FAS1

Four repeated domains in the Fasciclin I family of proteins, present in many other contexts.
FAS1
SMART accession number:SM00554
Description: -
Interpro abstract (IPR000782):

The FAS1 (fasciclin-like) domain is an extracellular module of about 140 amino acid residues. It has been suggested that the FAS1 domain represents an ancient cell adhesion domain common to plants and animals [(PUBMED:7925267)]; related FAS1 domains are also found in bacteria [(PUBMED:7822037)].

The crystal structure of FAS1 domains 3 and 4 of fasciclin I from Drosophila melanogaster (Fruit fly) has been determined, revealing a novel domain fold consisting of a seven-stranded beta wedge and at least five alpha helices; two well-ordered N-acetylglucosamine groups attached to a conserved asparagine are located in the interface region between the two FAS1 domains [(PUBMED:12575939)]. Fasciclin I is an insect neural cell adhesion molecule involved in axonal guidance that is attached to the membrane by a GPI-anchored protein.

FAS1 domains are present in many secreted and membrane-anchored proteins. These proteins are usually GPI anchored and consist of: (i) a single FAS1 domain, (ii) a tandem array of FAS1 domains, or (iii) FAS1 domain(s) interspersed with other domains.

Proteins known to contain a FAS1 domain include:

  • Fasciclin I (4 FAS1 domains).
  • Human TGF-beta induced Ig-H3 (BIgH3) protein (4 FAS1 domains), where the FAS1 domains mediate cell adhesion through an interaction with alpha3/beta1 integrin; mutation in the FAS1 domains result in corneal dystrophy [(PUBMED:10906123)].
  • Volvox major cell adhesion protein (2 FAS1 domains) [(PUBMED:7925267)].
  • Arabidopsis fasciclin-like arabinogalactan proteins (2 FAS1 domains) [(PUBMED:16944204)].
  • Mammalian stabilin protein, a family of fasciclin-like hyaluronan receptor homologues (7 FAS1 domains)[(PUBMED:15345724)].
  • Human extracellular matrix protein periostin (4 FAS1 domains).
  • Bacterial immunogenic protein MPT70 (1 FAS1 domain) [(PUBMED:7871388)].

The FAS1 domains of both human periostin (Q15063) and BIgH3 (Q15582) proteins were found to contain vitamin K-dependent gamma-carboxyglutamate residues [(PUBMED:18450759)]. Gamma-carboxyglutamate residues are more commonly associated with GLA domains (IPR000294), where they occur through post-translational modification catalysed by the vitamin K-dependent enzyme gamma-glutamylcarboxylase.

Family alignment:
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There are 8587 FAS1 domains in 4696 proteins in SMART's nrdb database.

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