| IED ID | IndEnz0002005052 |
| Enzyme Type ID | protease005052 |
| Protein Name |
Disintegrin and metalloproteinase domain-containing protein 15 ADAM 15 EC 3.4.24.- CRII-7 Metalloprotease RGD disintegrin protein Metalloproteinase-like, disintegrin-like, and cysteine-rich protein 15 MDC-15 Metargidin |
| Gene Name | Adam15 Mdc15 |
| 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 | MRLALLWALGLLGAGSPRPSPPLPNIGGTEEEQQASPERTQSRSLENQVVQDSPPINLTEVLQTGLPETLRIGLELDGENHILELQQNRDLVPGRPTLVWYQPDGTRMVSEGHSLENCCYRGRVQGRPSSWVSLCACSGIRGLVVLSPERSYTLELGPGDLQRPLIVSRIQDLLLPGHTCAPSWHAFVPTEAAPDLLLEQHHLRRLKRDVVTETKIVELVIVADNSEVRKYPDFQQLLNRTLEVALLLDTFFQPLNVRVALVGLEAWTQRDLIEMSSNPAVLLDNFLRWRRTDLLPRLPHDSAQLVTVTSFSGPMVGMAIQNSICSPDFSGGVNMDHSTSILGVASSIAHELGHSLGLDHDSPGNSCPCPGPAPAKSCIMEASTDFLPGLNFSNCSRWALEKALLDGMGSCLFEWPPSRAPMSSLCGNMFVDPGEQCDCGFPDECTDPCCDYFTCQLRPGAQCASDGPCCQNCKLQPAGWQCRLPTDDCDLPEFCLGDSSQCPPDIRLGDGEPCASGEAVCMHGRCASYTRQCQSLWGPGAQPAAPLCLQTANTRGNAFGSCGRSPSGSYMPCNLRDAICGQLQCQWGRNQPLLGSVQDQLSEVLEANGTQLNCSWVDLDLGNDVAQPLLALPGTACGPGLVCIGHRCQPVDLLGAQECRSKCHGHGVCDSSRHCHCDEGWAPPDCMTQLRATSSLTTGLLLSLLLLLVLVLLGASYWYRARLHQRLCQLKGSSCQYRAAQSGPPERPGPPQRAQQMPGTKQANVSFPVPPSRPLPPNPVPKKLQAELADRSNPPTRPLPADPVVWRPKPQGPTKPPPPRKPLPANPQGRPPLGDLPGPGDGSLQLVVPSRPAPPPPAASSLYL |
| Enzyme Length | 864 |
| Uniprot Accession Number | Q9QYV0 |
| Absorption | |
| Active Site | ACT_SITE 351; /evidence="ECO:0000255|PROSITE-ProRule:PRU00276, ECO:0000255|PROSITE-ProRule:PRU10095" |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.24.- |
| Enzyme Function | FUNCTION: Active metalloproteinase with gelatinolytic and collagenolytic activity. Plays a role in the wound healing process. Mediates both heterotypic intraepithelial cell/T-cell interactions and homotypic T-cell aggregation. Inhibits beta-1 integrin-mediated cell adhesion and migration of airway smooth muscle cells. Suppresses cell motility on or towards fibronectin possibly by driving alpha-v/beta-1 integrin (ITAGV-ITGB1) cell surface expression via ERK1/2 inactivation. Cleaves E-cadherin in response to growth factor deprivation. Plays a role in glomerular cell migration. Plays a role in pathological neovascularization. May play a role in cartilage remodeling. May be proteolytically processed, during sperm epididymal maturation and the acrosome reaction. May play a role in sperm-egg binding through its disintegrin domain (By similarity). {ECO:0000250}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Alternative sequence (1); Chain (1); Compositional bias (3); Disulfide bond (7); Domain (3); Glycosylation (6); Metal binding (4); Modified residue (2); Motif (3); Propeptide (1); Region (2); Sequence conflict (1); Signal peptide (1); Topological domain (2); Transmembrane (1) |
| Keywords | Alternative splicing;Angiogenesis;Cell adhesion;Cell junction;Cell projection;Cilium;Cleavage on pair of basic residues;Collagen degradation;Cytoplasmic vesicle;Disulfide bond;EGF-like domain;Flagellum;Glycoprotein;Hydrolase;Membrane;Metal-binding;Metalloprotease;Phosphoprotein;Protease;Reference proteome;SH3-binding;Signal;Transmembrane;Transmembrane helix;Zinc;Zymogen |
| Interact With | |
| Induction | INDUCTION: In response to sciatic nerve injury. |
| Subcellular Location | SUBCELLULAR LOCATION: Endomembrane system {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Cell junction, adherens junction {ECO:0000250}. Cell projection, cilium, flagellum {ECO:0000250}. Cytoplasmic vesicle, secretory vesicle, acrosome {ECO:0000250}. Note=The majority of the protein is localized in a perinuclear compartment which may correspond to the trans-Golgi network or the late endosome. The pro-protein is the major detectable form on the cell surface, whereas the majority of the protein in the cell is processed (By similarity). {ECO:0000250}. |
| Modified Residue | MOD_RES 717; /note=Phosphotyrosine; by HCK and LCK; /evidence=ECO:0000250|UniProtKB:Q13444; MOD_RES 737; /note=Phosphotyrosine; by HCK and LCK; /evidence=ECO:0000250|UniProtKB:Q13444 |
| Post Translational Modification | PTM: The precursor is cleaved by a furin endopeptidase. {ECO:0000250}.; PTM: Phosphorylation increases association with PTKs. {ECO:0000250}. |
| Signal Peptide | SIGNAL 1..17; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 12815633; 22230263; |
| Motif | MOTIF 178..185; /note=Cysteine switch; /evidence=ECO:0000250; MOTIF 816..822; /note=SH3-binding; /evidence=ECO:0000255; MOTIF 851..857; /note=SH3-binding; /evidence=ECO:0000255 |
| Gene Encoded By | |
| Mass | 93,308 |
| Kinetics | |
| Metal Binding | METAL 180; /note=Zinc; in inhibited form; /evidence=ECO:0000250; METAL 350; /note=Zinc; catalytic; /evidence=ECO:0000255; METAL 354; /note=Zinc; catalytic; /evidence=ECO:0000255; METAL 360; /note=Zinc; catalytic; /evidence=ECO:0000255 |
| Rhea ID | |
| Cross Reference Brenda |