIWKGIPESPQGAFVHKENGFTYFYKGKEYWKFNNQILKVEPGYPRSILKDFMGCDGPTDRDKEGLSPPDDVDIVIKLDNTASTVKAIAIVIPCILALCLLVLVYTVFQFKRKGTPRHILYCKRSMQEWV |
| Enzyme Length | 607 |
| Uniprot Accession Number | O35548 |
| Absorption | |
| Active Site | ACT_SITE 247; /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, such as collagen type III and fibronectin. Activates progelatinase A. Involved in the matrix remodeling of blood vessels. The short isoform efficiently converts progelatinase A to the intermediate form but not to the mature one. It has no effect on type I, II, IV and V collagen. However, upon interaction with CSPG4, it may be involved in degradation and invasion of type I collagen by melanoma cells. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Alternative sequence (1); Chain (1); Compositional bias (1); Disulfide bond (1); Glycosylation (1); Metal binding (16); Motif (1); Propeptide (1); Region (1); Repeat (4); Signal peptide (1); Topological domain (2); Transmembrane (1) |
| Keywords | Alternative splicing;Calcium;Cell membrane;Cleavage on pair of basic residues;Collagen degradation;Disulfide bond;Extracellular matrix;Glycoprotein;Hydrolase;Membrane;Metal-binding;Metalloprotease;Protease;Reference proteome;Repeat;Secreted;Signal;Transmembrane;Transmembrane helix;Zinc;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}; Extracellular side {ECO:0000305}. Note=Localized at the cell surface of melanoma cells. {ECO:0000250}.; SUBCELLULAR LOCATION: [Isoform Short]: 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..31; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 18784838; 23103411; |
| Motif | MOTIF 99..106; /note=Cysteine switch; /evidence=ECO:0000250 |
| Gene Encoded By | |
| Mass | 69,624 |
| Kinetics | |
| Metal Binding | METAL 101; /note=Zinc 1; in inhibited form; /evidence=ECO:0000250; METAL 183; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000250; METAL 193; /note=Zinc 1; /evidence=ECO:0000250; METAL 195; /note=Zinc 1; /evidence=ECO:0000250; METAL 200; /note=Calcium 2; /evidence=ECO:0000250; METAL 201; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250; METAL 203; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250; METAL 205; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250; METAL 215; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000250; METAL 217; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000250; METAL 219; /note=Calcium 1; /evidence=ECO:0000250; METAL 223; /note=Calcium 2; /evidence=ECO:0000250; METAL 226; /note=Calcium 2; /evidence=ECO:0000250; METAL 246; /note=Zinc 2; catalytic; /evidence=ECO:0000250; METAL 250; /note=Zinc 2; catalytic; /evidence=ECO:0000250; METAL 256; /note=Zinc 2; catalytic; /evidence=ECO:0000250 |
| Rhea ID | |
| Cross Reference Brenda |