| Protein Name | Disintegrin and Metalloproteinase Domain 9 |
|---|---|
| Gene | [ADAM9](/genes/adam9) |
| UniProt ID | Q13443 |
| Protein Size | 819 amino acids (~90 kDa) |
| Subcellular Localization | Cell surface; membrane-anchored; shed to soluble form |
| Protein Family | ADAM family (A Disintegrin And Metalloproteinase) |
| PDB Structures | 1JXK, 2EAO |
ADAM9 (A Disintegrin and Metalloproteinase 9) is a member of the ADAM family of transmembrane metalloproteinases that plays important roles in cell adhesion, migration, and proteolytic processing of various substrates, including the amyloid precursor protein (APP).
ADAM9 has the characteristic multi-domain structure of ADAM proteins:
In normal cells, ADAM9 participates in:
Proteolytic Processing: Cleaves various membrane proteins, including growth factors, cytokines, and adhesion molecules.
Cell Adhesion: The disintegrin domain interacts with integrins to mediate cell-cell and cell-matrix interactions.
Cell Migration: Facilitates cell migration by processing adhesion molecules and growth factor precursors.
Fertility: Important for sperm-egg fusion and testicular function.
Wound Healing: Involved in tissue repair processes.
ADAM9 is one of the alpha-secretase candidates that can cleave APP within the amyloid-beta sequence, potentially preventing amyloid plaque formation[1]. However, ADAM9 also:
ADAM9 is overexpressed in various cancers and promotes:
ADAM9 plays roles in atherosclerosis, restenosis, and heart failure.
ADAM9 is a potential therapeutic target:
ADAM9 interacts with: