| IED ID | IndEnz0002016332 |
| Enzyme Type ID | protease016332 |
| Protein Name |
Matrilysin EC 3.4.24.23 Matrin Matrix metalloproteinase-7 MMP-7 Pump-1 protease Uterine metalloproteinase |
| Gene Name | Mmp7 Mmp-7 |
| 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 | MAAMRLTLFRIVCLLPGCLALPLSQEAGEVTALQWEQAQNYLRKFYLHDSKTKKATSAVDKLREMQKFFGLPETGKLSPRVMEIMQKPRCGVPDVAEFSLMPNSPKWHSRTVTYRIVSYTTDLPRFLVDQIVKRALRMWSMQIPLNFKRVSWGTADIIIGFARGDHGDNFPFDGPGNTLGHAFAPGPGLGGDAHFDKDEYWTDGEDSGVNFLFVATHELGHSLGLGHSSVPSSVMYPTYQGDHSEDFSLTKDDIAGIQKLYGKRNKL |
| Enzyme Length | 267 |
| Uniprot Accession Number | P50280 |
| Absorption | |
| Active Site | ACT_SITE 218; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Cleavage of 14-Ala-|-Leu-15 and 16-Tyr-|-Leu-17 in B chain of insulin. No action on collagen types I, II, IV, V. Cleaves gelatin chain alpha-2(I) > alpha-1(I).; EC=3.4.24.23; |
| DNA Binding | |
| EC Number | 3.4.24.23 |
| Enzyme Function | FUNCTION: Degrades casein, gelatins of types I, III, IV, and V, and fibronectin. Activates procollagenase (By similarity). {ECO:0000250}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Metal binding (18); Motif (1); Propeptide (1); Signal peptide (1) |
| Keywords | Calcium;Collagen degradation;Extracellular matrix;Hydrolase;Metal-binding;Metalloprotease;Protease;Reference proteome;Secreted;Signal;Zinc;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000305}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..20; /evidence=ECO:0000250 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 10070364; 10645258; 10660581; 11406539; 12875773; 12923405; 15182445; 15894268; 17027671; 17670906; 18209025; 18644839; 19398663; 20054150; 20098355; 21139058; 21567117; 21935365; 23256367; 23313213; 9546322; 9549496; 9888422; |
| Motif | MOTIF 88..95; /note=Cysteine switch; /evidence=ECO:0000250 |
| Gene Encoded By | |
| Mass | 29,885 |
| Kinetics | |
| Metal Binding | METAL 90; /note=Zinc 2; in inhibited form; /evidence=ECO:0000250; METAL 156; /note=Calcium 1; /evidence=ECO:0000250; METAL 166; /note=Zinc 1; /evidence=ECO:0000250; METAL 168; /note=Zinc 1; /evidence=ECO:0000250; METAL 173; /note=Calcium 2; /evidence=ECO:0000250; METAL 174; /note=Calcium 2; via carbonyl oxygen; /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 181; /note=Zinc 1; /evidence=ECO:0000250; METAL 188; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000250; METAL 190; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000250; METAL 192; /note=Calcium 1; /evidence=ECO:0000250; METAL 194; /note=Zinc 1; /evidence=ECO:0000250; METAL 196; /note=Calcium 2; /evidence=ECO:0000250; METAL 199; /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 |
| Rhea ID | |
| Cross Reference Brenda | 3.4.24.23; |