Detail Information for IndEnz0002008099
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;