IED ID | IndEnz0002006551 |
Enzyme Type ID | protease006551 |
Protein Name |
Neutrophil collagenase EC 3.4.24.34 Matrix metalloproteinase-8 MMP-8 |
Gene Name | Mmp8 |
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 | MLHLKTLPFLFFFHTQLATALPVPPEHLEEKNMKTAENYLRKFYHLPSNQFRSARNATMIAEKLKEMQRFFGLPETGKPDAATIEIMEKPRCGVPDSGDFLLTPGSPKWTHTNLTYRIINHTPQMSKAEVKTEIEKAFKIWSVPSTLTFTETLEGEADINIAFVSRDHGDNSPFDGPNGILAHAFQPGRGIGGDAHFDSEETWTQDSKNYNLFLVAAHEFGHSLGLSHSTDPGALMYPNYAYREPSTYSLPQDDINGIQTIYGPSDNPVQPTGPSTPTACDPHLRFDAATTLRGEIYFFKDKYFWRRHPQLRTVDLNFISLFWPFLPNGLQAAYEDFDRDLVFLFKGRQYWALSAYDLQQGYPRDISNYGFPRSVQAIDAAVSYNGKTYFFVNNQCWRYDNQRRSMDPGYPTSIASVFPGINCRIDAVFQQDSFFLFFSGPQYFAFNLVSRRVTRVARSNLWLNCP |
Enzyme Length | 466 |
Uniprot Accession Number | O88766 |
Absorption | |
Active Site | ACT_SITE 219; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095 |
Activity Regulation | ACTIVITY REGULATION: Cannot be activated without removal of the activation peptide. {ECO:0000250}. |
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. |
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); 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 {ECO:0000250}. Note=Stored in intracellular granules. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | SIGNAL 1..20; /evidence=ECO:0000250 |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | 10773235; 15052653; 16153442; 16940237; 25049354; |
Motif | MOTIF 90..97; /note=Cysteine switch; /evidence=ECO:0000250 |
Gene Encoded By | |
Mass | 53,277 |
Kinetics | |
Metal Binding | METAL 92; /note=Zinc 2; in inhibited form; /evidence=ECO:0000250; METAL 158; /note=Calcium 1; /evidence=ECO:0000250; METAL 168; /note=Zinc 1; /evidence=ECO:0000250; METAL 170; /note=Zinc 1; /evidence=ECO:0000250; METAL 175; /note=Calcium 2; /evidence=ECO:0000250; METAL 176; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250; METAL 178; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250; METAL 180; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250; METAL 183; /note=Zinc 1; /evidence=ECO:0000250; METAL 190; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000250; METAL 192; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000250; METAL 194; /note=Calcium 1; /evidence=ECO:0000250; METAL 196; /note=Zinc 1; /evidence=ECO:0000250; METAL 198; /note=Calcium 2; /evidence=ECO:0000250; METAL 201; /note=Calcium 2; /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 287; /note=Calcium 3; via carbonyl oxygen; /evidence=ECO:0000250; METAL 379; /note=Calcium 3; via carbonyl oxygen; /evidence=ECO:0000250; METAL 426; /note=Calcium 3; via carbonyl oxygen; /evidence=ECO:0000250 |
Rhea ID | |
Cross Reference Brenda |