IED Industry Enzyme Database

Detail Information for IndEnz0002006545
IED ID IndEnz0002006545
Enzyme Type ID protease006545
Protein Name Stromelysin-1
SL-1
EC 3.4.24.17
EMS-2
Matrix metalloproteinase-3
MMP-3
Transin-1
Gene Name Mmp3
Organism Mus musculus (Mouse)
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 Mus Mus Mus musculus (Mouse)
Enzyme Sequence MKGLPVLLWLCVVVCSSYPLHDSARDDDAGMELLQKYLENYYGLAKDVKQFIKKKDSSLIVKKIQEMQKFLGLEMTGKLDSNTMELMHKPRCGVPDVGGFSTFPGSPKWRKSHITYRIVNYTPDLPRQSVDSAIEKALKVWEEVTPLTFSRISEGEADIMISFAVGEHGDFVPFDGPGTVLAHAYAPGPGINGDAHFDDDERWTEDVTGTNLFLVAAHELGHSLGLYHSAKAEALMYPVYKSSTDLSRFHLSQDDVDGIQSLYGTPTASPDVLVVPTKSNSLEPETSPMCSSTLFFDAVSTLRGEVLFFKDRHFWRKSLRTPEPEFYLISSFWPSLPSNMDAAYEVTNRDTVFIFKGNQFWAIRGHEELAGYPKSIHTLGLPATVKKIDAAISNKEKRKTYFFVEDKYWRFDEKKQSMEPGFPRKIAEDFPGVDSRVDAVFEAFGFLYFFSGSSQLEFDPNAKKVTHILKSNSWFNC
Enzyme Length 477
Uniprot Accession Number P28862
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); Disulfide bond (1); Erroneous initiation (1); Metal binding (24); Motif (1); Propeptide (1); Repeat (4); Sequence conflict (1); Signal peptide (1)
Keywords Calcium;Collagen degradation;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
Signal Peptide SIGNAL 1..17; /evidence=ECO:0000305
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 10048576; 10359808; 10419448; 10428026; 10433819; 10450741; 10502816; 10531025; 10553093; 10642592; 10657574; 10713697; 10731089; 10949577; 10985432; 11113146; 11350822; 11359935; 11566859; 11689884; 11830584; 11865039; 11869290; 12060661; 12097550; 12669125; 12815621; 12975354; 14673996; 14720510; 14726605; 15044844; 15063736; 15466188; 15470062; 15536133; 15550552; 15618213; 15734845; 15841177; 15893322; 15921521; 16141072; 16221765; 16509766; 16624562; 16678100; 17021275; 17116747; 17235437; 17307908; 17376075; 17540368; 17596135; 18036345; 18050203; 18172013; 18267097; 18337830; 18397366; 18639653; 18641052; 18802027; 18818437; 18923335; 19058297; 19111539; 19139395; 19608750; 19799610; 19815046; 19844242; 19853894; 19913533; 20165883; 20360864; 20368330; 20472558; 20495570; 20513444; 20534975; 20548288; 20609072; 20864640; 20930145; 20969476; 21719762; 21750040; 21800363; 21858843; 21871427; 21928379; 22014525; 22108898; 22171010; 22201681; 22345078; 22398316; 22484054; 22682244; 22786680; 22862420; 22927007; 22951731; 22959068; 23145787; 23281061; 23404611; 23421805; 23509775; 23554135; 23592797; 23658188; 23853428; 23871604; 23934123; 24006456; 24416274; 24957860; 25194508; 25285627; 25325922; 25344368; 25536219; 25652596; 25664857; 25693634; 25848906; 26008967; 26079709; 26163370; 26203177; 26358260; 26378628; 26445891; 27033979; 27096327; 27398409; 27461525; 27633994; 27676418; 27809288; 27879248; 28069922; 28158775; 29247173; 29276151; 29377313; 29761931; 30054581; 30269950; 30295685; 30479344; 31470007; 31652545; 32109382; 32959071; 32987131; 33859300; 33859779; 7669731; 7760812; 7960227; 8144618; 8175886; 8573787; 8672141; 8674412; 8872958; 9006971; 9030563; 9108368; 9291579; 9348221; 9398846; 9433876; 9490689; 9708806;
Motif MOTIF 90..97; /note=Cysteine switch; /evidence=ECO:0000250
Gene Encoded By
Mass 53,845
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 3.4.24.17;