IED ID | IndEnz0002002813 |
Enzyme Type ID | protease002813 |
Protein Name |
Stromelysin-1 SL-1 EC 3.4.24.17 Matrix metalloproteinase-3 MMP-3 |
Gene Name | MMP3 |
Organism | Canis lupus familiaris (Dog) (Canis familiaris) |
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 Carnivora Caniformia Canidae (dog coyote wolf fox) Canis Canis lupus (Gray wolf) Canis lupus familiaris (Dog) (Canis familiaris) |
Enzyme Sequence | MQNLPALLLFCGVVCSAYPVDRAAEDENNNMELTQQYLENYYNLGKDVKPFVRRRNSGPVVEKIREMQKFLGLEVTGKVDSDTLAMMRRPRCGVPDVGDFTTFPGMPKWRKTHLTYRIMNYTPDLPRDAVDSAIEKALNVWKEVTPLTFSRTDEGEADIKISFAVRDHGDFNPFDGPGNVLGHAYPPGPGIYGDAHFDDDEQWTSDTSGTNLFLVAAHELGHSLGLFHSADPSALMYPVYNVLADLARFHLSQDDVNGIQSLYGGPPSDSSNDPVVPTESVPPGPGTPAACDPTLSFDAISTLRGEFLFFKDRHFWRKSLRTLEPGFYLISSFWPSLPSGLDAAYEETSKDIVFIFKGNQFWAMRGTEVQAGYPKGIHTLGFPPTVKKIDAAVFDKEKKKTYFFVGDKYWRFDEKRQSMEPGFPKQIAEDFPGVDSKVDAAFEAFGFYYFFNGSSQLEFDPNAKKVTHVLKSNSWLNC |
Enzyme Length | 478 |
Uniprot Accession Number | Q6Y4Q5 |
Absorption | |
Active Site | ACT_SITE 219; /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 (By similarity). {ECO:0000250}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (1); Chain (1); Compositional bias (1); Disulfide bond (1); Glycosylation (1); Metal binding (23); Motif (1); Propeptide (1); Region (1); Repeat (4); Signal peptide (1) |
Keywords | Calcium;Collagen degradation;Disulfide bond;Extracellular matrix;Glycoprotein;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:0000250}. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | SIGNAL 1..17; /evidence=ECO:0000255 |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | MOTIF 90..97; /note=Cysteine switch; /evidence=ECO:0000250 |
Gene Encoded By | |
Mass | 53,633 |
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 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 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 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 |