IED ID | IndEnz0002006517 |
Enzyme Type ID | protease006517 |
Protein Name |
Matrix metalloproteinase-19 MMP-19 EC 3.4.24.- Matrix metalloproteinase RASI |
Gene Name | Mmp19 Rasi |
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 | MDWQQLWLAFLLPMTVSGRALGPTEKEAVLDYLLQYGYLQKPLEGADDFRLEDITEALRTFQEASGLPISGQMDDATRARMKQPRCGLEDPFNQKSLKYLLLGHWRKKNLTFRIFNVPSTLSLPRVRAALHQAFKYWSSVAPLTFREVKAGWADIRLSFHGRQSLYCSNTFDGPGKVLAHADIPELGSIHFDKDELWTEGTYQGVNLRIIAAHEVGHALGLGHSRYTQALMAPVYAGYQPFFKLHPDDVAGIQALYGKRSPETRDEEEETEMLTVSPVTAKPGPMPNPCSGEVDAMVLGPRGKTYAFKGDYVWTVTDSGPGPLFQISALWEGLPGNLDAAVYSPRTRRTHFFKGNKVWRYVDFKMSPGFPMKFNRVEPNLDAALYWPVNQKVFLFKGSGYWQWDELARTDLSRYPKPIKELFTGVPDRPSAAMSWQDGQVYFFKGKEYWRLNQQLRVAKGYPRNTTHWMHCGSQTPDTNSSTGDVTPSTTDTVLGTTPSTMGSTLDIPSATDSASLSFSANVTLLGA |
Enzyme Length | 527 |
Uniprot Accession Number | Q9JHI0 |
Absorption | |
Active Site | ACT_SITE 214; /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 aggrecan and cartilage oligomeric matrix protein (comp), during development, haemostasis and pathological conditions (arthritic disease). May also play a role in neovascularization or angiogenesis (By similarity). Hydrolyzes collagen type IV, laminin, nidogen, nascin-C isoform, fibronectin, and type I gelatin (By similarity). {ECO:0000250}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (1); Chain (1); Disulfide bond (1); Glycosylation (4); Lipidation (1); Metal binding (4); Motif (1); Propeptide (2); Region (1); Repeat (4); Signal peptide (1) |
Keywords | Angiogenesis;Calcium;Cell membrane;Collagen degradation;Developmental protein;Differentiation;Disulfide bond;Extracellular matrix;GPI-anchor;Glycoprotein;Hydrolase;Lipoprotein;Membrane;Metal-binding;Metalloprotease;Phosphoprotein;Protease;Reference proteome;Repeat;Secreted;Signal;Zinc;Zymogen |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor, GPI-anchor {ECO:0000305}; Extracellular side {ECO:0000305}. Secreted, extracellular space, extracellular matrix {ECO:0000305}. |
Modified Residue | |
Post Translational Modification | PTM: Activated by autolytic cleavage after Lys-98. {ECO:0000250}.; PTM: Tyrosine phosphorylated by PKDCC/VLK. {ECO:0000250|UniProtKB:Q99542}. |
Signal Peptide | SIGNAL 1..18; /evidence=ECO:0000255 |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | 12466851; 15063736; 15169894; 15734845; 16452166; 16707448; 18523579; 19843707; 21267068; 21677750; 22171010; 22297719; 22859522; 23056273; 23421805; 24006456; 25575513; 25636537; 26163370; 26555704; 26700939; 33153107; |
Motif | MOTIF 84..91; /note=Cysteine switch; /evidence=ECO:0000250 |
Gene Encoded By | |
Mass | 59,122 |
Kinetics | |
Metal Binding | METAL 86; /note=Zinc; in inhibited form; /evidence=ECO:0000250; METAL 213; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; METAL 217; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; METAL 223; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095 |
Rhea ID | |
Cross Reference Brenda |