| IED ID | IndEnz0002006101 |
| Enzyme Type ID | protease006101 |
| Protein Name |
Interstitial collagenase EC 3.4.24.7 Matrix metalloproteinase-1 MMP-1 Cleaved into: 18 kDa interstitial collagenase |
| Gene Name | MMP1 |
| Organism | Sus scrofa (Pig) |
| 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 Laurasiatheria Artiodactyla Suina Suidae (pigs) Sus Sus scrofa (Pig) |
| Enzyme Sequence | MFSLLLLLLLLCNTGSHGFPAATSETQEQDVEIVQKYLKNYYNLNSDGVPVEKKRNSGLVVEKLKQMQQFFGLKVTGKPDAETLNVMKQPRCGVPDVAEFVLTPGNPRWENTHLTYRIENYTPDLSREDVDRAIEKAFQLWSNVSPLTFTKVSEGQADIMISFVRGDHRDNSPFDGPGGNLAHAFQPGPGIGGDAHFDEDERWTKNFRDYNLYRVAAHELGHSLGLSHSTDIGALMYPNYIYTGDVQLSQDDIDGIQAIYGPSENPVQPSGPQTPQVCDSKLTFDAITTLRGELMFFKDRFYMRTNSFYPEVELNFISVFWPQVPNGLQAAYEIADRDEVRFFKGNKYWAVRGQDVLYGYPKDIHRSFGFPSTVKNIDAAVFEEDTGKTYFFVAHECWRYDEYKQSMDTGYPKMIAEEFPGIGNKVDAVFQKDGFLYFFHGTRQYQFDFKTKRILTLQKANSWFNCRKN |
| Enzyme Length | 469 |
| Uniprot Accession Number | P21692 |
| Absorption | |
| Active Site | ACT_SITE 219; /evidence="ECO:0000255|PROSITE-ProRule:PRU10095, ECO:0000269|PubMed:8590015" |
| Activity Regulation | ACTIVITY REGULATION: Can be activated without removal of the activation peptide. |
| 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); Beta strand (24); Chain (2); Disulfide bond (1); Glycosylation (1); Helix (7); Metal binding (24); Modified residue (3); Motif (1); Propeptide (1); Repeat (4); Signal peptide (1); Site (1); Turn (5) |
| Keywords | 3D-structure;Autocatalytic cleavage;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:0000250}. |
| Modified Residue | MOD_RES 57; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P03956; MOD_RES 274; /note=Phosphothreonine; /evidence=ECO:0000250|UniProtKB:P03956; MOD_RES 360; /note=Phosphotyrosine; by PKDCC; /evidence=ECO:0000250|UniProtKB:P03956 |
| Post Translational Modification | PTM: Undergoes autolytic cleavage to produce a N-terminal fragment having reduced collagenolytic activity.; PTM: Tyrosine phosphorylated in platelets by PKDCC/VLK. {ECO:0000250|UniProtKB:P03956}. |
| Signal Peptide | SIGNAL 1..19 |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 1FBL; |
| Mapped Pubmed ID | - |
| Motif | MOTIF 90..97; /note=Cysteine switch; /evidence=ECO:0000250 |
| Gene Encoded By | |
| Mass | 53,666 |
| Kinetics | |
| Metal Binding | METAL 92; /note=Zinc 2; in inhibited form; /evidence=ECO:0000250; METAL 124; /note=Calcium 1; METAL 158; /note=Calcium 2; METAL 168; /note=Zinc 1; METAL 170; /note=Zinc 1; METAL 175; /note=Calcium 3; METAL 176; /note=Calcium 3; via carbonyl oxygen; METAL 178; /note=Calcium 3; via carbonyl oxygen; METAL 180; /note=Calcium 3; via carbonyl oxygen; METAL 183; /note=Zinc 1; METAL 190; /note=Calcium 2; via carbonyl oxygen; METAL 192; /note=Calcium 2; via carbonyl oxygen; METAL 194; /note=Calcium 2; METAL 196; /note=Zinc 1; METAL 198; /note=Calcium 3; METAL 199; /note=Calcium 1; METAL 201; /note=Calcium 3; METAL 218; /note=Zinc 2; catalytic; METAL 222; /note=Zinc 2; catalytic; METAL 228; /note=Zinc 2; catalytic; METAL 285; /note=Calcium 4; via carbonyl oxygen; METAL 329; /note=Calcium 4; via carbonyl oxygen; METAL 378; /note=Calcium 4; via carbonyl oxygen; METAL 427; /note=Calcium 4; via carbonyl oxygen |
| Rhea ID | |
| Cross Reference Brenda |