| IED ID | IndEnz0002004577 |
| Enzyme Type ID | protease004577 |
| Protein Name |
Collagenase 3 EC 3.4.24.- Matrix metalloproteinase-13 MMP-13 |
| Gene Name | MMP13 |
| Organism | Oryctolagus cuniculus (Rabbit) |
| 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) Lagomorpha Leporidae (rabbits and hares) Oryctolagus Oryctolagus cuniculus (Rabbit) |
| Enzyme Sequence | MQPGVLAACLLLSWTHCWSLPLLNSNEDDDLSEEDFQFAESYLRSYYHPLNPAGILKKNAAGSMVDRLREMQSFFGLEVTGKLDDNTLAIMKQPRCGVPDVGEYNVFPRTLKWSQTNLTYRIVNYTPDLTHSEVEKAFKKAFKVWSDVTPLNFTRIHNGTADIMISFGTKEHGDFYPFDGPSGLLAHAFPPGPNYGGDAHFDDDETWTSSSKGYNLFLVAAHEFGHSLGLDHSKDPGALMFPIYTYTGKSHFMLPDDDVQGIQSLYGPGDEDPNPKHPKTPDKCDPSLSLDAITSLRGETMIFKDRFFWRLHPQQVDAELFLTKSFWPELPNRIDAAYEHPARDLIFIFRGKKFWAPNGYDILEGYPQKLSELGFPREVKKISAAVHFEDTGKTLFFSGNQVWSYDDTNHTMDQDYPRLIEEEFPGIGGKVDAVYEKNGYIYFFNGPIQFEYSIWSKRIVRVMPTNSLLWC |
| Enzyme Length | 471 |
| Uniprot Accession Number | O62806 |
| Absorption | |
| Active Site | ACT_SITE 223; /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 (4); Metal binding (30); Modified residue (1); Motif (1); Propeptide (1); Region (3); 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 366; /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 94..101; /note=Cysteine switch; /evidence=ECO:0000250 |
| Gene Encoded By | |
| Mass | 53,693 |
| Kinetics | |
| Metal Binding | METAL 96; /note=Zinc 2; in inhibited form; /evidence=ECO:0000250; METAL 128; /note=Calcium 1; /evidence=ECO:0000250; METAL 162; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250; METAL 172; /note=Zinc 1; via tele nitrogen; /evidence=ECO:0000250; METAL 174; /note=Zinc 1; /evidence=ECO:0000250; METAL 179; /note=Calcium 3; /evidence=ECO:0000250; METAL 180; /note=Calcium 3; via carbonyl oxygen; /evidence=ECO:0000250; METAL 182; /note=Calcium 3; via carbonyl oxygen; /evidence=ECO:0000250; METAL 184; /note=Calcium 3; via carbonyl oxygen; /evidence=ECO:0000250; METAL 187; /note=Zinc 1; via tele nitrogen; /evidence=ECO:0000250; METAL 194; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250; METAL 196; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250; METAL 198; /note=Calcium 2; /evidence=ECO:0000250; METAL 200; /note=Zinc 1; via pros nitrogen; /evidence=ECO:0000250; METAL 202; /note=Calcium 3; /evidence=ECO:0000250; METAL 203; /note=Calcium 1; /evidence=ECO:0000250; METAL 205; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000250; METAL 205; /note=Calcium 3; /evidence=ECO:0000250; METAL 222; /note=Zinc 2; via tele nitrogen; catalytic; /evidence=ECO:0000250; METAL 226; /note=Zinc 2; via tele nitrogen; catalytic; /evidence=ECO:0000250; METAL 232; /note=Zinc 2; via tele nitrogen; catalytic; /evidence=ECO:0000250; METAL 240; /note=Zinc 2; via carbonyl oxygen; catalytic; /evidence=ECO:0000250; METAL 291; /note=Calcium 4; via carbonyl oxygen; /evidence=ECO:0000250; METAL 293; /note=Calcium 5; via carbonyl oxygen; /evidence=ECO:0000250; METAL 335; /note=Calcium 4; via carbonyl oxygen; /evidence=ECO:0000250; METAL 337; /note=Calcium 5; via carbonyl oxygen; /evidence=ECO:0000250; METAL 383; /note=Calcium 4; via carbonyl oxygen; /evidence=ECO:0000250; METAL 385; /note=Calcium 5; via carbonyl oxygen; /evidence=ECO:0000250; METAL 432; /note=Calcium 4; via carbonyl oxygen; /evidence=ECO:0000250; METAL 434; /note=Calcium 5; via carbonyl oxygen; /evidence=ECO:0000250 |
| Rhea ID | |
| Cross Reference Brenda |