Detail Information for IndEnz0002002814
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