| IED ID | IndEnz0002006547 |
| Enzyme Type ID | protease006547 |
| Protein Name |
Matrilysin EC 3.4.24.23 Matrin Matrix metalloproteinase-7 MMP-7 Pump-1 protease Uterine metalloproteinase |
| Gene Name | Mmp7 |
| 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 | MQLTLFCFVCLLPGHLALPLSQEAGDVSAHQWEQAQNYLRKFYPHDSKTKKVNSLVDNLKEMQKFFGLPMTGKLSPYIMEIMQKPRCGVPDVAEYSLMPNSPKWHSRIVTYRIVSYTSDLPRIVVDQIVKKALRMWSMQIPLNFKRVSWGTADIIIGFARRDHGDSFPFDGPGNTLGHAFAPGPGLGGDAHFDKDEYWTDGEDAGVNFLFAATHEFGHSLGLSHSSVPGTVMYPTYQRDYSEDFSLTKDDIAGIQKLYGKRNTL |
| Enzyme Length | 264 |
| Uniprot Accession Number | Q10738 |
| Absorption | |
| Active Site | ACT_SITE 215; /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}.; FUNCTION: May play a role in tissue reorganization. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Metal binding (18); Motif (1); Propeptide (1); Sequence conflict (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..17; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 10204802; 10337617; 10359808; 10419448; 10433819; 10607586; 10642592; 10731089; 10934155; 10949577; 10987280; 11217851; 11248802; 11359935; 11733520; 11825873; 11983918; 12045257; 12359768; 12464176; 12466851; 12482850; 12506066; 12815621; 15149334; 15186480; 15201952; 15618213; 15734845; 15748811; 15778706; 15843578; 15921521; 15964556; 16141072; 16230531; 16397239; 16423057; 16515559; 16769909; 16822871; 17017992; 17101148; 17203242; 17218472; 17219436; 17617617; 17638887; 17681175; 17923522; 18334539; 18385523; 18499699; 18606667; 18639653; 18644839; 18663129; 18676849; 18713744; 19002110; 19181662; 19267908; 19329997; 19394326; 19398663; 19429912; 19549527; 19608871; 19668337; 19679556; 19766716; 19795413; 19855381; 19893044; 20048070; 20056603; 20139113; 20215503; 20332116; 20488791; 20616008; 20691176; 20809186; 20864640; 21079048; 21481787; 21991388; 22095947; 22957090; 23100416; 23258229; 23421805; 23554135; 24095877; 24129163; 24624896; 24670518; 24837365; 25118165; 25352026; 25636537; 25770908; 26015543; 26163370; 26933888; 26934381; 26934670; 27398409; 27510977; 27732661; 28622386; 29229950; 29600597; 30878215; 30967475; 31053533; 31743113; 32053892; 32270301; 32468660; 9037065; 9348221; 9722956; 9769324; |
| Motif | MOTIF 85..92; /note=Cysteine switch; /evidence=ECO:0000250 |
| Gene Encoded By | |
| Mass | 29,755 |
| Kinetics | |
| Metal Binding | METAL 87; /note=Zinc 2; in inhibited form; /evidence=ECO:0000250; METAL 153; /note=Calcium 1; /evidence=ECO:0000250; METAL 163; /note=Zinc 1; /evidence=ECO:0000250; METAL 165; /note=Zinc 1; /evidence=ECO:0000250; METAL 170; /note=Calcium 2; /evidence=ECO:0000250; METAL 171; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250; METAL 173; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250; METAL 175; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250; METAL 178; /note=Zinc 1; /evidence=ECO:0000250; METAL 185; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000250; METAL 187; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000250; METAL 189; /note=Calcium 1; /evidence=ECO:0000250; METAL 191; /note=Zinc 1; /evidence=ECO:0000250; METAL 193; /note=Calcium 2; /evidence=ECO:0000250; METAL 196; /note=Calcium 2; /evidence=ECO:0000250; METAL 214; /note=Zinc 2; catalytic; /evidence=ECO:0000250; METAL 218; /note=Zinc 2; catalytic; /evidence=ECO:0000250; METAL 224; /note=Zinc 2; catalytic; /evidence=ECO:0000250 |
| Rhea ID | |
| Cross Reference Brenda | 3.4.24.23; |