Aliases for ADAM10 Gene
- ADAM Metallopeptidase Domain 10 2 3 5
- Disintegrin And Metalloproteinase Domain-Containing Protein 10 3 4
- Mammalian Disintegrin-Metalloprotease 3 4
- Kuzbanian Protein Homolog 3 4
- EC 126.96.36.199 4 54
- CDw156 3 4
- MADM 3 4
- A Disintegrin And Metalloproteinase Domain 10 2
- A Disintegrin And Metalloprotease Domain 10 3
External Ids for ADAM10 Gene
Previous GeneCards Identifiers for ADAM10 Gene
Members of the ADAM family are cell surface proteins with a unique structure possessing both potential adhesion and protease domains. This gene encodes and ADAM family member that cleaves many proteins including TNF-alpha and E-cadherin. Alternate splicing results in multiple transcript variants encoding different proteins that may undergo similar processing. [provided by RefSeq, Feb 2016]
GeneCards Summary for ADAM10 Gene
ADAM10 (ADAM Metallopeptidase Domain 10) is a Protein Coding gene. Diseases associated with ADAM10 include Reticulate Acropigmentation Of Kitamura and Alzheimer Disease 18. Among its related pathways are NOTCH2 Activation and Transmission of Signal to the Nucleus and Hypertrophy Model. Gene Ontology (GO) annotations related to this gene include protein homodimerization activity and signaling receptor binding. An important paralog of this gene is ADAM17.
UniProtKB/Swiss-Prot Summary for ADAM10 Gene
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 (PubMed:20592283). 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) (PubMed:26686862, PubMed:11786905, PubMed:29224781). Contributes to the normal cleavage of the cellular prion protein (PubMed:11477090). Involved in the cleavage of the adhesion molecule L1 at the cell surface and in released membrane vesicles, suggesting a vesicle-based protease activity (PubMed:12475894). Controls also the proteolytic processing of Notch and mediates lateral inhibition during neurogenesis (By similarity). Responsible for the FasL ectodomain shedding and for the generation of the remnant ADAM10-processed FasL (FasL APL) transmembrane form (PubMed:17557115). Also cleaves the ectodomain of the integral membrane proteins CORIN and ITM2B (PubMed:19114711, PubMed:21288900). Mediates the proteolytic cleavage of LAG3, leading to release the secreted form of LAG3 (By similarity). Enhances the cleavage of CHL1 by BACE1 (By similarity). Cleaves NRCAM (By similarity). Cleaves TREM2, resulting in shedding of the TREM2 ectodomain (PubMed:24990881). Involved in the development and maturation of glomerular and coronary vasculature (By similarity). During development of the cochlear organ of Corti, promotes pillar cell separation by forming a ternary complex with CADH1 and EPHA4 and cleaving CADH1 at adherens junctions (By similarity). May regulate the EFNA5-EPHA3 signaling (PubMed:16239146).
(Microbial infection) Promotes the cytotoxic activity of S.aureus hly by binding to the toxin at zonula adherens and promoting formation of toxin pores.