| IED ID | IndEnz0002002815 |
| Enzyme Type ID | protease002815 |
| Protein Name |
Stromelysin-1 SL-1 EC 3.4.24.17 Matrix metalloproteinase-3 MMP-3 Transin-1 |
| Gene Name | MMP3 |
| 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 | MKTLPTLLLLCVALCSAYPLDGASRDADTTNMDLLQQYLENYYNLEKDVKQFVKRKDSSPVVKKIQEMQKFLGLEVTGKLDSNTLEVIRKPRCGVPDVGHFSTFPGTPKWTKTHLTYRIVNYTPDLPRDAVDAAIEKALKVWEEVTPLTFSRKYEGEADIMISFGVREHGDFIPFDGPGNVLAHAYAPGPGINGDAHFDDDEQWTKDTTGTNLFLVAAHELGHSLGLFHSANPEALMYPVYNAFTDLARFRLSQDDVDGIQSLYGPAPASPDNSGVPMEPVPPGSGTPVMCDPDLSFDAISTLRGEILFFKDRYFWRKSLRILEPEFHLISSFWPSLPSAVDAAYEVISRDTVFIFKGTQFWAIRGNEVQAGYPRSIHTLGFPSTIRKIDAAISDKERKKTYFFVEDKYWRFDEKRQSLEPGFPRHIAEDFPGINPKIDAVFEAFGFFYFFSGSSQSEFDPNAKKVTHVLKSNSWFQC |
| Enzyme Length | 478 |
| Uniprot Accession Number | P28863 |
| Absorption | |
| Active Site | ACT_SITE 220; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Preferential cleavage where P1', P2' and P3' are hydrophobic residues.; EC=3.4.24.17; |
| DNA Binding | |
| EC Number | 3.4.24.17 |
| Enzyme Function | FUNCTION: Can degrade fibronectin, laminin, gelatins of type I, III, IV, and V; collagens III, IV, X, and IX, and cartilage proteoglycans. Activates procollagenase. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Disulfide bond (1); Metal binding (24); Motif (1); Propeptide (1); Repeat (4); Sequence conflict (2); Signal peptide (1) |
| Keywords | Calcium;Collagen degradation;Disulfide bond;Extracellular matrix;Hydrolase;Metal-binding;Metalloprotease;Protease;Reference proteome;Repeat;Secreted;Signal;Zinc;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000305}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..17; /evidence=ECO:0000305 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 19778818; 20238014; 22853554; 23520014; 23879595; 26873249; |
| Motif | MOTIF 91..98; /note=Cysteine switch; /evidence=ECO:0000250 |
| Gene Encoded By | |
| Mass | 53,942 |
| Kinetics | |
| Metal Binding | METAL 93; /note=Zinc 2; in inhibited form; /evidence=ECO:0000250; METAL 125; /note=Calcium 1; /evidence=ECO:0000250; METAL 159; /note=Calcium 2; /evidence=ECO:0000250; METAL 169; /note=Zinc 1; /evidence=ECO:0000250; METAL 171; /note=Zinc 1; /evidence=ECO:0000250; METAL 176; /note=Calcium 3; /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 181; /note=Calcium 3; via carbonyl oxygen; /evidence=ECO:0000250; METAL 184; /note=Zinc 1; /evidence=ECO:0000250; METAL 191; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250; METAL 193; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250; METAL 195; /note=Calcium 2; /evidence=ECO:0000250; METAL 197; /note=Zinc 1; /evidence=ECO:0000250; METAL 199; /note=Calcium 3; /evidence=ECO:0000250; METAL 200; /note=Calcium 1; /evidence=ECO:0000250; METAL 202; /note=Calcium 1; /evidence=ECO:0000250; METAL 202; /note=Calcium 3; /evidence=ECO:0000250; METAL 219; /note=Zinc 2; catalytic; /evidence=ECO:0000250; METAL 223; /note=Zinc 2; catalytic; /evidence=ECO:0000250; METAL 229; /note=Zinc 2; catalytic; /evidence=ECO:0000250; METAL 298; /note=Calcium 4; via carbonyl oxygen; /evidence=ECO:0000250; METAL 390; /note=Calcium 4; via carbonyl oxygen; /evidence=ECO:0000250; METAL 439; /note=Calcium 4; via carbonyl oxygen; /evidence=ECO:0000250 |
| Rhea ID | |
| Cross Reference Brenda |