| IED ID | IndEnz0002008098 |
| Enzyme Type ID | protease008098 |
| Protein Name |
Collagenase 3 EC 3.4.24.- Matrix metalloproteinase-13 MMP-13 |
| Gene Name | MMP13 |
| Organism | Equus caballus (Horse) |
| 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 Perissodactyla (odd-toed ungulates) Equidae (horses) Equus Equus Equus caballus (Horse) |
| Enzyme Sequence | MHPGVLAAFLFLSWTRCWSLPVPNDDDDDDDMSEEDFQLAERYLKSYYYPLNPAGILKKTAANSVVDRLREMQSFFGLEVTGKLDDNTLDIMKKPRCGVPDVGEYNVFPRTLKWPKMNLTYRIVNYTPDLTHSEVEKAFKKAFKVWSDVTPLNFTRLYNGTADIMISFGTKEHGDFYPFDGPSGLLAHAFPPGPNYGGDAHFDDDETWTSSSKGYNLFLVAAHEFGHSLGLDHSKDPGALMFPIYTYTGKSHFVLPDDDVQGIQYLYGPGDEDPNPKHPKTPDKCDPSLSLDAITSLRGETMVFKDRFFWRLHPQLVDAELFLTKSFWPELPNRIDAAYEHPSKDLIFIFRGRKFWALNGYDILEGYPQKISELGFPKDVKKISAAVHFEDTGKTLFFSGNQVWRYDDTNRMMDKDYPRLIEEDFPGIGDKVDAVYEKNGYIYFFNGPIQFEYSIWSNRIVRVMPTNSLLWC |
| Enzyme Length | 472 |
| Uniprot Accession Number | O18927 |
| Absorption | |
| Active Site | ACT_SITE 224; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.24.- |
| Enzyme Function | FUNCTION: Plays a role in the degradation of extracellular matrix proteins including fibrillar collagen, fibronectin, TNC and ACAN. Cleaves triple helical collagens, including type I, type II and type III collagen, but has the highest activity with soluble type II collagen. Can also degrade collagen type IV, type XIV and type X. May also function by activating or degrading key regulatory proteins, such as TGFB1 and CCN2. Plays a role in wound healing, tissue remodeling, cartilage degradation, bone development, bone mineralization and ossification. Required for normal embryonic bone development and ossification. Plays a role in the healing of bone fractures via endochondral ossification. Plays a role in wound healing, probably by a mechanism that involves proteolytic activation of TGFB1 and degradation of CCN2. Plays a role in keratinocyte migration during wound healing. May play a role in cell migration and in tumor cell invasion (By similarity). {ECO:0000250}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Disulfide bond (1); Glycosylation (3); Metal binding (30); Modified residue (1); Motif (1); Propeptide (1); Region (2); Repeat (4); Signal peptide (1) |
| Keywords | Calcium;Collagen degradation;Disulfide bond;Extracellular matrix;Glycoprotein;Hydrolase;Metal-binding;Metalloprotease;Phosphoprotein;Protease;Reference proteome;Repeat;Secreted;Signal;Zinc;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000305}. Secreted {ECO:0000250}. |
| Modified Residue | MOD_RES 367; /note=Phosphotyrosine; by PKDCC; /evidence=ECO:0000250|UniProtKB:P45452 |
| Post Translational Modification | PTM: The proenzyme is activated by removal of the propeptide; this cleavage can be effected by other matrix metalloproteinases, such as MMP2, MMP3 and MMP14 and may involve several cleavage steps. Cleavage can also be autocatalytic, after partial maturation by another protease or after treatment with 4-aminophenylmercuric acetate (APMA) (in vitro) (By similarity). {ECO:0000250}.; PTM: N-glycosylated. {ECO:0000250}.; PTM: Tyrosine phosphorylated by PKDCC/VLK. {ECO:0000250|UniProtKB:P45452}. |
| Signal Peptide | SIGNAL 1..19; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | MOTIF 95..102; /note=Cysteine switch; /evidence=ECO:0000250 |
| Gene Encoded By | |
| Mass | 54,226 |
| Kinetics | |
| Metal Binding | METAL 97; /note=Zinc 2; in inhibited form; /evidence=ECO:0000250; METAL 129; /note=Calcium 1; /evidence=ECO:0000250; METAL 163; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250; METAL 173; /note=Zinc 1; via tele nitrogen; /evidence=ECO:0000250; METAL 175; /note=Zinc 1; /evidence=ECO:0000250; METAL 180; /note=Calcium 3; /evidence=ECO:0000250; METAL 181; /note=Calcium 3; via carbonyl oxygen; /evidence=ECO:0000250; METAL 183; /note=Calcium 3; via carbonyl oxygen; /evidence=ECO:0000250; METAL 185; /note=Calcium 3; via carbonyl oxygen; /evidence=ECO:0000250; METAL 188; /note=Zinc 1; via tele nitrogen; /evidence=ECO:0000250; METAL 195; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250; METAL 197; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250; METAL 199; /note=Calcium 2; /evidence=ECO:0000250; METAL 201; /note=Zinc 1; via pros nitrogen; /evidence=ECO:0000250; METAL 203; /note=Calcium 3; /evidence=ECO:0000250; METAL 204; /note=Calcium 1; /evidence=ECO:0000250; METAL 206; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000250; METAL 206; /note=Calcium 3; /evidence=ECO:0000250; METAL 223; /note=Zinc 2; via tele nitrogen; catalytic; /evidence=ECO:0000250; METAL 227; /note=Zinc 2; via tele nitrogen; catalytic; /evidence=ECO:0000250; METAL 233; /note=Zinc 2; via tele nitrogen; catalytic; /evidence=ECO:0000250; METAL 241; /note=Zinc 2; via carbonyl oxygen; catalytic; /evidence=ECO:0000250; METAL 292; /note=Calcium 4; via carbonyl oxygen; /evidence=ECO:0000250; METAL 294; /note=Calcium 5; via carbonyl oxygen; /evidence=ECO:0000250; METAL 336; /note=Calcium 4; via carbonyl oxygen; /evidence=ECO:0000250; METAL 338; /note=Calcium 5; via carbonyl oxygen; /evidence=ECO:0000250; METAL 384; /note=Calcium 4; via carbonyl oxygen; /evidence=ECO:0000250; METAL 386; /note=Calcium 5; via carbonyl oxygen; /evidence=ECO:0000250; METAL 433; /note=Calcium 4; via carbonyl oxygen; /evidence=ECO:0000250; METAL 435; /note=Calcium 5; via carbonyl oxygen; /evidence=ECO:0000250 |
| Rhea ID | |
| Cross Reference Brenda | 3.4.24.B4; |