Recombinant Mouse Lysosomal acid Glucosylceramidase (Gba1)

Function

Glucosylceramidase that catalyzes, within the lysosomal compartment, the hydrolysis of glucosylceramides/GlcCers (such as beta-D-glucosyl-(1<->1')-N-acylsphing-4-enine) into free ceramides (such as N-acylsphing-4-enine) and glucose (PubMed:24211208). Plays a central role in the degradation of complex lipids and the turnover of cellular membranes (PubMed:27378698). Through the production of ceramides, participates in the PKC-activated salvage pathway of ceramide formation (By similarity). Catalyzes the glucosylation of cholesterol, through a transglucosylation reaction where glucose is transferred from GlcCer to cholesterol (PubMed:24211208). GlcCer containing mono-unsaturated fatty acids (such as beta-D-glucosyl-N-(9Z-octadecenoyl)-sphing-4-enine) are preferred as glucose donors for cholesterol glucosylation when compared with GlcCer containing same chain length of saturated fatty acids (such as beta-D-glucosyl-N-octadecanoyl-sphing-4-enine) (By similarity). Under specific conditions, may alternatively catalyze the reverse reaction, transferring glucose from cholesteryl 3-beta-D-glucoside to ceramide (By similarity). Can also hydrolyze cholesteryl 3-beta-D-glucoside producing glucose and cholesterol (By similarity). Catalyzes the hydrolysis of galactosylceramides/GalCers (such as beta-D-galactosyl-(1<->1')-N-acylsphing-4-enine), as well as the transfer of galactose between GalCers and cholesterol in vitro, but with lower activity than with GlcCers (By similarity). Contrary to GlcCer and GalCer, xylosylceramide/XylCer (such as beta-D-xyosyl-(1<->1')-N-acylsphing-4-enine) is not a good substrate for hydrolysis, however it is a good xylose donor for transxylosylation activity to form cholesteryl 3-beta-D-xyloside (By similarity)

Subcellular Location

Lysosome membrane (Peripheral membrane protein)

Subunit

Interacts with saposin-C. Interacts with SCARB2. Interacts with TCP1 (By similarity). Interacts with GRN; this interaction prevents aggregation of GBA1-SCARB2 complex via interaction with HSPA1A upon stress (PubMed:27789271)

Pathway

Sphingolipid metabolism

• O'Neill R.R. et al. Comparison of the chromosomal localization of murine and human glucocerebrosidase genes and of the deduced amino acid sequences. — Proc. Natl. Acad. Sci. U.S.A. (1989)
• Sinclair G. et al. Comparative sequence analysis of the mouse and human GBA locus. (MAY-)
• Carninci P. et al. The transcriptional landscape of the mammalian genome. — Science (2005)
• The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). — Genome Res. (2004)
• Carstea E.D. et al. Molecular and functional characterization of the murine glucocerebrosidase gene. — Biochem. Biophys. Res. Commun. (1992)
• Lubec G. et al. PubMed: CI-DHLEILD3HP6AK (JAN-)
• Tybulewicz V.L. et al. Animal model of Gaucher's disease from targeted disruption of the mouse glucocerebrosidase gene. — Nature (1992)
• Uematsu R. et al. High throughput quantitative glycomics and glycoform-focused proteomics of murine dermis and epidermis. — Mol. Cell. Proteomics (2005)