| IED ID | IndEnz0002002817 |
| Enzyme Type ID | protease002817 |
| Protein Name |
Neutrophil collagenase EC 3.4.24.34 Collagenase 2 Matrix metalloproteinase-8 MMP-8 |
| Gene Name | Mmp8 |
| 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 | MFRLKTLPLLIFLHTQLANAFPVPEHLEEKNIKTAENYLRKFYNLPSNQFRSSRNATMVAEKLKEMQRFFSLAETGKLDAATMGIMEMPRCGVPDSGDFLLTPGSPKWTHTNLTYRIINHTPQLSRAEVKTAIEKAFHVWSVASPLTFTEILQGEADINIAFVSRDHGDNSPFDGPNGILAHAFQPGQGIGGDAHFDSEETWTQDSKNYNLFLVAAHEFGHSLGLSHSTDPGALMYPNYAYREPSTYSLPQDDINGIQTIYGPSDNPIQPTGPSTPKACDPHLRFDATTTLRGEIYFFKDKYFWRRHPQLRTVDLNFISLFWPFLPNGLQAAYEDFDRDLVFLFKGRQYWALSGYDLQQGYPRDISNYGFPRSVQAIDAAVSYNGKTYFFINNQCWRYDNQRRSMDPGYPKSIPSMFPGVNCRVDAVFLQDSFFLFFSGPQYFAFNFVSHRVTRVARSNLWLNCS |
| Enzyme Length | 465 |
| Uniprot Accession Number | O70138 |
| Absorption | |
| Active Site | ACT_SITE 218; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095 |
| Activity Regulation | ACTIVITY REGULATION: Cannot be activated without removal of the activation peptide. Activated by matrilysin. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Cleavage of interstitial collagens in the triple helical domain. Unlike EC 3.4.24.7, this enzyme cleaves type III collagen more slowly than type I.; EC=3.4.24.34; |
| DNA Binding | |
| EC Number | 3.4.24.34 |
| Enzyme Function | FUNCTION: Can degrade fibrillar type I, II, and III collagens. May play a role in the degradation of collagen fibers during uterine involution. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Disulfide bond (1); Glycosylation (2); Metal binding (21); Motif (1); Propeptide (1); Repeat (4); Sequence conflict (4); 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: Cytoplasmic granule. Secreted, extracellular space, extracellular matrix. Note=Stored in intracellular granules and released during inflammatory conditions. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..20; /evidence=ECO:0000250 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 10419448; 10949577; 11113146; 11731274; 11985514; 12466851; 14517555; 15063736; 15187163; 15563592; 15734845; 16081833; 16236725; 16301674; 16872848; 17017992; 17307908; 17375198; 17392479; 18245084; 18253113; 18270588; 18332263; 18413742; 18556780; 18694590; 19029300; 19233360; 19542530; 19583703; 19593770; 19745165; 19801498; 19995943; 20042585; 20223936; 20930145; 20949050; 20978081; 21120997; 21267068; 21840960; 22014525; 22464947; 22768176; 22815495; 23071158; 23421805; 23487425; 23512982; 23554135; 23824573; 24006456; 24158518; 24194600; 24373743; 24723558; 25036555; 25049354; 25421209; 25550459; 25636537; 25770908; 25848906; 26092731; 26111477; 26163370; 26923552; 27398409; 27435263; 27626380; 28283184; 28700664; 28827401; 29174564; 30670377; 30778537; 31128097; 31837324; 32370054; 32710469; 33153107; 33763067; 9611252; |
| Motif | MOTIF 89..96; /note=Cysteine switch; /evidence=ECO:0000250 |
| Gene Encoded By | |
| Mass | 53,126 |
| Kinetics | |
| Metal Binding | METAL 91; /note=Zinc 2; in inhibited form; /evidence=ECO:0000250; METAL 157; /note=Calcium 1; /evidence=ECO:0000250; METAL 167; /note=Zinc 1; /evidence=ECO:0000250; METAL 169; /note=Zinc 1; /evidence=ECO:0000250; METAL 174; /note=Calcium 2; /evidence=ECO:0000250; METAL 175; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250; METAL 177; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250; METAL 179; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250; METAL 182; /note=Zinc 1; /evidence=ECO:0000250; METAL 189; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000250; METAL 191; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000250; METAL 193; /note=Calcium 1; /evidence=ECO:0000250; METAL 195; /note=Zinc 1; /evidence=ECO:0000250; METAL 197; /note=Calcium 2; /evidence=ECO:0000250; METAL 200; /note=Calcium 2; /evidence=ECO:0000250; METAL 217; /note=Zinc 2; catalytic; /evidence=ECO:0000250; METAL 221; /note=Zinc 2; catalytic; /evidence=ECO:0000250; METAL 227; /note=Zinc 2; catalytic; /evidence=ECO:0000250; METAL 286; /note=Calcium 3; via carbonyl oxygen; /evidence=ECO:0000250; METAL 378; /note=Calcium 3; via carbonyl oxygen; /evidence=ECO:0000250; METAL 425; /note=Calcium 3; via carbonyl oxygen; /evidence=ECO:0000250 |
| Rhea ID | |
| Cross Reference Brenda | 3.4.24.34; |