IED ID | IndEnz0002002814 |
Enzyme Type ID | protease002814 |
Protein Name |
Stromelysin-1 SL-1 EC 3.4.24.17 Matrix metalloproteinase-3 MMP-3 |
Gene Name | MMP3 |
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 | MKNLPILLLLCVAACSAYPLDRSARDEDSNMDLLQDYLEKYYDLGKEMRQYVRRKDSGPIVKKIQEMQKFLGLKVTGKLDSDTVEVMHKSRCGVPDVGHFTTFPGMPKWSKTHLTYRIVNYTQDLPRDAVDSDVEKALKIWEEVTPLTFSRIYEGEADIMITFAVREHGDFFPFDGPGKVLAHAYPPGPGMNGDAHFDDDEHWTKDASGINFLLVAAHELGHSLGLYHSTNTEALMYPLYNTLKGPARVRLSQDDVTGIQSLYGPPPASPDSPVEPSEPEPPAPGTLAMCDPALSFDAISTLRGEILFFKDRYFWRKTFRTLVPEFHPISSFWPSLPSGIDAAYEVTSRDSVFIFKGNKFWAIRGNEEQAGYPRGIHTLGFPPTVRKIDAAIFDKEKQKTYFFVEDKYWRFDEKRQSMEPGYPKQIAEDFPGIDSKLDAAFESFGFFYFFSGSSQFEFDPNAKKVTHVLKSNSWFNC |
Enzyme Length | 477 |
Uniprot Accession Number | Q28397 |
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. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (1); Chain (1); Compositional bias (1); Disulfide bond (1); Glycosylation (1); Metal binding (24); Motif (1); Propeptide (1); Region (1); Repeat (4); Sequence conflict (1); 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:0000305}. |
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 | 54,190 |
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 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 297; /note=Calcium 4; via carbonyl oxygen; /evidence=ECO:0000250; METAL 389; /note=Calcium 4; via carbonyl oxygen; /evidence=ECO:0000250; METAL 438; /note=Calcium 4; via carbonyl oxygen; /evidence=ECO:0000250 |
Rhea ID | |
Cross Reference Brenda |