IED ID | IndEnz0002008099 |
Enzyme Type ID | protease008099 |
Protein Name |
Macrophage metalloelastase MME EC 3.4.24.65 Matrix metalloproteinase-12 MMP-12 |
Gene Name | Mmp12 Mme Mmel |
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 | MSCTLLKGVCTMKFLMMIVFLQVSACGAAPMNDSEFAEWYLSRFYDYGKDRIPMTKTKTNRNFLKEKLQEMQQFFGLEATGQLDNSTLAIMHIPRCGVPDVQHLRAVPQRSRWMKRYLTYRIYNYTPDMKREDVDYIFQKAFQVWSDVTPLRFRKLHKDEADIMILFAFGAHGDFNYFDGKGGTLAHAFYPGPGIQGDAHFDEAETWTKSFQGTNLFLVAVHELGHSLGLQHSNNPKSIMYPTYRYLNPSTFRLSADDIRNIQSLYGAPVKPPSLTKPSSPPSTFCHQSLSFDAVTTVGEKIFFFKDWFFWWKLPGSPATNITSISSIWPSIPSGIQAAYEIESRNQLFLFKDEKYWLINNLVPEPHYPRSIYSLGFSASVKKVDAAVFDPLRQKVYFFVDKHYWRYDVRQELMDPAYPKLISTHFPGIKPKIDAVLYFKRHYYIFQGAYQLEYDPLFRRVTKTLKSTSWFGC |
Enzyme Length | 473 |
Uniprot Accession Number | P34960 |
Absorption | |
Active Site | ACT_SITE 223; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095 |
Activity Regulation | |
Binding Site | |
Calcium Binding | |
catalytic Activity | CATALYTIC ACTIVITY: Reaction=Hydrolysis of soluble and insoluble elastin. Specific cleavages are also produced at 14-Ala-|-Leu-15 and 16-Tyr-|-Leu-17 in the B chain of insulin.; EC=3.4.24.65; |
DNA Binding | |
EC Number | 3.4.24.65 |
Enzyme Function | FUNCTION: May be involved in tissue injury and remodeling. Has significant elastolytic activity. Can accept large and small amino acids at the P1' site, but has a preference for leucine. Aromatic or hydrophobic residues are preferred at the P1 site, with small hydrophobic residues (preferably alanine) occupying P3 (By similarity). {ECO:0000250}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (1); Chain (1); Disulfide bond (1); Erroneous initiation (2); Glycosylation (3); Metal binding (23); Motif (1); Propeptide (1); Repeat (4); Sequence conflict (31); Signal peptide (1) |
Keywords | Calcium;Direct protein sequencing;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..28; /evidence=ECO:0000305 |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | 10187779; 10502816; 10760605; 10841523; 10949577; 11113146; 11395391; 11502863; 11689884; 12097550; 12189240; 12204900; 12634787; 12815621; 12842850; 12858542; 1431103; 14602826; 14633606; 14751561; 14993123; 15063736; 15342725; 15452344; 15579436; 15618213; 15654856; 15734845; 15800495; 15814723; 15983040; 16081501; 16221765; 16236725; 16495447; 16500946; 16571779; 16778188; 16912171; 17136358; 17209037; 17395890; 17446527; 17620183; 17681721; 18003950; 18203142; 18441096; 18479957; 18547653; 18660381; 18806126; 18852254; 18997394; 19218336; 19221044; 1931076; 19346698; 19513084; 19536155; 19620042; 19672072; 19935767; 20093499; 20101093; 20181883; 20651245; 21212406; 21267068; 21321074; 21378275; 21719762; 21784967; 21814804; 21856305; 21944884; 22014525; 22119538; 22153340; 22171010; 22223197; 22773692; 23061826; 23159549; 23271741; 23285156; 23295969; 23421805; 23813962; 23922714; 23978445; 24006456; 24526442; 24784232; 24828142; 24907602; 24914890; 24914938; 25166912; 25302498; 25310974; 25503990; 25636537; 25652021; 25686691; 25797678; 25864931; 26079807; 26438797; 26445891; 26563237; 26608672; 26676790; 26822129; 27015453; 27306493; 27398409; 27862656; 28237967; 28442300; 28814604; 29429629; 29503085; 29523595; 29550371; 29722565; 29925830; 30294471; 30510003; 30753170; 30880028; 30959793; 31009606; 31399604; 31562139; 32242260; 32295421; 32693803; 32882513; 32987131; 33072094; 34622152; 34653936; 34681679; 34703996; 7558021; 7559635; 8188294; 8226919; 8632994; 8812413; 9302297; 9344654; 9398846; |
Motif | MOTIF 94..101; /note=Cysteine switch; /evidence=ECO:0000250 |
Gene Encoded By | |
Mass | 54,971 |
Kinetics | |
Metal Binding | METAL 96; /note=Zinc 2; in inhibited form; /evidence=ECO:0000250; METAL 128; /note=Calcium 1; /evidence=ECO:0000250; METAL 162; /note=Calcium 2; /evidence=ECO:0000250; METAL 172; /note=Zinc 1; /evidence=ECO:0000250; METAL 174; /note=Zinc 1; /evidence=ECO:0000250; METAL 179; /note=Calcium 3; /evidence=ECO:0000250; METAL 180; /note=Calcium 3; via carbonyl oxygen; /evidence=ECO:0000250; METAL 182; /note=Calcium 3; via carbonyl oxygen; /evidence=ECO:0000250; METAL 184; /note=Calcium 3; via carbonyl oxygen; /evidence=ECO:0000250; METAL 187; /note=Zinc 1; /evidence=ECO:0000250; METAL 194; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250; METAL 198; /note=Calcium 2; /evidence=ECO:0000250; METAL 200; /note=Zinc 1; /evidence=ECO:0000250; METAL 202; /note=Calcium 3; /evidence=ECO:0000250; METAL 203; /note=Calcium 1; /evidence=ECO:0000250; METAL 205; /note=Calcium 1; /evidence=ECO:0000250; METAL 205; /note=Calcium 3; /evidence=ECO:0000250; METAL 222; /note=Zinc 2; catalytic; /evidence=ECO:0000250; METAL 226; /note=Zinc 2; catalytic; /evidence=ECO:0000250; METAL 232; /note=Zinc 2; catalytic; /evidence=ECO:0000250; METAL 293; /note=Calcium 4; via carbonyl oxygen; /evidence=ECO:0000250; METAL 385; /note=Calcium 4; via carbonyl oxygen; /evidence=ECO:0000250; METAL 434; /note=Calcium 4; via carbonyl oxygen; /evidence=ECO:0000250 |
Rhea ID | |
Cross Reference Brenda | 3.4.24.65; |