| IED ID | IndEnz0002004578 |
| Enzyme Type ID | protease004578 |
| Protein Name |
Matrix metalloproteinase-16 MMP-16 EC 3.4.24.- MMP-X2 Membrane-type matrix metalloproteinase 3 MT-MMP 3 MTMMP3 Membrane-type-3 matrix metalloproteinase MT3-MMP MT3MMP |
| Gene Name | MMP16 C8orf57 MMPX2 |
| Organism | Homo sapiens (Human) |
| 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 Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human) |
| Enzyme Sequence | MILLTFSTGRRLDFVHHSGVFFLQTLLWILCATVCGTEQYFNVEVWLQKYGYLPPTDPRMSVLRSAETMQSALAAMQQFYGINMTGKVDRNTIDWMKKPRCGVPDQTRGSSKFHIRRKRYALTGQKWQHKHITYSIKNVTPKVGDPETRKAIRRAFDVWQNVTPLTFEEVPYSELENGKRDVDITIIFASGFHGDSSPFDGEGGFLAHAYFPGPGIGGDTHFDSDEPWTLGNPNHDGNDLFLVAVHELGHALGLEHSNDPTAIMAPFYQYMETDNFKLPNDDLQGIQKIYGPPDKIPPPTRPLPTVPPHRSIPPADPRKNDRPKPPRPPTGRPSYPGAKPNICDGNFNTLAILRREMFVFKDQWFWRVRNNRVMDGYPMQITYFWRGLPPSIDAVYENSDGNFVFFKGNKYWVFKDTTLQPGYPHDLITLGSGIPPHGIDSAIWWEDVGKTYFFKGDRYWRYSEEMKTMDPGYPKPITVWKGIPESPQGAFVHKENGFTYFYKGKEYWKFNNQILKVEPGYPRSILKDFMGCDGPTDRVKEGHSPPDDVDIVIKLDNTASTVKAIAIVIPCILALCLLVLVYTVFQFKRKGTPRHILYCKRSMQEWV |
| Enzyme Length | 607 |
| Uniprot Accession Number | P51512 |
| Absorption | |
| Active Site | ACT_SITE 247 |
| Activity Regulation | ACTIVITY REGULATION: TIMP-2 shows little inhibitory activity compared to TIMP-1. TIMP-1 seems to have less binding affinity than TIMP-2 for the short isoform. |
| 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. Isoform short cleaves fibronectin and also collagen type III, but at lower rate. 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. {ECO:0000269|PubMed:11278606}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Alternative sequence (2); Beta strand (11); Chain (1); Compositional bias (1); Disulfide bond (1); Glycosylation (1); Helix (3); Metal binding (16); Motif (1); Propeptide (1); Region (1); Repeat (4); Sequence conflict (1); Signal peptide (1); Topological domain (2); Transmembrane (1); Turn (2) |
| Keywords | 3D-structure;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: [Isoform Long]: 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.; SUBCELLULAR LOCATION: [Isoform Short]: Secreted, extracellular space, extracellular matrix. Cell surface. Note=Localized at the cell surface of melanoma cells. |
| 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 | X-ray crystallography (1) |
| Cross Reference PDB | 1RM8; |
| Mapped Pubmed ID | 11830519; 20608975; 8314771; 8530478; 8621565; 8663255; 8804434; |
| Motif | MOTIF 99..106; /note=Cysteine switch; /evidence=ECO:0000250 |
| Gene Encoded By | |
| Mass | 69,521 |
| Kinetics | |
| Metal Binding | METAL 101; /note=Zinc 1; in inhibited form; /evidence=ECO:0000250; METAL 183; /note=Calcium 1; via carbonyl oxygen; METAL 193; /note=Zinc 1; METAL 195; /note=Zinc 1; METAL 200; /note=Calcium 2; METAL 201; /note=Calcium 2; via carbonyl oxygen; METAL 203; /note=Calcium 2; via carbonyl oxygen; METAL 205; /note=Calcium 2; via carbonyl oxygen; METAL 215; /note=Calcium 1; via carbonyl oxygen; METAL 217; /note=Calcium 1; via carbonyl oxygen; METAL 219; /note=Calcium 1; METAL 223; /note=Calcium 2; METAL 226; /note=Calcium 2; METAL 246; /note=Zinc 2; catalytic; METAL 250; /note=Zinc 2; catalytic; METAL 256; /note=Zinc 2; catalytic |
| Rhea ID | |
| Cross Reference Brenda |