| IED ID | IndEnz0002002816 |
| Enzyme Type ID | protease002816 |
| Protein Name |
Matrilysin EC 3.4.24.23 Matrin Matrix metalloproteinase-7 MMP-7 Pump-1 protease Uterine metalloproteinase Fragment |
| Gene Name | MMP7 |
| Organism | Felis catus (Cat) (Felis silvestris catus) |
| 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 Laurasiatheria Carnivora Feliformia Felidae (cat family) Felinae Felis Felis catus (Cat) (Felis silvestris catus) |
| Enzyme Sequence | LCVLCLLPQSPALPLPREAGGHSESQWKQAQEYLKRFYPSDAKSRDADSFGAQLKEMQKFFRLPVTGMLDSRVIVVMQQPRCGLPDTGEDLPSRNRPKWISKVVTYRIISYTRDLPRVTVDHLVAKALNMWSKEIPLSFRRVVLGIPDIVIGFARGAHGDFYPFDGPGGTLAHAYEPGPGLGGDAHFDEDERWADGRGLGINFLAVATHELGHSLGLRHSSDPDSVMYPTYGARDSENFKLSPGDIREIQELYGKRSKSRKK |
| Enzyme Length | 262 |
| Uniprot Accession Number | P55032 |
| Absorption | |
| Active Site | ACT_SITE 210; /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. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Metal binding (18); Motif (1); Non-terminal residue (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..12; /evidence=ECO:0000250 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | MOTIF 80..87; /note=Cysteine switch; /evidence=ECO:0000250 |
| Gene Encoded By | |
| Mass | 29,263 |
| Kinetics | |
| Metal Binding | METAL 82; /note=Zinc 2; in inhibited form; /evidence=ECO:0000250; METAL 148; /note=Calcium 1; /evidence=ECO:0000250; METAL 158; /note=Zinc 1; /evidence=ECO:0000250; METAL 160; /note=Zinc 1; /evidence=ECO:0000250; METAL 165; /note=Calcium 2; /evidence=ECO:0000250; METAL 166; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250; METAL 168; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250; METAL 170; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250; METAL 173; /note=Zinc 1; /evidence=ECO:0000250; METAL 180; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000250; METAL 182; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000250; METAL 184; /note=Calcium 1; /evidence=ECO:0000250; METAL 186; /note=Zinc 1; /evidence=ECO:0000250; METAL 188; /note=Calcium 2; /evidence=ECO:0000250; METAL 191; /note=Calcium 2; /evidence=ECO:0000250; METAL 209; /note=Zinc 2; catalytic; /evidence=ECO:0000250; METAL 213; /note=Zinc 2; catalytic; /evidence=ECO:0000250; METAL 219; /note=Zinc 2; catalytic; /evidence=ECO:0000250 |
| Rhea ID | |
| Cross Reference Brenda |