| IED ID | IndEnz0002019057 |
| Enzyme Type ID | protease019057 |
| Protein Name |
Disintegrin and metalloproteinase domain-containing protein 15 ADAM 15 EC 3.4.24.- AD56 Metalloprotease RGD disintegrin protein Metalloproteinase-like, disintegrin-like, and cysteine-rich protein 15 MDC-15 Metargidin |
| Gene Name | Adam15 Mdc15 |
| 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 | MRLALLWALGLLGAGSPRPSPPLPNIGGTEEEQQASPERTLSGSMESRVVQDSPPMSLADVLQTGLPEALRISLELDSESHVLELLQNRDLIPGRPTLVWYQPDGTRMVSEGYSLENCCYRGRVQGHPSSWVSLCACSGIRGLIVLSPERGYTLELGPGDLQRPVISRIQDHLLLGHTCAPSWHASVPTRAGPDLLLEQHHAHRLKRDVVTETKIVELVIVADNSEVRKYPDFQQLLNRTLEAALLLDTFFQPLNVRVALVGLEAWTQHNLIEMSSNPAVLLDNFLRWRRTDLLPRLPHDSAQLVTVTSFSGPMVGMAIQNSICSPDFSGGVNMDHSTSILGVASSIAHELGHSLGLDHDSPGHSCPCPGPAPAKSCIMEASTDFLPGLNFSNCSRQALEKALLEGMGSCLFERQPSLAPMSSLCGNMFVDPGEQCDCGFPDECTDPCCDHFTCQLRPGAQCASDGPCCQNCKLHPAGWLCRPPTDDCDLPEFCPGDSSQCPSDIRLGDGEPCASGEAVCMHGRCASYARQCQSLWGPGAQPAAPLCLQTANTRGNAFGSCGRSPGGSYMPCAPRDVMCGQLQCQWGRSQPLLGSVQDRLSEVLEANGTQLNCSWVDLDLGNDVAQPLLALPGTACGPGLVCIGHRCQPVDLLGAQECRRKCHGHGVCDSSGHCRCEEGWAPPDCMTQLKATSSLTTGLLLSLLLLLVLVLLGASYWHRARLHQRLCQLKGSSCQYRAPQSCPPERPGPPQRAQQMTGTKQASVVSFPVPPSRPLPPNPVPKKLQAALADRSNPPTRPLPADPVVRRPKSQGPTKPPPPRKPLPANPQGQHPPGDLPGPGDGSLPLVVPSRPAPPPPAASSLYL |
| Enzyme Length | 864 |
| Uniprot Accession Number | O88839 |
| Absorption | |
| Active Site | ACT_SITE 350; /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 (By similarity). 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. Interactions with egg membrane could be mediated via binding between the disintegrin-like domain to one or more integrin receptors on the egg. {ECO:0000250, ECO:0000269|PubMed:11882657, ECO:0000269|PubMed:12897135, ECO:0000269|PubMed:15818704, ECO:0000269|PubMed:18390692}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Alternative sequence (3); Chain (1); Compositional bias (4); Disulfide bond (7); Domain (3); Glycosylation (5); Metal binding (4); Modified residue (2); Motif (3); Mutagenesis (6); Propeptide (1); Region (2); Sequence conflict (15); Signal peptide (1); Site (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: By hypoxic stimulus in retina (at protein level). Up-regulated by VEGF in retina. {ECO:0000269|PubMed:12897135, ECO:0000269|PubMed:18381816}. |
| Subcellular Location | SUBCELLULAR LOCATION: Endomembrane system {ECO:0000269|PubMed:18390692}; Single-pass type I membrane protein {ECO:0000269|PubMed:18390692}. Cell junction, adherens junction {ECO:0000250}. Cell projection, cilium, flagellum {ECO:0000269|PubMed:18390692}. Cytoplasmic vesicle, secretory vesicle, acrosome {ECO:0000269|PubMed:18390692}. 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. |
| Modified Residue | MOD_RES 716; /note=Phosphotyrosine; by HCK and LCK; /evidence=ECO:0000250|UniProtKB:Q13444; MOD_RES 736; /note=Phosphotyrosine; by HCK and LCK; /evidence=ECO:0000250|UniProtKB:Q13444 |
| Post Translational Modification | PTM: The precursor is cleaved by a furin endopeptidase. An additional membrane proximal site of cleavage affects a small percentage of the proteins and results in disulfide-linked fragments. The prodomain is apparently cleaved in several positions that are N-terminal of the furin cleavage site. {ECO:0000269|PubMed:9748307}.; PTM: May be partially sialylated.; PTM: Phosphorylation increases association with PTKs. {ECO:0000250}. |
| Signal Peptide | SIGNAL 1..17; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | MOTIF 177..184; /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 | 92,664 |
| Kinetics | |
| Metal Binding | METAL 179; /note=Zinc; in inhibited form; /evidence=ECO:0000250; METAL 349; /note=Zinc; catalytic; /evidence=ECO:0000255; METAL 353; /note=Zinc; catalytic; /evidence=ECO:0000255; METAL 359; /note=Zinc; catalytic; /evidence=ECO:0000255 |
| Rhea ID | |
| Cross Reference Brenda |