GBA3

The protein encoded by this gene is an enzyme that can hydrolyze several types of glycosides. This gene is a polymorphic pseudogene, with the most common allele being the functional allele that encodes the full-length protein. Some individuals, as represented by the reference genome allele, contain a single nucleotide polymorphism that results in a premature stop codon in the coding region, and therefore this allele is pseudogenic due to the failure to produce a functional full-length protein. Alternative splicing of this gene results in multiple transcript variants.

Glucosylceramidase Beta 3 (Gene/Pseudogene)

Neutral cytosolic beta-glycosidase with a broad substrate specificity that could play a role in the catabolism of glycosylceramides (PubMed:11389701, PubMed:11784319, PubMed:20728381, PubMed:26724485, PubMed:17595169).

Has a significant glucosylceramidase activity in vitro (PubMed:26724485, PubMed:17595169).

However, that activity is relatively low and its significance in vivo is not clear (PubMed:26724485, PubMed:17595169, PubMed:20728381).

Also able to hydrolyze galactosylceramide/GalCer, glucosylsphingosine/GlcSph and galactosylsphingosine/GalSph (PubMed:17595169).

However, the in vivo relevance of these activities is unclear (PubMed:17595169).

It can also hydrolyze a broad variety of dietary glycosides including phytoestrogens, flavonols, flavones, flavanones and cyanogens in vitro and could therefore play a role in the metabolism of xenobiotics (PubMed:11784319).

Could also play a role in the catabolism of cytosolic sialyl free N-glycans (PubMed:26193330).

Beta-glucoside catabolic process Source: UniProtKB
Cellular oligosaccharide catabolic process Source: CAFA
Galactosylceramide catabolic process Source: UniProtKB
Glucosylceramide catabolic process Source: UniProtKB
Glycoside catabolic process Source: UniProtKB
Glycosphingolipid metabolic process Source: Reactome
Glycosylceramide catabolic process Source: GO_Central
Positive regulation of exo-alpha-sialidase activity Source: CAFA
Protein stabilization Source: CAFA

Cytosol

The N-terminus is blocked.