| IED ID | IndEnz0002006522 |
| Enzyme Type ID | protease006522 |
| Protein Name |
Matrix metalloproteinase-20 MMP-20 EC 3.4.24.- Enamel metalloproteinase Enamelysin |
| Gene Name | MMP20 |
| Organism | Sus scrofa (Pig) |
| 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 Suina Suidae (pigs) Sus Sus scrofa (Pig) |
| Enzyme Sequence | MKVLPASGLAVLLVTALKFSAAAPSLFAATPRTSRNNYHLAQAYLDKYYTKKGGHQVGEMVAKGGNSMVKKIKELQAFFGLRVTGKLDRTTMDVIKRPRCGVPDVANYRLFPGEPKWKKNTLTYRISKYTPSMTPAEVDKAMEMALQAWSSAVPLSFVRVNAGEADIMISFETGDHGDSYPFDGPRGTLAHAFAPGEGLGGDTHFDNAEKWTMGMNGFNLFTVAAHEFGHALGLAHSTDPSALMYPTYKYQNPYGFHLPKDDVKGIQALYGPRKTFTGKPTVPHGPPHNPSLPDICDSSSSFDAVTMLGKELLFFRDRIFWRRQVHLMSGIRPSTITSSFPQLMSNVDAAYEVADRGMAYFFKGPHYWITRGFQMQGPPRTIYDFGFPRYVQRIDAAVHLKDTQKTLFFVGDEYYSYDERKRKMDKDYPKNTEEEFSGVNGQIDAAVELNGYIYFFSGPKAYKYDTEKEDVVSVLKSNSWIGC |
| Enzyme Length | 483 |
| Uniprot Accession Number | P79287 |
| Absorption | |
| Active Site | ACT_SITE 227; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.24.- |
| Enzyme Function | FUNCTION: Degrades amelogenin, the major protein component of the enamel matrix and two of the macromolecules characterizing the cartilage extracellular matrix: aggrecan and the cartilage oligomeric matrix protein (COMP). May play a central role in tooth enamel formation (By similarity). {ECO:0000250}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Disulfide bond (1); Metal binding (21); Motif (1); Propeptide (1); Repeat (4); Signal peptide (1) |
| Keywords | Autocatalytic cleavage;Calcium;Disulfide bond;Extracellular matrix;Hydrolase;Metal-binding;Metalloprotease;Protease;Reference proteome;Repeat;Secreted;Signal;Zinc;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250}. |
| Modified Residue | |
| Post Translational Modification | PTM: Autoactivates at least at the 107-Asn-|-Tyr-108 site. {ECO:0000250}. |
| Signal Peptide | SIGNAL 1..22; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 20400724; |
| Motif | MOTIF 98..105; /note=Cysteine switch; /evidence=ECO:0000250 |
| Gene Encoded By | |
| Mass | 54,085 |
| Kinetics | |
| Metal Binding | METAL 100; /note=Zinc 1; in inhibited form; /evidence=ECO:0000250; METAL 164; /note=Calcium 1; /evidence=ECO:0000250; METAL 165; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000250; METAL 166; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000250; METAL 176; /note=Zinc 2; /evidence=ECO:0000250; METAL 178; /note=Zinc 2; /evidence=ECO:0000250; METAL 183; /note=Calcium 2; /evidence=ECO:0000250; METAL 184; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250; METAL 186; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250; METAL 188; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250; METAL 191; /note=Zinc 2; /evidence=ECO:0000250; METAL 197; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000250; METAL 198; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000250; METAL 200; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000250; METAL 202; /note=Calcium 1; /evidence=ECO:0000250; METAL 204; /note=Zinc 2; /evidence=ECO:0000250; METAL 206; /note=Calcium 2; /evidence=ECO:0000250; METAL 209; /note=Calcium 2; /evidence=ECO:0000250; METAL 226; /note=Zinc 1; catalytic; /evidence=ECO:0000250; METAL 230; /note=Zinc 1; catalytic; /evidence=ECO:0000250; METAL 236; /note=Zinc 1; catalytic; /evidence=ECO:0000250 |
| Rhea ID | |
| Cross Reference Brenda | 3.4.24.B6; |