| IED ID | IndEnz0002005053 |
| Enzyme Type ID | protease005053 |
| Protein Name |
Disintegrin and metalloproteinase domain-containing protein 15 ADAM 15 EC 3.4.24.- Metalloprotease RGD disintegrin protein Metalloproteinase-like, disintegrin-like, and cysteine-rich protein 15 MDC-15 Metargidin |
| Gene Name | ADAM15 MDC15 |
| 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 | MRLALLWALGLLGAGSPLPSWPLPNIGGTEEQQAESEKAPREPLEPQVLQDDLPISLKKVLQTSLPEPLRIKLELDGDSHILELLQNRELVPGRPTLVWYQPDGTRVVSEGHTLENCCYQGRVRGYAGSWVSICTCSGLRGLVVLTPERSYTLEQGPGDLQGPPIISRIQDLHLPGHTCALSWRESVHTQKPPEHPLGQRHIRRRRDVVTETKTVELVIVADHSEAQKYRDFQHLLNRTLEVALLLDTFFRPLNVRVALVGLEAWTQRDLVEISPNPAVTLENFLHWRRAHLLPRLPHDSAQLVTGTSFSGPTVGMAIQNSICSPDFSGGVNMDHSTSILGVASSIAHELGHSLGLDHDLPGNSCPCPGPAPAKTCIMEASTDFLPGLNFSNCSRRALEKALLDGMGSCLFERLPSLPPMAAFCGNMFVEPGEQCDCGFLDDCVDPCCDSLTCQLRPGAQCASDGPCCQNCQLRPSGWQCRPTRGDCDLPEFCPGDSSQCPPDVSLGDGEPCAGGQAVCMHGRCASYAQQCQSLWGPGAQPAAPLCLQTANTRGNAFGSCGRNPSGSYVSCTPRDAICGQLQCQTGRTQPLLGSIRDLLWETIDVNGTELNCSWVHLDLGSDVAQPLLTLPGTACGPGLVCIDHRCQRVDLLGAQECRSKCHGHGVCDSNRHCYCEEGWAPPDCTTQLKATSSLTTGLLLSLLVLLVLVMLGASYWYRARLHQRLCQLKGPTCQYRAAQSGPSERPGPPQRALLARGTKQASALSFPAPPSRPLPPDPVSKRLQAELADRPNPPTRPLPADPVVRSPKSQGPAKPPPPRKPLPADPQGRCPSGDLPGPGAGIPPLVVPSRPAPPPPTVSSLYL |
| Enzyme Length | 863 |
| Uniprot Accession Number | Q13444 |
| Absorption | |
| Active Site | ACT_SITE 349; /evidence="ECO:0000255|PROSITE-ProRule:PRU00276, ECO:0000255|PROSITE-ProRule:PRU10095" |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by hydroxamate-type metalloproteinase inhibitors such as marimastat. Inhibited by metalloproteinase inhibitor 2 (TIMP-2) and TIMP-3 at nanomolar concentrations. Not significantly inhibited by TIMP-1 at concentrations of up to 100 nM. Not activated by PMA or ionomycin. {ECO:0000269|PubMed:19207106}. |
| 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. {ECO:0000269|PubMed:12091380, ECO:0000269|PubMed:15358598, ECO:0000269|PubMed:15818704, ECO:0000269|PubMed:17416588, ECO:0000269|PubMed:17575078, ECO:0000269|PubMed:18387333, ECO:0000269|PubMed:18434311}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Alternative sequence (14); Chain (1); Compositional bias (2); Disulfide bond (7); Domain (3); Glycosylation (5); Metal binding (4); Modified residue (2); Motif (4); Mutagenesis (1); Natural variant (3); Propeptide (1); Region (2); Sequence conflict (7); 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 | Q8N9N5; Q06187; Q13643; P06241; P62993; P08631; P06239; P07948; O15259; P37198; Q92882; Q9UKS6; Q93062; Q99962; Q5TCZ1; Q8WV41; Q9Y5X1; Q02446; P12931; P54253; A1E959; Q8WV41 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Endomembrane system {ECO:0000269|PubMed:12243749}; Single-pass type I membrane protein {ECO:0000269|PubMed:12243749}. Cell junction, adherens junction {ECO:0000269|PubMed:12243749}. 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 715; /note=Phosphotyrosine; by HCK and LCK; /evidence=ECO:0000269|PubMed:11741929; MOD_RES 735; /note=Phosphotyrosine; by HCK and LCK; /evidence=ECO:0000269|PubMed:11741929 |
| Post Translational Modification | PTM: The precursor is cleaved by a furin endopeptidase. {ECO:0000250}.; PTM: Phosphorylation increases association with PTKs. {ECO:0000269|PubMed:11741929}. |
| Signal Peptide | SIGNAL 1..17; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 11839628; 11840679; 11882657; 12777399; 12897135; 14707550; 15263807; 15384173; 15618016; 15756594; 15958533; 16189514; 16374509; 16756724; 16894352; 17080222; 18281484; 18695922; 18774960; 19253070; 19487280; 19550037; 20189953; 20213810; 20711500; 20851104; 21190186; 21196774; 21728902; 22505472; 22544741; 22621184; 23365087; 23688428; 23910172; 23918525; 25208722; 25333931; 25416956; 25650586; 26323669; 26930657; 27554339; 28282546; 30634456; 30685994; 31271758; 31467400; 32522006; 32677970; 33208450; 34685689; |
| Motif | MOTIF 177..184; /note=Cysteine switch; /evidence=ECO:0000250; MOTIF 484..486; /note=Cell attachment site; /evidence=ECO:0000255|PROSITE-ProRule:PRU00068; MOTIF 815..821; /note=SH3-binding; /evidence=ECO:0000255; MOTIF 850..856; /note=SH3-binding; /evidence=ECO:0000255 |
| Gene Encoded By | |
| Mass | 92,959 |
| Kinetics | |
| Metal Binding | METAL 179; /note=Zinc; in inhibited form; /evidence=ECO:0000250; METAL 348; /note=Zinc; catalytic; /evidence=ECO:0000250; METAL 352; /note=Zinc; catalytic; /evidence=ECO:0000250; METAL 358; /note=Zinc; catalytic; /evidence=ECO:0000250 |
| Rhea ID | |
| Cross Reference Brenda | 3.4.24.B28; |