ID:ADA15_HUMAN DESCRIPTION: RecName: Full=Disintegrin and metalloproteinase domain-containing protein 15; Short=ADAM 15; EC=3.4.24.-; AltName: Full=Metalloprotease RGD disintegrin protein; AltName: Full=Metalloproteinase-like, disintegrin-like, and cysteine-rich protein 15; Short=MDC-15; AltName: Full=Metargidin; Flags: Precursor; 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. COFACTOR: Binds 1 zinc ion per subunit (By similarity). ENZYME 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. SUBUNIT: Interacts with ITAGV-ITGB3 (vitronectin receptor), PACSIN3 and SNX9. PACSIN3 and SNX9 preferentially bind the precursor but not the processed form of ADAM15, suggesting that the interaction occurs in a secretory pathway compartment prior to the medial Golgi (By similarity). Interacts with ITAG9-ITGB1 (By similarity). Interacts specifically with Src family protein- tyrosine kinases (PTKs). Interacts with SH3PXD2A. Interacts with ITAGV-ITGB1. Interacts with GRB2, HCK, ITSN1, ITSN2, LYN, MAPK1, MAPK3, NCF1, NCK1, nephrocystin, PTK6, SNX33, LCK and SRC. INTERACTION: Q9UKS6:PACSIN3; NbExp=2; IntAct=EBI-77818, EBI-77926; Q99962:SH3GL2; NbExp=2; IntAct=EBI-77818, EBI-77938; SUBCELLULAR LOCATION: Endomembrane system; Single-pass type I membrane protein. Cell junction, adherens junction. Cell projection, cilium, flagellum (By similarity). Cytoplasmic vesicle, secretory vesicle, acrosome (By similarity). 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). TISSUE SPECIFICITY: Expressed in colon and small intestine. Expressed in airway smooth muscle and glomerular mesangial cells (at protein level). Ubiquitously expressed. Overexpressed in atherosclerotic lesions. Constitutively expressed in cultured endothelium and smooth muscle. Expressed in chondrocytes. Expressed in airway smooth muscle and glomerular mesangial cells. DOMAIN: The cytoplasmic domain interacts with endophilin I and sorting nexin 9 (By similarity). DOMAIN: Disintegrin domain binds to integrin alphaV-beta3. DOMAIN: The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme. PTM: The precursor is cleaved by a furin endopeptidase (By similarity). PTM: Phosphorylation increases association with PTKs. SIMILARITY: Contains 1 disintegrin domain. SIMILARITY: Contains 1 EGF-like domain. SIMILARITY: Contains 1 peptidase M12B domain.
The RNAfold program from the Vienna RNA Package is used to perform the secondary structure predictions and folding calculations. The estimated folding energy is in kcal/mol. The more negative the energy, the more secondary structure the RNA is likely to have.
ModBase Predicted Comparative 3D Structure on Q13444
Front
Top
Side
The pictures above may be empty if there is no ModBase structure for the protein. The ModBase structure frequently covers just a fragment of the protein. You may be asked to log onto ModBase the first time you click on the pictures. It is simplest after logging in to just click on the picture again to get to the specific info on that model.
Orthologous Genes in Other Species
Orthologies between human, mouse, and rat are computed by taking the best BLASTP hit, and filtering out non-syntenic hits. For more distant species reciprocal-best BLASTP hits are used. Note that the absence of an ortholog in the table below may reflect incomplete annotations in the other species rather than a true absence of the orthologous gene.