| IED ID | IndEnz0002006098 |
| Enzyme Type ID | protease006098 |
| Protein Name |
Interstitial collagenase EC 3.4.24.7 Matrix metalloproteinase-1 MMP-1 TC1 |
| Gene Name | |
| Organism | Lithobates catesbeianus (American bullfrog) (Rana catesbeiana) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amphibia Batrachia Anura Neobatrachia Ranoidea Ranidae (riparian frogs) Lithobates Lithobates catesbeianus (American bullfrog) (Rana catesbeiana) |
| Enzyme Sequence | MLSGLWSSILALLGVFLQSVGEFRAETQEQDVEIVQKYLKNYYNSDKRNSGLVVEILKQFFGLKVTGKPDAETLVMKQSTCGVPDVGEYVLTPGNPRWENTHLTYRIENYTPDLVSPLTFTKVSEGQADIMISFVRGDHRDKYPFDGPGGNLAHASQPGPGIGGDAHFDEYERWTKNFQDYNLYRVAAHELGHSLGLSHSTDIGALMYPTYLRGDVQLSQDDIDGPSGNPVQPRGPQTPQVCDSKLTFDAITTVRGELMFFKMRTNRFYPEVELGLQAAYEMADRDEVRFFKGNKYWAVSGQDVLYGYPKDIHSSFGFPTGVAHECWSYDEYKQSMDTGYADEFPGDAVFQKFFHGTRQYQFDLKTKRILTLQKANSWFNCRKN |
| Enzyme Length | 384 |
| Uniprot Accession Number | Q11133 |
| Absorption | |
| Active Site | ACT_SITE 190; /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. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Disulfide bond (1); Metal binding (23); Motif (1); Propeptide (1); Region (1); Repeat (2); Signal peptide (1) |
| Keywords | Calcium;Collagen degradation;Disulfide bond;Extracellular matrix;Hydrolase;Metal-binding;Metalloprotease;Protease;Repeat;Secreted;Signal;Zinc;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..25; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | MOTIF 79..86; /note=Cysteine switch; /evidence=ECO:0000250 |
| Gene Encoded By | |
| Mass | 43,582 |
| Kinetics | |
| Metal Binding | METAL 81; /note=Zinc 2; in inhibited form; /evidence=ECO:0000250; METAL 113; /note=Calcium 1; /evidence=ECO:0000250; METAL 129; /note=Calcium 2; /evidence=ECO:0000250; METAL 139; /note=Zinc 1; /evidence=ECO:0000250; METAL 141; /note=Zinc 1; /evidence=ECO:0000250; METAL 146; /note=Calcium 3; /evidence=ECO:0000250; METAL 147; /note=Calcium 3; via carbonyl oxygen; /evidence=ECO:0000250; METAL 149; /note=Calcium 3; via carbonyl oxygen; /evidence=ECO:0000250; METAL 151; /note=Calcium 3; via carbonyl oxygen; /evidence=ECO:0000250; METAL 154; /note=Zinc 1; /evidence=ECO:0000250; METAL 161; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250; METAL 163; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250; METAL 165; /note=Calcium 2; /evidence=ECO:0000250; METAL 167; /note=Zinc 1; /evidence=ECO:0000250; METAL 169; /note=Calcium 3; /evidence=ECO:0000250; METAL 170; /note=Calcium 1; /evidence=ECO:0000250; METAL 172; /note=Calcium 3; /evidence=ECO:0000250; METAL 189; /note=Zinc 2; catalytic; /evidence=ECO:0000250; METAL 193; /note=Zinc 2; catalytic; /evidence=ECO:0000250; METAL 199; /note=Zinc 2; catalytic; /evidence=ECO:0000250; METAL 249; /note=Calcium 4; via carbonyl oxygen; /evidence=ECO:0000250; METAL 277; /note=Calcium 4; via carbonyl oxygen; /evidence=ECO:0000250; METAL 347; /note=Calcium 4; via carbonyl oxygen; /evidence=ECO:0000250 |
| Rhea ID | |
| Cross Reference Brenda |