Detail Information for IndEnz0002006546
IED ID IndEnz0002006546
Enzyme Type ID protease006546
Protein Name Stromelysin-1
SL-1
EC 3.4.24.17
Matrix metalloproteinase-3
MMP-3
PTR1 protein
Transin-1
Gene Name Mmp3
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 MKGLPVLLWLCTAVCSSYPLHGSEEDAGMEVLQKYLENYYGLEKDVKQFTKKKDSSPVVKKIQEMQKFLGLKMTGKLDSNTMELMHKPRCGVPDVGGFSTFPGSPKWRKNHISYRIVNYTLDLPRESVDSAIERALKVWEEVTPLTFSRISEGEADIMISFAVEEHGDFIPFDGPGMVLAHAYAPGPGTNGDAHFDDDERWTDDVTGTNLFLVAAHELGHSLGLFHSANAEALMYPVYKSSTDLARFHLSQDDVDGIQSLYGPPTESPDVLVVPTKSNSLDPETLPMCSSALSFDAVSTLRGEVLFFKDRHFWRKSLRTPEPGFYLISSFWPSLPSNMDAAYEVTNRDTVFILKGNQIWAIRGHEELAGYPKSIHTLGLPETVQKIDAAISLKDQKKTYFFVEDKFWRFDEKKQSMDPEFPRKIAENFPGIGTKVDAVFEAFGFLYFFSGSSQLEFDPNAGKVTHILKSNSWFNC
Enzyme Length 475
Uniprot Accession Number P03957
Absorption
Active Site ACT_SITE 217; /evidence=ECO:0000269|PubMed:2841336
Activity Regulation ACTIVITY REGULATION: Inhibited by a synthetic peptide corresponding to the inhibitory cysteine switch motif (PubMed:1988438). Inhibited by ethylenediaminetetraacetic acid (EDTA), 1,10-pheanthroline, 2-mecaptoethanol, dithiothreitol and metalloproteinase inhibitor protein TIMP (PubMed:1963430, PubMed:2841336). {ECO:0000269|PubMed:1963430, ECO:0000269|PubMed:1988438, ECO:0000269|PubMed:2841336}.
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=Preferential cleavage where P1', P2' and P3' are hydrophobic residues.; EC=3.4.24.17; Evidence={ECO:0000269|PubMed:1963430, ECO:0000269|PubMed:1988438, ECO:0000269|PubMed:2841336};
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. {ECO:0000269|PubMed:1963430}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (1); Chain (1); Disulfide bond (1); Glycosylation (1); Metal binding (24); Motif (1); Mutagenesis (14); Propeptide (1); Repeat (4); Signal peptide (1)
Keywords Calcium;Collagen degradation;Direct protein sequencing;Disulfide bond;Extracellular matrix;Glycoprotein;Hydrolase;Metal-binding;Metalloprotease;Protease;Reference proteome;Repeat;Secreted;Signal;Zinc;Zymogen
Interact With
Induction INDUCTION: By epidermal growth factor and is increased in FR3T3 and RAT-1 fibroblasts transformed by polyoma virus, Rous sarcoma virus, or the human cellular H-Ras oncogene.
Subcellular Location SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000305}. Secreted {ECO:0000269|PubMed:1963430, ECO:0000269|PubMed:1988438, ECO:0000269|PubMed:2841336}.
Modified Residue
Post Translational Modification
Signal Peptide SIGNAL 1..17; /evidence=ECO:0000305
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 10428026; 10435007; 11095647; 12489160; 12963432; 15044600; 15099024; 15238617; 15375341; 15504731; 15672041; 15698619; 15863497; 16046515; 16140193; 16150423; 16158251; 16290189; 16935996; 16977379; 17027671; 17083784; 17094476; 17456343; 17539323; 17704356; 18072934; 18172013; 18404723; 18439420; 18629001; 18754875; 18765931; 18832569; 19345799; 19389428; 19397203; 19463894; 19834065; 19889233; 19961752; 20043115; 20056896; 20153826; 20162718; 20472983; 20515599; 20948465; 21038694; 21055467; 21330369; 21649785; 21679445; 22056600; 22114772; 22363061; 22498097; 22615070; 22961837; 23042903; 23086831; 23142217; 23204894; 23224597; 23277113; 24011916; 24194350; 24244039; 25062286; 25536219; 26047379; 26075533; 26087281; 27339256; 27425890; 28265573; 28753453; 29197741; 29462373; 29523370; 29928874; 31493243; 33130223; 33655326; 9327785;
Motif MOTIF 88..95; /note="Cysteine switch"; /evidence="ECO:0000269|PubMed:1988438, ECO:0000269|PubMed:2841336"
Gene Encoded By
Mass 53,428
Kinetics
Metal Binding METAL 90; /note=Zinc 2; in inhibited form; /evidence=ECO:0000250|UniProtKB:P03956; METAL 122; /note=Calcium 1; /evidence=ECO:0000250|UniProtKB:P03956; METAL 156; /note=Calcium 2; /evidence=ECO:0000250|UniProtKB:P03956; METAL 166; /note=Zinc 1; /evidence=ECO:0000250|UniProtKB:P03956; METAL 168; /note=Zinc 1; /evidence=ECO:0000250|UniProtKB:P03956; METAL 173; /note=Calcium 3; /evidence=ECO:0000250|UniProtKB:P03956; METAL 174; /note=Calcium 3; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P03956; METAL 176; /note=Calcium 3; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P03956; METAL 178; /note=Calcium 3; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P03956; METAL 181; /note=Zinc 1; /evidence=ECO:0000250|UniProtKB:P03956; METAL 188; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P03956; METAL 190; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P03956; METAL 192; /note=Calcium 2; /evidence=ECO:0000250|UniProtKB:P03956; METAL 194; /note=Zinc 1; /evidence=ECO:0000250|UniProtKB:P03956; METAL 196; /note=Calcium 3; /evidence=ECO:0000250|UniProtKB:P03956; METAL 197; /note=Calcium 1; /evidence=ECO:0000250|UniProtKB:P03956; METAL 199; /note=Calcium 1; /evidence=ECO:0000250|UniProtKB:P03956; METAL 199; /note=Calcium 3; /evidence=ECO:0000250|UniProtKB:P03956; METAL 216; /note=Zinc 2; catalytic; /evidence=ECO:0000250|UniProtKB:P03956; METAL 220; /note=Zinc 2; catalytic; /evidence=ECO:0000250|UniProtKB:P03956; METAL 226; /note=Zinc 2; catalytic; /evidence=ECO:0000250|UniProtKB:P03956; METAL 295; /note=Calcium 4; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P03956; METAL 387; /note=Calcium 4; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P03956; METAL 436; /note=Calcium 4; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P03956
Rhea ID
Cross Reference Brenda