| IED ID | IndEnz0002016110 |
| Enzyme Type ID | protease016110 |
| Protein Name |
Interstitial collagenase EC 3.4.24.7 Fibroblast collagenase Matrix metalloproteinase-1 MMP-1 Myocardial collagenase Fragment |
| Gene Name | Mmp1 |
| 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 | DTLKSEKNADFKDLY |
| Enzyme Length | 15 |
| Uniprot Accession Number | P81563 |
| Absorption | |
| Active Site | |
| Activity Regulation | ACTIVITY REGULATION: Can be activated without removal of the activation peptide. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Cleavage of the triple helix of collagen at about three-quarters of the length of the molecule from the N-terminus, at 775-Gly-|-Ile-776 in the alpha-1(I) chain. Cleaves synthetic substrates and alpha-macroglobulins at bonds where P1' is a hydrophobic residue.; EC=3.4.24.7; |
| DNA Binding | |
| EC Number | 3.4.24.7 |
| Enzyme Function | FUNCTION: Cleaves collagens of types I, II, and III at one site in the helical domain. Also cleaves collagens of types VII and X. May play a role in the deterioration of the heart wall extracellular matrix proteins during the onset of dilated cardiomyopathy. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (1); Non-terminal residue (2) |
| Keywords | Calcium;Collagen degradation;Direct protein sequencing;Extracellular matrix;Hydrolase;Metalloprotease;Phosphoprotein;Protease;Reference proteome;Secreted;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250}. |
| Modified Residue | |
| Post Translational Modification | PTM: The N-terminus is blocked.; PTM: Tyrosine phosphorylated in platelets by PKDCC/VLK. {ECO:0000250|UniProtKB:P03956}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 1,787 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.4.24.7; |