ADAM10 Cleaves the membrane-bound precursor of TNF-alpha at '76-Ala-|-Val-77' to its mature soluble form. Responsible for the proteolytical release of soluble JAM3 from endothelial cells surface. Responsible for the proteolytic release of several other cell-surface proteins, including heparin-binding epidermal growth-like factor, ephrin-A2, CD44, CDH2 and for constitutive and regulated alpha-secretase cleavage of amyloid precursor protein (APP). Contributes to the normal cleavage of the cellular prion protein. Involved in the cleavage of the adhesion molecule L1 at the cell surface and in released membrane vesicles, suggesting a vesicle-based protease activity. Controls also the proteolytic processing of Notch and mediates lateral inhibition during neurogenesis. Responsible for the FasL ectodomain shedding and for the generation of the remnant ADAM10-processed FasL (FasL APL) transmembrane form. Also cleaves the ectodomain of the integral membrane proteins CORIN and ITM2B. Mediates the proteolytic cleavage of LAG3, leading to release the secreted form of LAG3. May regulate the EFNA5-EPHA3 signaling. Expressed in spleen, lymph node, thymus, peripheral blood leukocyte, bone marrow, cartilage, chondrocytes and fetal liver. 2 alternatively spliced human isoforms have been reported. Note: This description may include information from UniProtKB.
Protein type: Cell adhesion; Cell surface; EC 3.4.24.81; Membrane protein, integral; Motility/polarity/chemotaxis; Protease; Vesicle
Chromosomal Location of Human Ortholog: 9 D|9 39.53 cM
Cellular Component:  cell surface; cytoplasm; dendrite; dendritic spine; glutamatergic synapse; Golgi apparatus; Golgi-associated vesicle; integral component of membrane; membrane; neuronal cell body; nucleus; perinuclear endoplasmic reticulum; plasma membrane; postsynapse; postsynaptic density; postsynaptic membrane; synaptic vesicle; tetraspanin-enriched microdomain; trans-Golgi network
Molecular Function:  endopeptidase activity; hydrolase activity; metal ion binding; metalloendopeptidase activity; metallopeptidase activity; peptidase activity; protein binding; protein homodimerization activity; protein kinase binding; SH2 domain binding; SH3 domain binding
Biological Process:  amyloid-beta formation; constitutive protein ectodomain proteolysis; in utero embryonic development; membrane protein ectodomain proteolysis; monocyte activation; negative regulation of cell adhesion; Notch receptor processing; Notch signaling pathway; nucleocytoplasmic transport; PMA-inducible membrane protein ectodomain proteolysis; positive regulation of apoptotic process; positive regulation of cell growth; positive regulation of cell migration; positive regulation of cell proliferation; positive regulation of T cell chemotaxis; postsynapse organization; protein phosphorylation; protein processing; proteolysis; regulation of dendritic spine morphogenesis; regulation of neurotransmitter receptor localization to postsynaptic specialization membrane; response to tumor necrosis factor
Reference #:  O35598 (UniProtKB)
Alt. Names/Synonyms: 1700031C13Rik; a disintegrin and metallopeptidase domain 10; a disintegrin and metalloprotease domain (ADAM) 10; a disintegrin and metalloprotease domain 10; ADA10; ADAM 10; Adam10; CD156c; Disintegrin and metalloproteinase domain-containing protein 10; Kuz; kuzb; kuzbanian; Kuzbanian protein homolog; Madm; Mammalian disintegrin-metalloprotease
Gene Symbols: Adam10
Molecular weight: 83,968 Da
Basal Isoelectric point: 8.27  Predict pI for various phosphorylation states
CST Pathways:  Alzheimer's Disease  |  Notch Signaling
Select Structure to View Below

ADAM10

Protein Structure Not Found.


Cross-references to other databases:  STRING  |  Reactome  |  BioGPS  |  Pfam  |  ENZYME  |  Phospho.ELM  |  NetworKIN  |  UniProtKB  |  Entrez-Gene  |  Ensembl Gene