| IED ID | IndEnz0002006535 |
| Enzyme Type ID | protease006535 |
| Protein Name |
Matrix metalloproteinase-27 MMP-27 EC 3.4.24.- |
| Gene Name | MMP27 UNQ2503/PRO5992 |
| Organism | Homo sapiens (Human) |
| 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 Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human) |
| Enzyme Sequence | MKRLLLLFLFFITFSSAFPLVRMTENEENMQLAQAYLNQFYSLEIEGNHLVQSKNRSLIDDKIREMQAFFGLTVTGKLDSNTLEIMKTPRCGVPDVGQYGYTLPGWRKYNLTYRIINYTPDMARAAVDEAIQEGLEVWSKVTPLKFTKISKGIADIMIAFRTRVHGRCPRYFDGPLGVLGHAFPPGPGLGGDTHFDEDENWTKDGAGFNLFLVAAHEFGHALGLSHSNDQTALMFPNYVSLDPRKYPLSQDDINGIQSIYGGLPKEPAKPKEPTIPHACDPDLTFDAITTFRREVMFFKGRHLWRIYYDITDVEFELIASFWPSLPADLQAAYENPRDKILVFKDENFWMIRGYAVLPDYPKSIHTLGFPGRVKKIDAAVCDKTTRKTYFFVGIWCWRFDEMTQTMDKGFPQRVVKHFPGISIRVDAAFQYKGFFFFSRGSKQFEYDIKTKNITRIMRTNTWFQCKEPKNSSFGFDINKEKAHSGGIKILYHKSLSLFIFGIVHLLKNTSIYQ |
| Enzyme Length | 513 |
| Uniprot Accession Number | Q9H306 |
| Absorption | |
| Active Site | ACT_SITE 217; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.24.- |
| Enzyme Function | FUNCTION: Matrix metalloproteinases degrade protein components of the extracellular matrix such as fibronectin, laminin, gelatins and/or collagens. {ECO:0000250}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Disulfide bond (1); Glycosylation (3); Metal binding (20); Motif (1); Mutagenesis (3); Natural variant (7); Propeptide (1); Region (1); Repeat (4); Signal peptide (1) |
| Keywords | Calcium;Collagen degradation;Disulfide bond;Endoplasmic reticulum;Glycoprotein;Hydrolase;Membrane;Metal-binding;Metalloprotease;Protease;Reference proteome;Repeat;Signal;Zinc;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral membrane protein {ECO:0000269|PubMed:24548619}. Note=Retained in the endoplasmic reticulum. {ECO:0000269|PubMed:24548619}. |
| Modified Residue | |
| Post Translational Modification | PTM: N-glycosylated. {ECO:0000269|PubMed:24548619}. |
| Signal Peptide | SIGNAL 1..17; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 19913121; 20484597; 20628086; 31067818; |
| Motif | MOTIF 89..96; /note=Cysteine switch; /evidence=ECO:0000250 |
| Gene Encoded By | |
| Mass | 59,026 |
| Kinetics | |
| Metal Binding | METAL 91; /note=Zinc 2; in inhibited form; /evidence=ECO:0000250; METAL 121; /note=Calcium 1; /evidence=ECO:0000250; METAL 155; /note=Calcium 2; /evidence=ECO:0000250; METAL 165; /note=Zinc 1; /evidence=ECO:0000250; METAL 173; /note=Calcium 3; /evidence=ECO:0000250; METAL 174; /note=Calcium 3; via carbonyl oxygen; /evidence=ECO:0000250; METAL 178; /note=Calcium 3; via carbonyl oxygen; /evidence=ECO:0000250; METAL 181; /note=Zinc 1; /evidence=ECO:0000250; METAL 188; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250; METAL 192; /note=Calcium 2; /evidence=ECO:0000250; METAL 194; /note=Zinc 1; /evidence=ECO:0000250; METAL 196; /note=Calcium 3; /evidence=ECO:0000250; METAL 199; /note=Calcium 1; /evidence=ECO:0000250; METAL 199; /note=Calcium 3; /evidence=ECO:0000250; METAL 216; /note=Zinc 2; catalytic; /evidence=ECO:0000250; METAL 220; /note=Zinc 2; catalytic; /evidence=ECO:0000250; METAL 226; /note=Zinc 2; catalytic; /evidence=ECO:0000250; METAL 286; /note=Calcium 4; via carbonyl oxygen; /evidence=ECO:0000250; METAL 377; /note=Calcium 4; via carbonyl oxygen; /evidence=ECO:0000250; METAL 426; /note=Calcium 4; via carbonyl oxygen; /evidence=ECO:0000250 |
| Rhea ID | |
| Cross Reference Brenda |