| Primary Identifier | IPR036378 | Type | Homologous_superfamily |
| Short Name | FAS1_dom_sf |
| description | 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 []; related FAS1 domains are also found in bacteria [].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 []. 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 [].Volvox major cell adhesion protein (2 FAS1 domains) [].Arabidopsis fasciclin-like arabinogalactan proteins (2 FAS1 domains) [].Mammalian stabilin protein, a family of fasciclin-like hyaluronan receptor homologues (7 FAS1 domains)[].Human extracellular matrix protein periostin (4 FAS1 domains).Bacterial immunogenic protein MPT70 (1 FAS1 domain) [].The FAS1 domains of both human periostin () and BIgH3 () proteins were found to contain vitamin K-dependent gamma-carboxyglutamate residues []. Gamma-carboxyglutamate residues are more commonly associated with GLA domains (), where they occur through post-translational modification catalysed by the vitamin K-dependent enzyme gamma-glutamylcarboxylase. |
