| IED ID | IndEnz0002006521 |
| Enzyme Type ID | protease006521 |
| Protein Name |
Interstitial collagenase EC 3.4.24.7 Matrix metalloproteinase-1 MMP-1 |
| Gene Name | MMP1 |
| Organism | Equus caballus (Horse) |
| 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 Laurasiatheria Perissodactyla (odd-toed ungulates) Equidae (horses) Equus Equus Equus caballus (Horse) |
| Enzyme Sequence | MLSLPLLLLLLWGMGSHSFPTVPSETREEDVEMVQKYLENYYNLKSDGEQIEKQRHRSPVVEKLKQMQEFFGLKVTGKPDAETLNVMKQPRCGVPDVAEFVLTEGNPRWENTHLTYRIENYTPDLPRADVDQAIEKAFQLWSNVSPLTFTKVSEGQADIMISFVRGDHRDNSPFDGPGGNLAHAFQPGPRIGGDAHFDEDETWTSNFRNYNLYRVAAHEFGHSLGLSHSTDIGALMYPNYFFTGDVQLSQDDINGIQAIYGPSQNPIQPIGPQTPEVCDSKLTFDAITTIRGEVMFFKDRFYMRINPYYPEAELNFISIFWPQLPNGLQAAYEVSHRDEVRFFKGNKYWAVKGQDVLYGYPKDIHRSFGFPSTVKNIDAAVSEEDTGKTYFFVADKYWRYDEYKRSMDAGYPKMIADDFPGIGDKVDAVFQKDGFFYFFHGTRQYKFDPKTKRILTLQKANSWFNCRKN |
| Enzyme Length | 469 |
| Uniprot Accession Number | Q9XSZ5 |
| Absorption | |
| Active Site | ACT_SITE 219; /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); Metal binding (24); Modified residue (2); Motif (1); Propeptide (1); Repeat (4); Signal peptide (1) |
| Keywords | Calcium;Collagen degradation;Disulfide bond;Extracellular matrix;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 274; /note=Phosphothreonine; /evidence=ECO:0000250|UniProtKB:P03956; MOD_RES 360; /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; /evidence=ECO:0000250 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | MOTIF 90..97; /note=Cysteine switch; /evidence=ECO:0000250 |
| Gene Encoded By | |
| Mass | 54,002 |
| Kinetics | |
| Metal Binding | METAL 92; /note=Zinc 2; in inhibited form; /evidence=ECO:0000250; METAL 124; /note=Calcium 1; /evidence=ECO:0000250; METAL 158; /note=Calcium 2; /evidence=ECO:0000250; METAL 168; /note=Zinc 1; /evidence=ECO:0000250; METAL 170; /note=Zinc 1; /evidence=ECO:0000250; METAL 175; /note=Calcium 3; /evidence=ECO:0000250; METAL 176; /note=Calcium 3; via carbonyl oxygen; /evidence=ECO:0000250; METAL 178; /note=Calcium 3; via carbonyl oxygen; /evidence=ECO:0000250; METAL 180; /note=Calcium 3; via carbonyl oxygen; /evidence=ECO:0000250; METAL 183; /note=Zinc 1; /evidence=ECO:0000250; METAL 190; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250; METAL 192; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250; METAL 194; /note=Calcium 2; /evidence=ECO:0000250; METAL 196; /note=Zinc 1; /evidence=ECO:0000250; METAL 198; /note=Calcium 3; /evidence=ECO:0000250; METAL 199; /note=Calcium 1; /evidence=ECO:0000250; METAL 201; /note=Calcium 3; /evidence=ECO:0000250; METAL 218; /note=Zinc 2; catalytic; /evidence=ECO:0000250; METAL 222; /note=Zinc 2; catalytic; /evidence=ECO:0000250; METAL 228; /note=Zinc 2; catalytic; /evidence=ECO:0000250; METAL 285; /note=Calcium 4; via carbonyl oxygen; /evidence=ECO:0000250; METAL 329; /note=Calcium 4; via carbonyl oxygen; /evidence=ECO:0000250; METAL 378; /note=Calcium 4; via carbonyl oxygen; /evidence=ECO:0000250; METAL 427; /note=Calcium 4; via carbonyl oxygen; /evidence=ECO:0000250 |
| Rhea ID | |
| Cross Reference Brenda |