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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:15916907, PubMed:24211208, PubMed:32144204, PubMed:39395789, PubMed:9201993). 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 (PubMed:19279011). Catalyzes the glucosylation of cholesterol, through a transglucosylation reaction where glucose is transferred from GlcCer to cholesterol (PubMed:24211208, PubMed:26724485, PubMed:32144204). 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) (PubMed:24211208). Under specific conditions, may alternatively catalyze the reverse reaction, transferring glucose from cholesteryl 3-beta-D-glucoside to ceramide (Probable) (PubMed:26724485). Can also hydrolyze cholesteryl 3-beta-D-glucoside producing glucose and cholesterol (PubMed:24211208, PubMed:26724485, PubMed:39395789). 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 (PubMed:32144204). 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 (PubMed:33361282). 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prosaposin/PSAP (PubMed:9201993). Saposin-C activates GBA1 through its recruitment to membranes (PubMed:10781797, PubMed:9201993). The membrane structure and composition in anionic phospholipids are also important for the activation (PubMed:10781797, PubMed:9201993). Activated by PKC in the salvage pathway of ceramide formation (PubMed:19279011). Inhibited by conduritol B epoxide/CBE (PubMed:24211208, PubMed:26724485)"}],"commentType":"ACTIVITY REGULATION"},{"commentType":"BIOPHYSICOCHEMICAL PROPERTIES","phDependence":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24211208"}],"value":"Optimum pH is 5.3."}]},"temperatureDependence":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24211208"}],"value":"Optimum temperature is 43 degrees Celsius."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24211208"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26724485"}],"value":"Steroid metabolism; cholesterol metabolism"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16293621"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24211208"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26724485"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9201993"}],"value":"Sphingolipid metabolism"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10781797"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18022370"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21098288"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23266198"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27789271"}],"value":"Interacts with saposin-C (PubMed:10781797). Interacts with SCARB2 (PubMed:18022370). Interacts with TCP1 (PubMed:21098288). May interact with SNCA; this interaction may inhibit the glucosylceramidase activity (PubMed:23266198). Interacts with GRN; this interaction prevents aggregation of GBA1-SCARB2 complex via interaction with HSPA1A upon stress (PubMed:27789271)"}],"commentType":"SUBUNIT"},{"commentType":"INTERACTION","interactions":[{"interactantOne":{"uniProtKBAccession":"P04062","intActId":"EBI-1564609"},"interactantTwo":{"uniProtKBAccession":"P17987","geneName":"TCP1","intActId":"EBI-356553"},"numberOfExperiments":2,"organismDiffer":false}]},{"commentType":"SUBCELLULAR LOCATION","note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10781797"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18022370"}],"value":"Interaction with saposin-C promotes membrane association (PubMed:10781797). Targeting to lysosomes occurs through an alternative MPR-independent mechanism via SCARB2 (PubMed:18022370)"}]},"subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17187079"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17897319"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18022370"}],"value":"Lysosome membrane","id":"SL-0157"},"topology":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10781797"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18022370"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"1848227"}],"value":"Peripheral membrane protein","id":"SL-9903"},"orientation":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18022370"}],"value":"Lumenal side","id":"SL-9914"}}]},{"commentType":"ALTERNATIVE PRODUCTS","events":["Alternative splicing","Alternative initiation"],"isoforms":[{"name":{"value":"Long"},"isoformIds":["P04062-1"],"isoformSequenceStatus":"Displayed"},{"name":{"value":"Short"},"isoformIds":["P04062-2"],"sequenceIds":["VSP_018800"],"isoformSequenceStatus":"Described"},{"name":{"value":"3"},"isoformIds":["P04062-3"],"sequenceIds":["VSP_025216","VSP_025217","VSP_025218"],"isoformSequenceStatus":"Described"},{"name":{"value":"4"},"isoformIds":["P04062-4"],"sequenceIds":["VSP_054655"],"isoformSequenceStatus":"Described"},{"name":{"value":"5"},"isoformIds":["P04062-5"],"sequenceIds":["VSP_054656"],"isoformSequenceStatus":"Described"}]},{"commentType":"DISEASE","disease":{"diseaseId":"Gaucher disease","diseaseAccession":"DI-03092","acronym":"GD","description":"An autosomal recessive lysosomal storage disease due to deficient activity of lysosomal beta-glucocerebrosidase, and characterized by accumulation of glucosylceramide in the reticulo-endothelial system. 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Couples epoxidation and carboxylation in the same active site (PubMed:39880952, PubMed:39880037). Catalyzes gamma-carboxylation of blood coagulation factors (F2, F7, F9 and F10) and anticoagulants such as PROC, which are essential for thrombosis(PubMed:17073445, PubMed:39880037). Catalyzes gamma-carboxylation of osteocalcin/BGLAP, which is essential for bone metabolism (PubMed:17073445, PubMed:39880952). 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