UniProt functional annotation for P04062



	UniProt functional annotation for P04062

UniProt code: P04062.

Organism: Homo sapiens (Human).

Taxonomy: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.

Function: Glucosylceramidase that catalyzes, within the lysosomal compartment, the hydrolysis of glucosylceramide/GlcCer into free ceramide and glucose (PubMed:9201993, PubMed:24211208, PubMed:15916907). Thereby, 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). Also plays a role in cholesterol metabolism (PubMed:24211208, PubMed:26724485). May either catalyze the glucosylation of cholesterol, through a transglucosylation reaction that transfers glucose from glucosylceramide to cholesterol (PubMed:24211208, PubMed:26724485). The short chain saturated C8:0- GlcCer and the mono-unsaturated C18:0-GlcCer being the most effective glucose donors for that transglucosylation reaction (PubMed:24211208). Under specific conditions, may alternatively catalyze the reverse reaction, transferring glucose from cholesteryl-beta-D-glucoside to ceramide (PubMed:26724485). Finally, may also hydrolyze cholesteryl- beta-D-glucoside to produce D-glucose and cholesterol (PubMed:24211208, PubMed:26724485). {ECO:0000269|PubMed:15916907, ECO:0000269|PubMed:19279011, ECO:0000269|PubMed:24211208, ECO:0000269|PubMed:26724485, ECO:0000269|PubMed:27378698, ECO:0000269|PubMed:9201993}.

Catalytic activity: Reaction=a beta-D-glucosyl-(1<->1')-N-acylsphing-4-enine + H2O = an N- acylsphing-4-enine + D-glucose; Xref=Rhea:RHEA:13269, ChEBI:CHEBI:4167, ChEBI:CHEBI:15377, ChEBI:CHEBI:22801, ChEBI:CHEBI:52639; EC=3.2.1.45; Evidence={ECO:0000269|PubMed:15916907, ECO:0000269|PubMed:16293621, ECO:0000269|PubMed:24211208, ECO:0000269|PubMed:9201993}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13270; Evidence={ECO:0000269|PubMed:16293621};

Catalytic activity: Reaction=cholesteryl 3-beta-D-glucoside + H2O = cholesterol + D- glucose; Xref=Rhea:RHEA:11956, ChEBI:CHEBI:4167, ChEBI:CHEBI:15377, ChEBI:CHEBI:16113, ChEBI:CHEBI:17495; Evidence={ECO:0000269|PubMed:24211208}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11957; Evidence={ECO:0000305|PubMed:24211208};

Catalytic activity: Reaction=a beta-D-glucosyl-(1<->1')-N-acylsphing-4-enine + cholesterol = an N-acylsphing-4-enine + cholesteryl 3-beta-D-glucoside; Xref=Rhea:RHEA:58264, ChEBI:CHEBI:16113, ChEBI:CHEBI:17495, ChEBI:CHEBI:22801, ChEBI:CHEBI:52639; Evidence={ECO:0000269|PubMed:24211208, ECO:0000269|PubMed:26724485};

Activity regulation: Synergistically activated by saposin-A and saposin-C, two saposin peptides produced by proteolytic processing of prosaposin/PSAP (PubMed:9201993). Saposin-C activates GBA through its recruitment to membranes (PubMed:10781797, PubMed:9201993). The membrane structure and composition in anionic phospholipids are also important for the activition (PubMed:9201993, PubMed:10781797). Activated by PKC in the salvage pathway of ceramide formation (PubMed:19279011). Inhibited by conduritol B epoxide/CBE (PubMed:24211208, PubMed:26724485). {ECO:0000269|PubMed:10781797, ECO:0000269|PubMed:19279011, ECO:0000269|PubMed:24211208, ECO:0000269|PubMed:26724485, ECO:0000269|PubMed:9201993}.

Biophysicochemical properties: pH dependence: Optimum pH is 5.3. {ECO:0000269|PubMed:24211208}; Temperature dependence: Optimum temperature is 43 degrees Celsius. {ECO:0000269|PubMed:24211208};

Pathway: Steroid metabolism; cholesterol metabolism. {ECO:0000269|PubMed:24211208, ECO:0000269|PubMed:26724485}.

Pathway: Sphingolipid metabolism. {ECO:0000269|PubMed:16293621, ECO:0000269|PubMed:24211208, ECO:0000269|PubMed:26724485, ECO:0000269|PubMed:9201993}.

Subunit: Interacts with saposin-C (PubMed:10781797). Interacts with SCARB2 (PubMed:18022370). Interacts with TCP1 (PubMed:21098288). May interact with SNCA; may inhibit the glucosylceramidase activity (PubMed:23266198). Interacts with GRN; this interaction prevents aggregation of GBA-SCARB2 complex via interaction with HSPA1A upon stress (PubMed:27789271). {ECO:0000269|PubMed:10781797, ECO:0000269|PubMed:18022370, ECO:0000269|PubMed:21098288, ECO:0000269|PubMed:23266198, ECO:0000269|PubMed:27789271}.

Subcellular location: Lysosome membrane {ECO:0000269|PubMed:17187079, ECO:0000269|PubMed:17897319, ECO:0000269|PubMed:18022370}; Peripheral membrane protein {ECO:0000269|PubMed:10781797, ECO:0000269|PubMed:18022370, ECO:0000269|PubMed:1848227}; Lumenal side {ECO:0000269|PubMed:18022370}. Note=Interaction with saposin-C promotes membrane association (PubMed:10781797). Targeting to lysosomes occurs through an alternative MPR-independent mechanism via SCARB2 (PubMed:18022370). {ECO:0000269|PubMed:10781797, ECO:0000269|PubMed:18022370}.

Disease: Gaucher disease (GD) [MIM:230800]: A lysosomal storage disease due to deficient activity of beta-glucocerebrosidase and characterized by accumulation of glucosylceramide in the reticulo-endothelial system. Different clinical forms are recognized depending on the presence (neuronopathic forms) or absence of central nervous system involvement, severity and age of onset. {ECO:0000269|PubMed:10352942, ECO:0000269|PubMed:10360404, ECO:0000269|PubMed:10447266, ECO:0000269|PubMed:10744424, ECO:0000269|PubMed:10796875, ECO:0000269|PubMed:11933202, ECO:0000269|PubMed:11992489, ECO:0000269|PubMed:12204005, ECO:0000269|PubMed:15292921, ECO:0000269|PubMed:15826241, ECO:0000269|PubMed:15916907, ECO:0000269|PubMed:16293621, ECO:0000269|PubMed:17620502, ECO:0000269|PubMed:18332251, ECO:0000269|PubMed:1864608, ECO:0000269|PubMed:1972019, ECO:0000269|PubMed:1974409, ECO:0000269|PubMed:19846850, ECO:0000269|PubMed:7475546, ECO:0000269|PubMed:7627184, ECO:0000269|PubMed:7627192, ECO:0000269|PubMed:7916532, ECO:0000269|PubMed:8076951, ECO:0000269|PubMed:8112750, ECO:0000269|PubMed:8294033, ECO:0000269|PubMed:8432537, ECO:0000269|PubMed:8790604, ECO:0000269|PubMed:8829654, ECO:0000269|PubMed:8829663, ECO:0000269|PubMed:8937765, ECO:0000269|PubMed:9061570, ECO:0000269|PubMed:9153297, ECO:0000269|PubMed:9182788, ECO:0000269|PubMed:9217217, ECO:0000269|PubMed:9516376, ECO:0000269|PubMed:9554454, ECO:0000269|PubMed:9554746, ECO:0000269|PubMed:9650766, ECO:0000269|PubMed:9683600}. Note=The disease is caused by variants affecting the gene represented in this entry.

Disease: Gaucher disease 1 (GD1) [MIM:230800]: A form of Gaucher disease characterized by hepatosplenomegaly with consequent anemia and thrombopenia, and bone involvement. The central nervous system is not involved. {ECO:0000269|PubMed:10206680, ECO:0000269|PubMed:10340647, ECO:0000269|PubMed:15605411, ECO:0000269|PubMed:21098288, ECO:0000269|PubMed:22658918, ECO:0000269|PubMed:24022302, ECO:0000269|PubMed:24434810, ECO:0000269|PubMed:24577513, ECO:0000269|PubMed:8889591, ECO:0000269|Ref.14}. Note=The disease is caused by variants affecting the gene represented in this entry.

Disease: Gaucher disease 2 (GD2) [MIM:230900]: The most severe form of Gaucher disease. It manifests soon after birth, with death generally occurring before patients reach two years of age. {ECO:0000269|PubMed:10796875, ECO:0000269|PubMed:16293621, ECO:0000269|PubMed:21098288, ECO:0000269|PubMed:24022302, ECO:0000269|PubMed:7627192, ECO:0000269|PubMed:9279145, ECO:0000269|PubMed:9554454, ECO:0000269|PubMed:9637431, ECO:0000269|PubMed:9851895}. Note=The disease is caused by variants affecting the gene represented in this entry.

Disease: Gaucher disease 3 (GD3) [MIM:231000]: A subacute form of neuronopathic Gaucher disease. It has later onset and slower progression compared to the acute form of neuronopathic Gaucher disease 2. {ECO:0000269|PubMed:11933202, ECO:0000269|PubMed:24022302, ECO:0000269|PubMed:8780099}. Note=The disease is caused by variants affecting the gene represented in this entry.

Disease: Gaucher disease 3C (GD3C) [MIM:231005]: A variant of subacute neuronopathic Gaucher disease 3 associated with cardiovascular calcifications. {ECO:0000269|PubMed:9040001}. Note=The disease is caused by variants affecting the gene represented in this entry.

Disease: Gaucher disease perinatal lethal (GDPL) [MIM:608013]: Distinct form of Gaucher disease type 2, characterized by fetal onset. Hydrops fetalis, in utero fetal death and neonatal distress are prominent features. When hydrops is absent, neurologic involvement begins in the first week and leads to death within 3 months. Hepatosplenomegaly is a major sign, and is associated with ichthyosis, arthrogryposis, and facial dysmorphism. {ECO:0000269|PubMed:10352942, ECO:0000269|PubMed:11933202}. Note=The disease is caused by variants affecting the gene represented in this entry. Perinatal lethal Gaucher disease is associated with non-immune hydrops fetalis, a generalized edema of the fetus with fluid accumulation in the body cavities due to non-immune causes. Non-immune hydrops fetalis is not a diagnosis in itself but a symptom, a feature of many genetic disorders, and the end- stage of a wide variety of disorders. {ECO:0000269|PubMed:10352942}.

Disease: Parkinson disease (PARK) [MIM:168600]: A complex neurodegenerative disorder characterized by bradykinesia, resting tremor, muscular rigidity and postural instability. Additional features are characteristic postural abnormalities, dysautonomia, dystonic cramps, and dementia. The pathology of Parkinson disease involves the loss of dopaminergic neurons in the substantia nigra and the presence of Lewy bodies (intraneuronal accumulations of aggregated proteins), in surviving neurons in various areas of the brain. The disease is progressive and usually manifests after the age of 50 years, although early-onset cases (before 50 years) are known. The majority of the cases are sporadic suggesting a multifactorial etiology based on environmental and genetic factors. However, some patients present with a positive family history for the disease. Familial forms of the disease usually begin at earlier ages and are associated with atypical clinical features. {ECO:0000269|PubMed:12847165, ECO:0000269|PubMed:16148263, ECO:0000269|PubMed:17620502, ECO:0000269|PubMed:18332251, ECO:0000269|PubMed:19286695, ECO:0000269|PubMed:19846850}. Note=Disease susceptibility may be associated with variants affecting the gene represented in this entry.

Pharmaceutical: Available under the names Ceredase and Cerezyme (Genzyme). Used to treat Gaucher disease.

Miscellaneous: [Isoform Long]: Major isoform. {ECO:0000269|PubMed:3687939}.

Miscellaneous: [Isoform Short]: Produced by alternative initiation from a downstream AUG. Two to three times less protein is produced from this downstream AUG. {ECO:0000269|PubMed:3687939}.

Miscellaneous: [Isoform 3]: Produced by alternative splicing. {ECO:0000305}.

Similarity: Belongs to the glycosyl hydrolase 30 family. {ECO:0000305}.

Annotations taken from UniProtKB at the EBI.


Organism:		Homo sapiens (Human).
Taxonomy:		Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.



Function:		Glucosylceramidase that catalyzes, within the lysosomal compartment, the hydrolysis of glucosylceramide/GlcCer into free ceramide and glucose (PubMed:9201993, PubMed:24211208, PubMed:15916907). Thereby, 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). Also plays a role in cholesterol metabolism (PubMed:24211208, PubMed:26724485). May either catalyze the glucosylation of cholesterol, through a transglucosylation reaction that transfers glucose from glucosylceramide to cholesterol (PubMed:24211208, PubMed:26724485). The short chain saturated C8:0- GlcCer and the mono-unsaturated C18:0-GlcCer being the most effective glucose donors for that transglucosylation reaction (PubMed:24211208). Under specific conditions, may alternatively catalyze the reverse reaction, transferring glucose from cholesteryl-beta-D-glucoside to ceramide (PubMed:26724485). Finally, may also hydrolyze cholesteryl- beta-D-glucoside to produce D-glucose and cholesterol (PubMed:24211208, PubMed:26724485). {ECO:0000269\|PubMed:15916907, ECO:0000269\|PubMed:19279011, ECO:0000269\|PubMed:24211208, ECO:0000269\|PubMed:26724485, ECO:0000269\|PubMed:27378698, ECO:0000269\|PubMed:9201993}.


Catalytic activity:		Reaction=a beta-D-glucosyl-(1<->1')-N-acylsphing-4-enine + H2O = an N- acylsphing-4-enine + D-glucose; Xref=Rhea:RHEA:13269, ChEBI:CHEBI:4167, ChEBI:CHEBI:15377, ChEBI:CHEBI:22801, ChEBI:CHEBI:52639; EC=3.2.1.45; Evidence={ECO:0000269\|PubMed:15916907, ECO:0000269\|PubMed:16293621, ECO:0000269\|PubMed:24211208, ECO:0000269\|PubMed:9201993}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13270; Evidence={ECO:0000269\|PubMed:16293621};
Catalytic activity:		Reaction=cholesteryl 3-beta-D-glucoside + H2O = cholesterol + D- glucose; Xref=Rhea:RHEA:11956, ChEBI:CHEBI:4167, ChEBI:CHEBI:15377, ChEBI:CHEBI:16113, ChEBI:CHEBI:17495; Evidence={ECO:0000269\|PubMed:24211208}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11957; Evidence={ECO:0000305\|PubMed:24211208};
Catalytic activity:		Reaction=a beta-D-glucosyl-(1<->1')-N-acylsphing-4-enine + cholesterol = an N-acylsphing-4-enine + cholesteryl 3-beta-D-glucoside; Xref=Rhea:RHEA:58264, ChEBI:CHEBI:16113, ChEBI:CHEBI:17495, ChEBI:CHEBI:22801, ChEBI:CHEBI:52639; Evidence={ECO:0000269\|PubMed:24211208, ECO:0000269\|PubMed:26724485};
Activity regulation:		Synergistically activated by saposin-A and saposin-C, two saposin peptides produced by proteolytic processing of prosaposin/PSAP (PubMed:9201993). Saposin-C activates GBA through its recruitment to membranes (PubMed:10781797, PubMed:9201993). The membrane structure and composition in anionic phospholipids are also important for the activition (PubMed:9201993, PubMed:10781797). Activated by PKC in the salvage pathway of ceramide formation (PubMed:19279011). Inhibited by conduritol B epoxide/CBE (PubMed:24211208, PubMed:26724485). {ECO:0000269\|PubMed:10781797, ECO:0000269\|PubMed:19279011, ECO:0000269\|PubMed:24211208, ECO:0000269\|PubMed:26724485, ECO:0000269\|PubMed:9201993}.
Biophysicochemical properties:		pH dependence: Optimum pH is 5.3. {ECO:0000269\|PubMed:24211208}; Temperature dependence: Optimum temperature is 43 degrees Celsius. {ECO:0000269\|PubMed:24211208};
Pathway:		Steroid metabolism; cholesterol metabolism. {ECO:0000269\|PubMed:24211208, ECO:0000269\|PubMed:26724485}.
Pathway:		Sphingolipid metabolism. {ECO:0000269\|PubMed:16293621, ECO:0000269\|PubMed:24211208, ECO:0000269\|PubMed:26724485, ECO:0000269\|PubMed:9201993}.
Subunit:		Interacts with saposin-C (PubMed:10781797). Interacts with SCARB2 (PubMed:18022370). Interacts with TCP1 (PubMed:21098288). May interact with SNCA; may inhibit the glucosylceramidase activity (PubMed:23266198). Interacts with GRN; this interaction prevents aggregation of GBA-SCARB2 complex via interaction with HSPA1A upon stress (PubMed:27789271). {ECO:0000269\|PubMed:10781797, ECO:0000269\|PubMed:18022370, ECO:0000269\|PubMed:21098288, ECO:0000269\|PubMed:23266198, ECO:0000269\|PubMed:27789271}.
Subcellular location:		Lysosome membrane {ECO:0000269\|PubMed:17187079, ECO:0000269\|PubMed:17897319, ECO:0000269\|PubMed:18022370}; Peripheral membrane protein {ECO:0000269\|PubMed:10781797, ECO:0000269\|PubMed:18022370, ECO:0000269\|PubMed:1848227}; Lumenal side {ECO:0000269\|PubMed:18022370}. Note=Interaction with saposin-C promotes membrane association (PubMed:10781797). Targeting to lysosomes occurs through an alternative MPR-independent mechanism via SCARB2 (PubMed:18022370). {ECO:0000269\|PubMed:10781797, ECO:0000269\|PubMed:18022370}.
Disease:		Gaucher disease (GD) [MIM:230800]: A lysosomal storage disease due to deficient activity of beta-glucocerebrosidase and characterized by accumulation of glucosylceramide in the reticulo-endothelial system. Different clinical forms are recognized depending on the presence (neuronopathic forms) or absence of central nervous system involvement, severity and age of onset. {ECO:0000269\|PubMed:10352942, ECO:0000269\|PubMed:10360404, ECO:0000269\|PubMed:10447266, ECO:0000269\|PubMed:10744424, ECO:0000269\|PubMed:10796875, ECO:0000269\|PubMed:11933202, ECO:0000269\|PubMed:11992489, ECO:0000269\|PubMed:12204005, ECO:0000269\|PubMed:15292921, ECO:0000269\|PubMed:15826241, ECO:0000269\|PubMed:15916907, ECO:0000269\|PubMed:16293621, ECO:0000269\|PubMed:17620502, ECO:0000269\|PubMed:18332251, ECO:0000269\|PubMed:1864608, ECO:0000269\|PubMed:1972019, ECO:0000269\|PubMed:1974409, ECO:0000269\|PubMed:19846850, ECO:0000269\|PubMed:7475546, ECO:0000269\|PubMed:7627184, ECO:0000269\|PubMed:7627192, ECO:0000269\|PubMed:7916532, ECO:0000269\|PubMed:8076951, ECO:0000269\|PubMed:8112750, ECO:0000269\|PubMed:8294033, ECO:0000269\|PubMed:8432537, ECO:0000269\|PubMed:8790604, ECO:0000269\|PubMed:8829654, ECO:0000269\|PubMed:8829663, ECO:0000269\|PubMed:8937765, ECO:0000269\|PubMed:9061570, ECO:0000269\|PubMed:9153297, ECO:0000269\|PubMed:9182788, ECO:0000269\|PubMed:9217217, ECO:0000269\|PubMed:9516376, ECO:0000269\|PubMed:9554454, ECO:0000269\|PubMed:9554746, ECO:0000269\|PubMed:9650766, ECO:0000269\|PubMed:9683600}. Note=The disease is caused by variants affecting the gene represented in this entry.
Disease:		Gaucher disease 1 (GD1) [MIM:230800]: A form of Gaucher disease characterized by hepatosplenomegaly with consequent anemia and thrombopenia, and bone involvement. The central nervous system is not involved. {ECO:0000269\|PubMed:10206680, ECO:0000269\|PubMed:10340647, ECO:0000269\|PubMed:15605411, ECO:0000269\|PubMed:21098288, ECO:0000269\|PubMed:22658918, ECO:0000269\|PubMed:24022302, ECO:0000269\|PubMed:24434810, ECO:0000269\|PubMed:24577513, ECO:0000269\|PubMed:8889591, ECO:0000269\|Ref.14}. Note=The disease is caused by variants affecting the gene represented in this entry.
Disease:		Gaucher disease 2 (GD2) [MIM:230900]: The most severe form of Gaucher disease. It manifests soon after birth, with death generally occurring before patients reach two years of age. {ECO:0000269\|PubMed:10796875, ECO:0000269\|PubMed:16293621, ECO:0000269\|PubMed:21098288, ECO:0000269\|PubMed:24022302, ECO:0000269\|PubMed:7627192, ECO:0000269\|PubMed:9279145, ECO:0000269\|PubMed:9554454, ECO:0000269\|PubMed:9637431, ECO:0000269\|PubMed:9851895}. Note=The disease is caused by variants affecting the gene represented in this entry.
Disease:		Gaucher disease 3 (GD3) [MIM:231000]: A subacute form of neuronopathic Gaucher disease. It has later onset and slower progression compared to the acute form of neuronopathic Gaucher disease 2. {ECO:0000269\|PubMed:11933202, ECO:0000269\|PubMed:24022302, ECO:0000269\|PubMed:8780099}. Note=The disease is caused by variants affecting the gene represented in this entry.
Disease:		Gaucher disease 3C (GD3C) [MIM:231005]: A variant of subacute neuronopathic Gaucher disease 3 associated with cardiovascular calcifications. {ECO:0000269\|PubMed:9040001}. Note=The disease is caused by variants affecting the gene represented in this entry.
Disease:		Gaucher disease perinatal lethal (GDPL) [MIM:608013]: Distinct form of Gaucher disease type 2, characterized by fetal onset. Hydrops fetalis, in utero fetal death and neonatal distress are prominent features. When hydrops is absent, neurologic involvement begins in the first week and leads to death within 3 months. Hepatosplenomegaly is a major sign, and is associated with ichthyosis, arthrogryposis, and facial dysmorphism. {ECO:0000269\|PubMed:10352942, ECO:0000269\|PubMed:11933202}. Note=The disease is caused by variants affecting the gene represented in this entry. Perinatal lethal Gaucher disease is associated with non-immune hydrops fetalis, a generalized edema of the fetus with fluid accumulation in the body cavities due to non-immune causes. Non-immune hydrops fetalis is not a diagnosis in itself but a symptom, a feature of many genetic disorders, and the end- stage of a wide variety of disorders. {ECO:0000269\|PubMed:10352942}.
Disease:		Parkinson disease (PARK) [MIM:168600]: A complex neurodegenerative disorder characterized by bradykinesia, resting tremor, muscular rigidity and postural instability. Additional features are characteristic postural abnormalities, dysautonomia, dystonic cramps, and dementia. The pathology of Parkinson disease involves the loss of dopaminergic neurons in the substantia nigra and the presence of Lewy bodies (intraneuronal accumulations of aggregated proteins), in surviving neurons in various areas of the brain. The disease is progressive and usually manifests after the age of 50 years, although early-onset cases (before 50 years) are known. The majority of the cases are sporadic suggesting a multifactorial etiology based on environmental and genetic factors. However, some patients present with a positive family history for the disease. Familial forms of the disease usually begin at earlier ages and are associated with atypical clinical features. {ECO:0000269\|PubMed:12847165, ECO:0000269\|PubMed:16148263, ECO:0000269\|PubMed:17620502, ECO:0000269\|PubMed:18332251, ECO:0000269\|PubMed:19286695, ECO:0000269\|PubMed:19846850}. Note=Disease susceptibility may be associated with variants affecting the gene represented in this entry.
Pharmaceutical:		Available under the names Ceredase and Cerezyme (Genzyme). Used to treat Gaucher disease.
Miscellaneous:		[Isoform Long]: Major isoform. {ECO:0000269\|PubMed:3687939}.
Miscellaneous:		[Isoform Short]: Produced by alternative initiation from a downstream AUG. Two to three times less protein is produced from this downstream AUG. {ECO:0000269\|PubMed:3687939}.
Miscellaneous:		[Isoform 3]: Produced by alternative splicing. {ECO:0000305}.
Similarity:		Belongs to the glycosyl hydrolase 30 family. {ECO:0000305}.