| IED ID | IndEnz0002006538 |
| Enzyme Type ID | protease006538 |
| Protein Name |
72 kDa type IV collagenase EC 3.4.24.24 72 kDa gelatinase Matrix metalloproteinase-2 MMP-2 Cleaved into: PEX |
| Gene Name | MMP2 |
| Organism | Bos taurus (Bovine) |
| 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 Artiodactyla Ruminantia Pecora Bovidae Bovinae Bos (oxen cattle) Bos taurus (Bovine) |
| Enzyme Sequence | MTEARVSRGALAALLRALCALGCLLGRAAAAPSPIIKFPGDVAPKTDKELAVQYLNTFYGCPKESCNLFVLKDTLKKMQKFFGLPQTGELDQSTIETMRKPRCGNPDVANYNFFPRKPKWDKNQITYRIIGYTPDLDPQTVDDAFARAFQVWSDVTPLRFSRIHDGEADIMINFGRWEHGDGYPFDGKDGLLAHAFAPGPGVGGDSHFDDDELRTLGEGQVVRVKYGNADGEYCKFPFRFNGKEYTSCTDTGRSDGFLWCSTTYNFDKDGKYGFCPHEALFTMGGNADGQPCKFPFRFQGTSYDSCTTEGRTDGYRWCGTTEDYDRDKEYGFCPETAMSTVGGNSEGAPCVLPFTFLGNKHESCTSAGRSDGKLWCATTSNYDDDRKWGFCPDQGYSLFLVAAHEFGHAMGLEHSQDPGALMAPIYTYTKNFRLSHDDIQGIQELYGASPDIDTGTGPTPTLGPVTPELCKQDIVFDGISQIRGEIFFFKDRFIWRTVTPRDKPTGPLLVATFWPELPEKIDAVYEDPQEEKAVFFAGNEYWVYSASTLERGYPKPLTSLGLPPGVQKVDAAFNWSKNKKTYIFAGDKFWRYNEVKKKMDPGFPKLIADAWNAIPDNLDAVVDLQGGGHSYFFKGAYYLKLENQSLKSVKFGSIKSDWLGC |
| Enzyme Length | 661 |
| Uniprot Accession Number | Q9GLE5 |
| Absorption | |
| Active Site | ACT_SITE 405; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Cleavage of gelatin type I and collagen types IV, V, VII, X. Cleaves the collagen-like sequence Pro-Gln-Gly-|-Ile-Ala-Gly-Gln.; EC=3.4.24.24; Evidence={ECO:0000250|UniProtKB:P08253}; |
| DNA Binding | |
| EC Number | 3.4.24.24 |
| Enzyme Function | FUNCTION: Ubiquitinous metalloproteinase that is involved in diverse functions such as remodeling of the vasculature, angiogenesis, tissue repair, tumor invasion, inflammation, and atherosclerotic plaque rupture. As well as degrading extracellular matrix proteins, can also act on several nonmatrix proteins such as big endothelial 1 and beta-type CGRP promoting vasoconstriction. Also cleaves KISS at a Gly-|-Leu bond. Appears to have a role in myocardial cell death pathways. Contributes to myocardial oxidative stress by regulating the activity of GSK3beta. Cleaves GSK3beta in vitro. Involved in the formation of the fibrovascular tissues (By similarity). {ECO:0000250}.; FUNCTION: PEX, the C-terminal non-catalytic fragment of MMP2, posseses anti-angiogenic and anti-tumor properties and inhibits cell migration and cell adhesion to FGF2 and vitronectin. Ligand for integrin alpha-v/beta-3 on the surface of blood vessels (By similarity). {ECO:0000250}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (2); Disulfide bond (7); Domain (3); Glycosylation (2); Metal binding (23); Motif (1); Propeptide (1); Region (4); Repeat (4); Signal peptide (1) |
| Keywords | Angiogenesis;Calcium;Collagen degradation;Disulfide bond;Extracellular matrix;Glycoprotein;Hydrolase;Membrane;Metal-binding;Metalloprotease;Nucleus;Phosphoprotein;Protease;Reference proteome;Repeat;Secreted;Signal;Zinc;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250}. Membrane {ECO:0000250}. Nucleus {ECO:0000250}. Note=Colocalizes with integrin alphaV/beta3 at the membrane surface in angiogenic blood vessels and melanomas. Found in mitochondria, along microfibrils, and in nuclei of cardiomyocytes (By similarity). {ECO:0000250}. |
| Modified Residue | |
| Post Translational Modification | PTM: Phosphorylation on multiple sites modulates enzymatic activity. Phosphorylated by PKC in vitro (By similarity). {ECO:0000250}.; PTM: The propeptide is processed by MMP14 (MT-MMP1) and MMP16 (MT-MMP3). Autocatalytic cleavage in the C-terminal produces the anti-angiogenic peptide, PEX. This processing appears to be facilitated by binding integrinv/beta3 (By similarity). {ECO:0000250}. |
| Signal Peptide | SIGNAL 1..30; /evidence=ECO:0000250|UniProtKB:P33436 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | MOTIF 101..108; /note=Cysteine switch; /evidence=ECO:0000250 |
| Gene Encoded By | |
| Mass | 73,777 |
| Kinetics | |
| Metal Binding | METAL 103; /note=Zinc 1; in inhibited form; /evidence=ECO:0000250|UniProtKB:P08253; METAL 135; /note=Calcium 1; /evidence=ECO:0000250|UniProtKB:P08253; METAL 169; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P08253; METAL 179; /note=Zinc 2; /evidence=ECO:0000250|UniProtKB:P08253; METAL 181; /note=Zinc 2; /evidence=ECO:0000250|UniProtKB:P08253; METAL 186; /note=Calcium 3; /evidence=ECO:0000250|UniProtKB:P08253; METAL 187; /note=Calcium 3; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P08253; METAL 194; /note=Zinc 2; /evidence=ECO:0000250|UniProtKB:P08253; METAL 201; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P08253; METAL 203; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P08253; METAL 205; /note=Calcium 2; /evidence=ECO:0000250|UniProtKB:P08253; METAL 207; /note=Zinc 2; /evidence=ECO:0000250|UniProtKB:P08253; METAL 209; /note=Calcium 3; /evidence=ECO:0000250|UniProtKB:P08253; METAL 210; /note=Calcium 1; /evidence=ECO:0000250|UniProtKB:P08253; METAL 212; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P08253; METAL 212; /note=Calcium 3; /evidence=ECO:0000250|UniProtKB:P08253; METAL 404; /note=Zinc 1; catalytic; /evidence=ECO:0000250|UniProtKB:P08253; METAL 408; /note=Zinc 1; catalytic; /evidence=ECO:0000250|UniProtKB:P08253; METAL 414; /note=Zinc 1; catalytic; /evidence=ECO:0000250|UniProtKB:P08253; METAL 477; /note=Calcium 4; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P08253; METAL 522; /note=Calcium 4; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P08253; METAL 570; /note=Calcium 4; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P08253; METAL 619; /note=Calcium 4; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P08253 |
| Rhea ID | |
| Cross Reference Brenda |