Fibrillin 1 is an extracellular acidic protein with a high cysteine content and an extended thread-like shape with mosaic composition of different types of extracellular modules. Most of the fibrillin molecule is contributed by 47 epidermal growth factor-like (EGF-like) repeats; 43 of them have a consensus sequence for calcium binding (cb). Other modules including 8-cysteine motifs (seven), hybrid motifs (two), and unique domains (three) are interspersed throughout the molecule[3-7]. Fibrillin 1 contains a proline-rich region close to the N-terminus that is replaced by a glycine-rich region in Fibrillin 2. The fibrillins are found throughout the connective tissue as integral components of extended fibrils.
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Protein Aliases: Asprosin; fibrillin 15; Fibrillin-1; tight skin
Gene Aliases: ACMICD; AI536462; B430209H23; ECTOL1; FBN; Fbn-1; FBN1; Fib-1; GPHYSD2; MASS; MFLS; MFS1; OCTD; SGS; SSKS; Tsk; WMS; WMS2
Molecular Function: annexin calcium-binding protein calmodulin cell adhesion molecule extracellular matrix glycoprotein extracellular matrix protein extracellular matrix structural protein intracellular calcium-sensing protein signaling molecule