FAS1Four repeated domains in the Fasciclin I family of proteins, present in many other contexts.
|SMART accession number:||SM00554|
|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:
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.
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- Evolution (species in which this domain is found)
- Literature (relevant references for this domain)
- Disease (disease genes where sequence variants are found in this domain)
- Structure (3D structures containing this domain)
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