| IED ID | IndEnz0002006518 |
| Enzyme Type ID | protease006518 |
| Protein Name |
Interstitial collagenase A EC 3.4.24.7 Matrix metalloproteinase-1a MMP-1a Mcol-A |
| Gene Name | Mmp1a McolA |
| Organism | Mus musculus (Mouse) |
| 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 Mus Mus Mus musculus (Mouse) |
| Enzyme Sequence | MPSLPLLLLLWAASSYSFPVFHNGDRQNVETVWKYLENYYNLGKNMQAKNVNGKEMMAEKLRQMQQLFGLKVTGNSDPETLRAMKKPRCGVPDVAPYAITHNNPRWTKTHLTYSILNYTPYLPKAVVEDAIARAFRVWSDVTPLTFQRVFEEEGDIVLSFHRGDHGDNNPFDGPNYKLAHTFQPGPGLGGDVHYDLDETWTNSSENFNLFYVTAHELGHSLGLTHSSDIGALMFPSYTWYTEDFVLNQDDINRIQDLYGPSPNPIQPTGATTPHPCNGDLTFDAITTFRGEVFFFKGRFYIRVNRFMPEPELNLIGILWPNLPVKLDAAYEASMIDQVRYFKGSKVWAVQEQSVLRGFPRDIHSFFGFPSNVTHIDAAVCEEETGKTYFFVDHMYWRYDENTQSMDPGYPRLTAEDFPGIDDKVDDVFQKGENFYFFHQSVQHRFNLQIRRVDDSRDSSTWFNC |
| Enzyme Length | 464 |
| Uniprot Accession Number | Q9EPL5 |
| Absorption | |
| Active Site | ACT_SITE 216; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095 |
| Activity Regulation | ACTIVITY REGULATION: Can be activated without removal of the activation peptide. {ECO:0000250}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Cleavage of the triple helix of collagen at about three-quarters of the length of the molecule from the N-terminus, at 775-Gly-|-Ile-776 in the alpha-1(I) chain. Cleaves synthetic substrates and alpha-macroglobulins at bonds where P1' is a hydrophobic residue.; EC=3.4.24.7; |
| DNA Binding | |
| EC Number | 3.4.24.7 |
| Enzyme Function | FUNCTION: Cleaves collagens of types I, II, and III at one site in the helical domain. Also cleaves collagens of types VII and X (By similarity). Able to degrade synthetic peptides and type I and II fibrillar collagen. {ECO:0000250}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Disulfide bond (1); Glycosylation (2); Metal binding (19); Motif (1); Propeptide (1); Region (1); Repeat (4); Signal peptide (1) |
| Keywords | Autocatalytic cleavage;Calcium;Collagen degradation;Disulfide bond;Extracellular matrix;Glycoprotein;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:0000305}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..17; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 12815621; 17307908; 18267097; 19853894; 19913533; 21267068; 22171010; 22987638; 23085232; 23421805; 23548910; 23565059; 23708660; 23934123; 24737602; 25352026; 25664857; 33761760; |
| Motif | MOTIF 87..94; /note=Cysteine switch; /evidence=ECO:0000250 |
| Gene Encoded By | |
| Mass | 53,488 |
| Kinetics | |
| Metal Binding | METAL 89; /note=Zinc 2; in inhibited form; /evidence=ECO:0000250; METAL 155; /note=Calcium 2; /evidence=ECO:0000250; METAL 165; /note=Zinc 1; /evidence=ECO:0000250; METAL 167; /note=Zinc 1; /evidence=ECO:0000250; METAL 172; /note=Calcium 3; /evidence=ECO:0000250; METAL 173; /note=Calcium 3; via carbonyl oxygen; /evidence=ECO:0000250; METAL 180; /note=Zinc 1; /evidence=ECO:0000250; METAL 187; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250; METAL 189; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250; METAL 191; /note=Calcium 2; /evidence=ECO:0000250; METAL 193; /note=Zinc 1; /evidence=ECO:0000250; METAL 195; /note=Calcium 3; /evidence=ECO:0000250; METAL 198; /note=Calcium 3; /evidence=ECO:0000250; METAL 215; /note=Zinc 2; catalytic; /evidence=ECO:0000250; METAL 219; /note=Zinc 2; catalytic; /evidence=ECO:0000250; METAL 225; /note=Zinc 2; catalytic; /evidence=ECO:0000250; METAL 283; /note=Calcium 4; via carbonyl oxygen; /evidence=ECO:0000250; METAL 376; /note=Calcium 4; via carbonyl oxygen; /evidence=ECO:0000250; METAL 425; /note=Calcium 4; via carbonyl oxygen; /evidence=ECO:0000250 |
| Rhea ID | |
| Cross Reference Brenda |