| IED ID | IndEnz0002006317 |
| Enzyme Type ID | protease006317 |
| Protein Name |
Collagenase 3 EC 3.4.24.- Matrix metalloproteinase-13 MMP-13 UMRCASE Fragment |
| Gene Name | Mmp13 |
| Organism | Rattus norvegicus (Rat) |
| 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) Rodentia Myomorpha (mice and others) Muroidea Muridae Murinae Rattus Rattus norvegicus (Rat) |
| Enzyme Sequence | ATFFLLSWTHCWSLPLPYGDDDDDDLSEEDLEFAEHYLKSYYHPVTLAGILKKSTVTSTVDRLREMQSFFGLDVTGKLDDPTLDIMRKPRCGVPDVGVYNVFPRTLKWSQTNLTYRIVNYTPDISHSEVEKAFRKAFKVWSDVTPLNFTRIHDGTADIMISFGTKEHGDFYPFDGPSGLLAHAFPPGPNLGGDAHFDDDETWTSSSKGYNLFIVAAHELGHSLGLDHSKDPGALMFPIYTYTGKSHFMLPDDDVQGIQSLYGPGDEDPNPKHPKTPEKCDPALSLDAITSLRGETMIFKDRFFWRLHPQQVEPELFLTKSFWPELPNHVDAAYEHPSRDLMFIFRGRKFWALNGYDIMEGYPRKISDLGFPKEVKRLSAAVHFEDTGKTLFFSGNHVWSYDDANQTMDKDYPRLIEEEFPGIGDKVDAVYEKNGYIYFFNGPIQFEYSIWSNRIVRVMPTNSLLWC |
| Enzyme Length | 466 |
| Uniprot Accession Number | P23097 |
| Absorption | |
| Active Site | ACT_SITE 218; /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); Non-terminal residue (1); Propeptide (1); Region (3); Repeat (4); Signal peptide (1) |
| Keywords | Calcium;Collagen degradation;Direct protein sequencing;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 361; /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..13; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 10430840; 10514495; 10528234; 10537164; 10623612; 10646117; 10773234; 10773235; 11435459; 11751895; 11850435; 12061388; 12213812; 12663239; 12771515; 14645243; 14751562; 14982932; 15026307; 15375341; 15475197; 15601621; 15609084; 15782494; 15883642; 16112096; 16256123; 16286264; 16639721; 16961140; 16965566; 17116693; 17485851; 17530714; 17568546; 17607299; 17623656; 17941091; 18039280; 18052689; 18404723; 18464888; 18470577; 18807189; 18814267; 18985055; 19050895; 19063844; 19121369; 19241444; 19300451; 19346731; 19393988; 19847888; 20056896; 20097749; 20472983; 20870727; 20948465; 21055467; 21180139; 21246051; 21342246; 21447140; 21450970; 21856922; 22357747; 22517354; 22670655; 22890185; 22961837; 22992737; 23192728; 23277113; 23325540; 23974514; 23981230; 24126863; 24244039; 25128628; 25190659; 25595313; 26558633; 26721462; 28157489; 28265573; 28419442; 29860993; 29928874; 31061278; 31258642; 31666602; 31960421; 34830409; 8691099; 8910479; 9553127; 9614183; |
| Motif | MOTIF 89..96; /note=Cysteine switch; /evidence=ECO:0000250 |
| Gene Encoded By | |
| Mass | 53,375 |
| Kinetics | |
| Metal Binding | METAL 91; /note=Zinc 2; in inhibited form; /evidence=ECO:0000250; METAL 123; /note=Calcium 1; /evidence=ECO:0000250; METAL 157; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250; METAL 167; /note=Zinc 1; via tele nitrogen; /evidence=ECO:0000250; METAL 169; /note=Zinc 1; /evidence=ECO:0000250; METAL 174; /note=Calcium 3; /evidence=ECO:0000250; METAL 175; /note=Calcium 3; via carbonyl oxygen; /evidence=ECO:0000250; METAL 177; /note=Calcium 3; via carbonyl oxygen; /evidence=ECO:0000250; METAL 179; /note=Calcium 3; via carbonyl oxygen; /evidence=ECO:0000250; METAL 182; /note=Zinc 1; via tele nitrogen; /evidence=ECO:0000250; METAL 189; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250; METAL 191; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250; METAL 193; /note=Calcium 2; /evidence=ECO:0000250; METAL 195; /note=Zinc 1; via pros nitrogen; /evidence=ECO:0000250; METAL 197; /note=Calcium 3; /evidence=ECO:0000250; METAL 198; /note=Calcium 1; /evidence=ECO:0000250; METAL 200; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000250; METAL 200; /note=Calcium 3; /evidence=ECO:0000250; METAL 217; /note=Zinc 2; via tele nitrogen; catalytic; /evidence=ECO:0000250; METAL 221; /note=Zinc 2; via tele nitrogen; catalytic; /evidence=ECO:0000250; METAL 227; /note=Zinc 2; via tele nitrogen; catalytic; /evidence=ECO:0000250; METAL 235; /note=Zinc 2; via carbonyl oxygen; catalytic; /evidence=ECO:0000250; METAL 286; /note=Calcium 4; via carbonyl oxygen; /evidence=ECO:0000250; METAL 288; /note=Calcium 5; via carbonyl oxygen; /evidence=ECO:0000250; METAL 330; /note=Calcium 4; via carbonyl oxygen; /evidence=ECO:0000250; METAL 332; /note=Calcium 5; via carbonyl oxygen; /evidence=ECO:0000250; METAL 378; /note=Calcium 4; via carbonyl oxygen; /evidence=ECO:0000250; METAL 380; /note=Calcium 5; via carbonyl oxygen; /evidence=ECO:0000250; METAL 427; /note=Calcium 4; via carbonyl oxygen; /evidence=ECO:0000250; METAL 429; /note=Calcium 5; via carbonyl oxygen; /evidence=ECO:0000250 |
| Rhea ID | |
| Cross Reference Brenda | 3.4.24.B4; |