| IED ID | IndEnz0002003761 |
| Enzyme Type ID | protease003761 |
| Protein Name |
Matrix metalloproteinase-14 MMP-14 EC 3.4.24.80 MMP-X1 MT-MMP Membrane-type matrix metalloproteinase 1 MT-MMP 1 MTMMP1 Membrane-type-1 matrix metalloproteinase MT1-MMP MT1MMP |
| Gene Name | Mmp14 Mtmmp |
| 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 | MSPAPRPSRSLLLPLLTLGTALASLGWAQGSNFSPEAWLQQYGYLPPGDLRTHTQRSPQSLSAAIAAMQKFYGLQVTGKADLATMMAMRRPRCGVPDKFGTEIKANVRRKRYAIQGLKWQHNEITFCIQNYTPKVGEYATFEAIRKAFRVWESATPLRFREVPYAYIREGHEKQADIMILFAEGFHGDSTPFDGEGGFLAHAYFPGPNIGGDTHFDSAEPWTVQNEDLNGNDIFLVAVHELGHALGLEHSNDPSAIMAPFYQWMDTENFVLPDDDRRGIQQLYGSKSGSPTKMPPQPRTTSRPSVPDKPKNPAYGPNICDGNFDTVAMLRGEMFVFKERWFWRVRNNQVMDGYPMPIGQFWRGLPASINTAYERKDGKFVFFKGDKHWVFDEASLEPGYPKHIKELGRGLPTDKIDAALFWMPNGKTYFFRGNKYYRFNEEFRAVDSEYPKNIKVWEGIPESPRGSFMGSDEVFTYFYKGNKYWKFNNQKLKVEPGYPKSALRDWMGCPSGGRPDEGTEEETEVIIIEVDEEGSGAVSAAAVVLPVLLLLLVLAVGLAVFFFRRHGTPKRLLYCQRSLLDKV |
| Enzyme Length | 582 |
| Uniprot Accession Number | P53690 |
| Absorption | |
| Active Site | ACT_SITE 240; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Endopeptidase activity. Activates progelatinase A by cleavage of the propeptide at 37-Asn-|-Leu-38. Other bonds hydrolyzed include 35-Gly-|-Ile-36 in the propeptide of collagenase 3, and 341-Asn-|-Phe-342, 441-Asp-|-Leu-442 and 354-Gln-|-Thr-355 in the aggrecan interglobular domain.; EC=3.4.24.80; |
| DNA Binding | |
| EC Number | 3.4.24.80 |
| Enzyme Function | FUNCTION: Endopeptidase that degrades various components of the extracellular matrix such as collagen. Activates progelatinase A. Essential for pericellular collagenolysis and modeling of skeletal and extraskeletal connective tissues during development (PubMed:10520996). May be involved in actin cytoskeleton reorganization by cleaving PTK7 (By similarity). Acts as a positive regulator of cell growth and migration via activation of MMP15. Involved in the formation of the fibrovascular tissues (By similarity). Cleaves ADGRB1 to release vasculostatin-40 which inhibits angiogenesis (By similarity). {ECO:0000250|UniProtKB:P50281, ECO:0000269|PubMed:10520996}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Disulfide bond (1); Metal binding (4); Modified residue (1); Motif (1); Propeptide (1); Region (1); Repeat (4); Sequence conflict (13); Signal peptide (1); Topological domain (2); Transmembrane (1) |
| Keywords | Calcium;Cleavage on pair of basic residues;Collagen degradation;Cytoplasm;Disulfide bond;Hydrolase;Membrane;Metal-binding;Metalloprotease;Phosphoprotein;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}. Melanosome {ECO:0000250}. Cytoplasm {ECO:0000250}. Note=Forms a complex with BST2 and localizes to the cytoplasm. {ECO:0000250}. |
| Modified Residue | MOD_RES 399; /note=Phosphotyrosine; by PKDCC; /evidence=ECO:0000250|UniProtKB:P50281 |
| Post Translational Modification | PTM: The precursor is cleaved by a furin endopeptidase. {ECO:0000250}.; PTM: Tyrosine phosphorylated by PKDCC/VLK. {ECO:0000250|UniProtKB:P50281}. |
| Signal Peptide | SIGNAL 1..20; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 10419448; 10433819; 10737763; 10949577; 11165481; 11221894; 11359935; 11675412; 11747814; 11828004; 11865039; 12049638; 12466851; 12507218; 12592384; 12815621; 12842442; 12900459; 12950084; 12952212; 12952213; 14610065; 14688206; 14979875; 15064723; 15094525; 15304103; 15456762; 15516694; 15522913; 15545316; 15557125; 15563592; 15572153; 15601659; 15695374; 15734845; 15739229; 15800063; 15805464; 15895410; 15944163; 15978592; 16113801; 16147977; 16158179; 16234249; 16236725; 16251193; 16551362; 16678100; 16926191; 17018528; 17136358; 17204469; 17229722; 17393098; 17405818; 17483344; 17548469; 17557804; 17606763; 17620416; 17623673; 17709990; 18022611; 18071307; 18250269; 18445063; 18541723; 18627313; 18639653; 18663148; 18762577; 18799693; 19010778; 19051246; 19066283; 19085378; 19197139; 19264910; 19371380; 19419317; 19542530; 19566825; 19571574; 19706774; 19855192; 19898483; 19915148; 20049897; 20056917; 20152179; 20223936; 20356925; 20418476; 20643648; 20660624; 20663879; 20727881; 20858856; 20978081; 21267068; 21372132; 21436261; 21572390; 21641389; 21666120; 21738685; 21840960; 21893028; 22014525; 22171010; 22202174; 22262018; 22345520; 22423112; 22464947; 22544701; 22632802; 22670674; 22687584; 22688677; 22717126; 22859368; 22971618; 23091646; 23250208; 23334579; 23349620; 23413031; 23421805; 23438179; 23438475; 23685250; 23984338; 24136919; 24395927; 24492617; 24611815; 24670518; 24990232; 25015352; 25180193; 25636537; 25664857; 25735873; 25770908; 25794647; 25920569; 25991604; 26234751; 26390284; 26724533; 26780723; 26926389; 27066886; 27085457; 27435625; 27573347; 27633994; 27736644; 28120021; 28531375; 28692057; 28735290; 28763805; 28914985; 29033361; 29196321; 29401593; 29567669; 29643184; 29712618; 29934628; 30160940; 30269950; 30389913; 30521382; 30822518; 31297933; 31366822; 31600777; 31677819; 31793743; 31988105; 32024800; 32208136; 32229724; 32268857; 32523119; 32730638; 33000497; 33063665; 33805743; 34048934; 34572097; 34830157; 8015608; 8743942; 9037199; |
| Motif | MOTIF 91..98; /note=Cysteine switch; /evidence=ECO:0000250 |
| Gene Encoded By | |
| Mass | 65,919 |
| Kinetics | |
| Metal Binding | METAL 93; /note=Zinc; in inhibited form; /evidence=ECO:0000250; METAL 239; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; METAL 243; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; METAL 249; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095 |
| Rhea ID | |
| Cross Reference Brenda | 3.4.24.80; |