| IED ID | IndEnz0002016240 |
| Enzyme Type ID | protease016240 |
| Protein Name |
Collagenase 3 EC 3.4.24.- Matrix metalloproteinase-13 MMP-13 Fragment |
| Gene Name | mmp13 |
| Organism | Xenopus laevis (African clawed frog) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amphibia Batrachia Anura Pipoidea Pipidae Xenopodinae Xenopus Xenopus Xenopus laevis (African clawed frog) |
| Enzyme Sequence | SSLSVLVLSLSFAYCLSAPVPQDEDSELTPGDLQLAEHYLNRLYSSSSNPVGMLRMKNVNSIETKLKEMQSFFGLEVTGKLNEDTLDIMKQPRCGVPDVGQYNFFPRKLKWPRNNLTYRIVNYTPDLSTSEVDRAIKKALKVWSDVTPLNFTRLRTGTADIMVSFGKKEHGDYYPFDGPDGLLAHAFPPGEKLGGDTHFDDDEMFSTDNKGYNLFVVAAHEFGHALGLDHSRDPGSLMFPVYTYTETSRFVLPDDDVQGIQVLYGPGNRDPHPKHPKTPEKCDPDLSIDAITELRGEKMIFKDRFFWRVHPQMTDAELVLIKSFWPELPNKLDAAYEHPAKDLSYLFRGKKFWALNGYDIVEDYPKKLHELGFPKTLKAIDAAVYNKDTGKTFFFTEDSYWSFDEEARTLDKGFPRLISEDFPGIGEKVDAAYQRNGYLYFFNGALQFEYSIWSQRITRILKTNFVLMC |
| Enzyme Length | 469 |
| Uniprot Accession Number | Q10835 |
| Absorption | |
| Active Site | ACT_SITE 221; /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 several types of triple helical collagen. May also function by activating or degrading key regulatory proteins. Plays a role in wound healing, tissue remodeling, cartilage degradation, bone development, bone mineralization and ossification (By similarity). {ECO:0000250}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Disulfide bond (1); Glycosylation (2); Metal binding (26); Motif (1); Non-terminal residue (1); Propeptide (1); Region (1); Repeat (4); Signal peptide (1) |
| Keywords | Calcium;Collagen degradation;Disulfide bond;Extracellular matrix;Glycoprotein;Hydrolase;Metal-binding;Metalloprotease;Protease;Repeat;Secreted;Signal;Zinc;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250}. Secreted {ECO:0000250}. |
| Modified Residue | |
| Post Translational Modification | PTM: The proenzyme is activated by removal of the propeptide; this cleavage can be effected by other matrix metalloproteinases 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}. |
| Signal Peptide | SIGNAL <1..17; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | MOTIF 92..99; /note=Cysteine switch; /evidence=ECO:0000250 |
| Gene Encoded By | |
| Mass | 53,641 |
| Kinetics | |
| Metal Binding | METAL 94; /note=Zinc 2; in inhibited form; /evidence=ECO:0000250; METAL 126; /note=Calcium 1; /evidence=ECO:0000250; METAL 160; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250; METAL 170; /note=Zinc 1; via tele nitrogen; /evidence=ECO:0000250; METAL 172; /note=Zinc 1; /evidence=ECO:0000250; METAL 177; /note=Calcium 3; /evidence=ECO:0000250; METAL 178; /note=Calcium 3; via carbonyl oxygen; /evidence=ECO:0000250; METAL 182; /note=Calcium 3; via carbonyl oxygen; /evidence=ECO:0000250; METAL 185; /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; /evidence=ECO:0000250; METAL 198; /note=Zinc 1; via pros nitrogen; /evidence=ECO:0000250; METAL 200; /note=Calcium 3; /evidence=ECO:0000250; METAL 201; /note=Calcium 1; /evidence=ECO:0000250; METAL 203; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000250; METAL 203; /note=Calcium 3; /evidence=ECO:0000250; METAL 220; /note=Zinc 2; via tele nitrogen; catalytic; /evidence=ECO:0000250; METAL 224; /note=Zinc 2; via tele nitrogen; catalytic; /evidence=ECO:0000250; METAL 230; /note=Zinc 2; via tele nitrogen; catalytic; /evidence=ECO:0000250; METAL 238; /note=Zinc 2; via carbonyl oxygen; catalytic; /evidence=ECO:0000250; METAL 289; /note=Calcium 4; via carbonyl oxygen; /evidence=ECO:0000250; METAL 291; /note=Calcium 5; via carbonyl oxygen; /evidence=ECO:0000250; METAL 333; /note=Calcium 4; via carbonyl oxygen; /evidence=ECO:0000250; METAL 335; /note=Calcium 5; via carbonyl oxygen; /evidence=ECO:0000250; METAL 383; /note=Calcium 5; via carbonyl oxygen; /evidence=ECO:0000250; METAL 430; /note=Calcium 4; via carbonyl oxygen; /evidence=ECO:0000250 |
| Rhea ID | |
| Cross Reference Brenda | 3.4.24.B4; |