| IED ID | IndEnz0002008100 |
| Enzyme Type ID | protease008100 |
| Protein Name |
Stromelysin-3 SL-3 ST3 EC 3.4.24.- Matrix metalloproteinase-11 MMP-11 |
| Gene Name | Mmp11 |
| 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 | MARAACLLRAISRALLLPLPLLLLLLLLLPPQLMARARPPENHRHRPVKRVPQLLPAALPNSLPSVPASHWVPGPASSSRPLRCGVPDPPDVLNARNRQKRFVLSGGRWEKTDLTYRILRFPWQLVREQVRQTVAEALRVWSEVTPLTFTEVHEGRADIMIDFTRYWHGDNLPFDGPGGILAHAFFPKTHREGDVHFDYDETWTIGDKGTDLLQVAAHEFGHVLGLQHTTAAKALMSPFYTFRYPLSLSPDDRRGIQHLYGRPQLTPTSPTPTLSSQAGTDTNEIALQEPEVPPEVCETSFDAVSTIRGELFFFKAGFVWRLRSGQLQPGYPALASRHWQGLPSPVDAAFEDAQGQIWFFQGAQYWVYDGEKPVLGPAPLSKLGLQGSPVHAALVWGPEKNKIYFFRGGDYWRFHPRTQRVDNPVPRRTTDWRGVPSEIDAAFQDAEGYAYFLRGHLYWKFDPVKVKVLESFPRPIGPDFFDCAEPANTFR |
| Enzyme Length | 491 |
| Uniprot Accession Number | Q499S5 |
| Absorption | |
| Active Site | ACT_SITE 219; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.24.- |
| Enzyme Function | FUNCTION: May play an important role in the progression of epithelial malignancies. {ECO:0000250}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Compositional bias (1); Disulfide bond (1); Erroneous initiation (2); Metal binding (12); Motif (1); Propeptide (1); Region (1); Repeat (4); Signal peptide (1) |
| Keywords | Calcium;Cleavage on pair of basic residues;Collagen degradation;Disulfide bond;Extracellular matrix;Hydrolase;Metal-binding;Metalloprotease;Protease;Reference proteome;Repeat;Secreted;Signal;Zinc;Zymogen |
| Interact With | |
| Induction | INDUCTION: In skin fibroblasts of superficial dermis upon skin lesion with highest level between days 5-10. {ECO:0000269|PubMed:9055814}. |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250}. |
| Modified Residue | |
| Post Translational Modification | PTM: The precursor is cleaved by a furin endopeptidase. {ECO:0000269|PubMed:9055814}. |
| Signal Peptide | SIGNAL 1..35; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | MOTIF 82..89; /note=Cysteine switch; /evidence=ECO:0000250 |
| Gene Encoded By | |
| Mass | 55,511 |
| Kinetics | |
| Metal Binding | METAL 84; /note=Zinc 2; in inhibited form; /evidence=ECO:0000250; METAL 168; /note=Zinc 1; /evidence=ECO:0000250; METAL 170; /note=Zinc 1; /evidence=ECO:0000250; METAL 175; /note=Calcium; /evidence=ECO:0000250; METAL 176; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250; METAL 178; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250; METAL 180; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250; METAL 183; /note=Zinc 1; /evidence=ECO:0000250; METAL 196; /note=Zinc 1; /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 |
| Rhea ID | |
| Cross Reference Brenda |