Detail Information for IndEnz0002006551
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