| IED ID | IndEnz0002006320 |
| Enzyme Type ID | protease006320 |
| Protein Name |
Interstitial collagenase EC 3.4.24.7 Matrix metalloproteinase-1 MMP-1 |
| Gene Name | MMP1 |
| Organism | Oryctolagus cuniculus (Rabbit) |
| 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) Lagomorpha Leporidae (rabbits and hares) Oryctolagus Oryctolagus cuniculus (Rabbit) |
| Enzyme Sequence | MPGLPLLLLLLWGVGSHGFPAASETQEQDVEMVQKYLENYYNLKDDWRKIPKQRGNGLAVEKLKQMQEFFGLKVTGKPDAETLKMMKQPRCGVPDVAQFVLTPGNPRWEQTHLTYRIENYTPDLSRADVDNAIEKAFQLWSNVTPLTFTKVSKGQADIMISFVRGDHRDNSPFDGPEGQLAHAFQPGLGIGGDVHFDEDDRWTKDFRNYNLYRVAAHELGHSLGLSHSTDIGALMYPNYMFSGDVQLAQDDIDGIQAIYGPSQNPSQPVGPQTPKVCDSKLTFDAITTIRGEIMFFKDRFYMRANPYYSEVELNFISVFWPHLPNGLQAAYEVAHRDEILFFKGNKYWTVQGQNELPGYPKDIHSSFGFPRSVNHIDAAVSEEDTGKTYFFVANKYWRYDEYKRSMDAGYPKMIEYDFPGIGNKVDAVFKKDGFFYFFHGTRQYKFDPKTKRILTLQKANSWFNCRKN |
| Enzyme Length | 468 |
| Uniprot Accession Number | P13943 |
| Absorption | |
| Active Site | ACT_SITE 218; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095 |
| 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. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Disulfide bond (1); Glycosylation (1); Metal binding (24); Modified residue (2); Motif (1); Propeptide (1); Repeat (4); Signal peptide (1) |
| Keywords | Calcium;Collagen degradation;Disulfide bond;Extracellular matrix;Glycoprotein;Hydrolase;Metal-binding;Metalloprotease;Phosphoprotein;Protease;Reference proteome;Repeat;Secreted;Signal;Zinc;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250}. |
| Modified Residue | MOD_RES 273; /note=Phosphothreonine; /evidence=ECO:0000250|UniProtKB:P03956; MOD_RES 359; /note=Phosphotyrosine; by PKDCC; /evidence=ECO:0000250|UniProtKB:P03956 |
| Post Translational Modification | PTM: Tyrosine phosphorylated in platelets by PKDCC/VLK. {ECO:0000250|UniProtKB:P03956}. |
| Signal Peptide | SIGNAL 1..18 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 21742783; 23879595; 27697532; 30626725; |
| Motif | MOTIF 89..96; /note=Cysteine switch; /evidence=ECO:0000250 |
| Gene Encoded By | |
| Mass | 53,740 |
| Kinetics | |
| Metal Binding | METAL 91; /note=Zinc 2; in inhibited form; /evidence=ECO:0000250; METAL 123; /note=Calcium 1; /evidence=ECO:0000250; METAL 157; /note=Calcium 2; /evidence=ECO:0000250; METAL 167; /note=Zinc 1; /evidence=ECO:0000250; METAL 169; /note=Zinc 1; /evidence=ECO:0000250; METAL 174; /note=Calcium 3; /evidence=ECO:0000250; METAL 175; /note=Calcium 3; via carbonyl oxygen; /evidence=ECO:0000250; METAL 177; /note=Calcium 3; via carbonyl oxygen; /evidence=ECO:0000250; METAL 179; /note=Calcium 3; via carbonyl oxygen; /evidence=ECO:0000250; METAL 182; /note=Zinc 1; /evidence=ECO:0000250; METAL 189; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250; METAL 191; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250; METAL 193; /note=Calcium 2; /evidence=ECO:0000250; METAL 195; /note=Zinc 1; /evidence=ECO:0000250; METAL 197; /note=Calcium 3; /evidence=ECO:0000250; METAL 198; /note=Calcium 1; /evidence=ECO:0000250; METAL 200; /note=Calcium 3; /evidence=ECO:0000250; METAL 217; /note=Zinc 2; catalytic; /evidence=ECO:0000250; METAL 221; /note=Zinc 2; catalytic; /evidence=ECO:0000250; METAL 227; /note=Zinc 2; catalytic; /evidence=ECO:0000250; METAL 284; /note=Calcium 4; via carbonyl oxygen; /evidence=ECO:0000250; METAL 328; /note=Calcium 4; via carbonyl oxygen; /evidence=ECO:0000250; METAL 377; /note=Calcium 4; via carbonyl oxygen; /evidence=ECO:0000250; METAL 426; /note=Calcium 4; via carbonyl oxygen; /evidence=ECO:0000250 |
| Rhea ID | |
| Cross Reference Brenda |