Fibromodulin (FMOD; also FM and collagen-binding 59kD protein) is a secreted, 60-70kD class II member of the SLRP family of matrix proteins. It is expressed by a variety of cell types, including keratinocytes, fibroblasts and chrondrocytes, and is known to bind to type I and XII collagen, plus TGF-B. Fibromodulin is posited to displace lumican binding to collagen, generating 3D collagen fibrils from simple lumican-induced collagen dimers. Mature human Fibromodulin is 358aa in length (aa19-376). It contains 12 LRRs (Leu-rich repeats) (aa98-376), with the seventh and eleventh LRR principally responsible for collagen type I binding. Fibromodulin contains varying amounts of keratan sulfate, and undergoes significant tyrosine sulfation. There is one splice form that shows a deletion of aa88-101. Over aa76-376, human Fibromodulin shares 96% aa identity with mouse and rat Fibromodulin.
Intended for research use only. Not for use in human, therapeutic, or diagnostic applications.