| IED ID | IndEnz0002006095 |
| Enzyme Type ID | protease006095 |
| Protein Name |
Stromelysin-3 SL-3 ST3 EC 3.4.24.- Matrix metalloproteinase-11 MMP-11 |
| Gene Name | MMP11 STMY3 |
| Organism | Homo sapiens (Human) |
| 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 Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human) |
| Enzyme Sequence | MAPAAWLRSAAARALLPPMLLLLLQPPPLLARALPPDAHHLHAERRGPQPWHAALPSSPAPAPATQEAPRPASSLRPPRCGVPDPSDGLSARNRQKRFVLSGGRWEKTDLTYRILRFPWQLVQEQVRQTMAEALKVWSDVTPLTFTEVHEGRADIMIDFARYWHGDDLPFDGPGGILAHAFFPKTHREGDVHFDYDETWTIGDDQGTDLLQVAAHEFGHVLGLQHTTAAKALMSAFYTFRYPLSLSPDDCRGVQHLYGQPWPTVTSRTPALGPQAGIDTNEIAPLEPDAPPDACEASFDAVSTIRGELFFFKAGFVWRLRGGQLQPGYPALASRHWQGLPSPVDAAFEDAQGHIWFFQGAQYWVYDGEKPVLGPAPLTELGLVRFPVHAALVWGPEKNKIYFFRGRDYWRFHPSTRRVDSPVPRRATDWRGVPSEIDAAFQDADGYAYFLRGRLYWKFDPVKVKALEGFPRLVGPDFFGCAEPANTFL |
| Enzyme Length | 488 |
| Uniprot Accession Number | P24347 |
| Absorption | |
| Active Site | ACT_SITE 216; /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. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Disulfide bond (1); Metal binding (11); Motif (1); Natural variant (6); Propeptide (1); Region (1); Repeat (4); Signal peptide (1) |
| Keywords | Calcium;Cleavage on pair of basic residues;Collagen degradation;Direct protein sequencing;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 | PTM: The precursor is cleaved by a furin endopeptidase. {ECO:0000250}. |
| Signal Peptide | SIGNAL 1..31; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 11857311; 12006591; 12429794; 12538453; 12845673; 1480033; 15459498; 15509588; 15582574; 15989693; 1698775; 17085465; 17091452; 17233884; 17543340; 17980449; 18172255; 18208802; 18476627; 18622425; 19159011; 19212658; 19509157; 19913121; 19914229; 20060156; 20160732; 20230842; 20452482; 20587546; 20628086; 20673868; 21048031; 21442356; 21513571; 2169257; 21773755; 21935455; 22076168; 22227581; 22286800; 22488635; 22768249; 22927434; 23115007; 23211491; 23755751; 24564996; 24838924; 25081520; 25423087; 25987024; 26084486; 26507719; 26892540; 26956825; 27002762; 27081863; 27364572; 28409241; 28427180; 28445974; 28801789; 29374701; 29725257; 30218127; 30710321; 30787663; 31335488; 31337950; 31342542; 31570432; 31595150; 32590618; 33228130; 33396463; 33649832; 34038440; 7981201; 8645182; |
| Motif | MOTIF 78..85; /note=Cysteine switch; /evidence=ECO:0000250 |
| Gene Encoded By | |
| Mass | 54,590 |
| Kinetics | |
| Metal Binding | METAL 80; /note=Zinc 2; in inhibited form; /evidence=ECO:0000250; METAL 166; /note=Zinc 1; /evidence=ECO:0000250; METAL 171; /note=Calcium; /evidence=ECO:0000250; METAL 172; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250; METAL 174; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250; METAL 176; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250; METAL 179; /note=Zinc 1; /evidence=ECO:0000250; METAL 192; /note=Zinc 1; /evidence=ECO:0000250; METAL 215; /note=Zinc 2; catalytic; /evidence=ECO:0000250; METAL 219; /note=Zinc 2; catalytic; /evidence=ECO:0000250; METAL 225; /note=Zinc 2; catalytic; /evidence=ECO:0000250 |
| Rhea ID | |
| Cross Reference Brenda | 3.4.24.B3; |