GLA

Existing Annotations Review

GO Term	Evidence	Action	Reason
GO:0005737 cytoplasm	IBA GO_REF:0000033	REMOVE	Summary: Phylogenetic cytoplasm annotation conflicts with the established lysosomal-lumen localization of human GLA. Reason: The reviewed evidence supports lysosome/lysosomal lumen and secretory trafficking, not a cytoplasmic active location for this soluble lysosomal hydrolase. Supporting Evidence: file:human/GLA/GLA-notes.md Cytoplasm annotations are not supported by the accessible GLA evidence reviewed here; the direct localization papers support lysosome/lysosomal lumen, secretory trafficking, extracellular secretion/uptake, and overexpression-associated TGN aggregates instead.
GO:0004557 alpha-galactosidase activity	IBA GO_REF:0000033	ACCEPT	Summary: Alpha-galactosidase activity is the core molecular function of GLA. Reason: Multiple biochemical, disease-variant, Reactome, and UniProt lines support EC 3.2.1.22 alpha-galactosidase activity toward alpha-D-galactosides/glycosphingolipids. Supporting Evidence: file:human/GLA/GLA-notes.md GLA encodes lysosomal alpha-galactosidase A, a glycosyl hydrolase whose core function is hydrolysis of terminal alpha-D-galactose from glycosphingolipids in the lysosomal lumen. file:human/GLA/GLA-deep-research-falcon.md Primary molecular function. Lysosomal α‑galactosidase A (EC 3.2.1.22) that removes terminal α‑galactose** from glycoconjugates
GO:0009311 oligosaccharide metabolic process	IBA GO_REF:0000033	KEEP AS NON CORE	Summary: Oligosaccharide metabolic process reflects the broader substrate class of alpha-galactosidases but is not the best summary of the human GLA core pathway. Reason: The central physiological process for GLA is lysosomal glycosphingolipid catabolism, while oligosaccharide substrate turnover is secondary/broader. Supporting Evidence: file:human/GLA/GLA-notes.md GLA encodes lysosomal alpha-galactosidase A, a glycosyl hydrolase whose core function is hydrolysis of terminal alpha-D-galactose from glycosphingolipids in the lysosomal lumen.
GO:0016139 glycoside catabolic process	IBA GO_REF:0000033	MODIFY	Summary: Glycoside catabolic process is directionally correct but too broad for the characterized human GLA pathway. Reason: The specific core biological process supported for human GLA is glycosphingolipid catabolic process. Proposed replacements: glycosphingolipid catabolic process Supporting Evidence: file:human/GLA/GLA-notes.md GLA encodes lysosomal alpha-galactosidase A, a glycosyl hydrolase whose core function is hydrolysis of terminal alpha-D-galactose from glycosphingolipids in the lysosomal lumen.
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds	IEA GO_REF:0000002	MODIFY	Summary: Hydrolase activity hydrolyzing O-glycosyl compounds is true but too broad for the characterized GLA enzyme activity. Reason: The specific supported molecular function is alpha-galactosidase activity. Proposed replacements: alpha-galactosidase activity Supporting Evidence: file:human/GLA/GLA-notes.md GLA encodes lysosomal alpha-galactosidase A, a glycosyl hydrolase whose core function is hydrolysis of terminal alpha-D-galactose from glycosphingolipids in the lysosomal lumen.
GO:0004557 alpha-galactosidase activity	IEA GO_REF:0000120	ACCEPT	Summary: Alpha-galactosidase activity is the core molecular function of GLA. Reason: Multiple biochemical, disease-variant, Reactome, and UniProt lines support EC 3.2.1.22 alpha-galactosidase activity toward alpha-D-galactosides/glycosphingolipids. Supporting Evidence: file:human/GLA/GLA-notes.md GLA encodes lysosomal alpha-galactosidase A, a glycosyl hydrolase whose core function is hydrolysis of terminal alpha-D-galactose from glycosphingolipids in the lysosomal lumen.
GO:0005576 extracellular region	IEA GO_REF:0000117	KEEP AS NON CORE	Summary: Automated extracellular-region annotation reflects secretion/extracellular recovery of a lysosomal enzyme rather than the core site of action. Reason: GLA can be secreted or detected extracellularly, but the central functional compartment remains the lysosomal lumen. Supporting Evidence: file:human/GLA/GLA-notes.md Extracellular-region, extracellular-exosome, and azurophil-granule annotations are best treated as non-core localization/trafficking observations; they do not change the core function from lysosomal glycosphingolipid catabolism.
GO:0005764 lysosome	IEA GO_REF:0000120	ACCEPT	Summary: Automated lysosome annotation is consistent with the established subcellular location of alpha-galactosidase A. Reason: The enzyme is a lysosomal hydrolase acting in glycosphingolipid degradation. Supporting Evidence: file:human/GLA/GLA-notes.md The physiologically central compartment is the lysosomal lumen.
GO:0005975 carbohydrate metabolic process	IEA GO_REF:0000002	MODIFY	Summary: Carbohydrate metabolic process is a very broad automated inference from glycosidase domains. Reason: Human GLA should be represented by the more specific lysosomal glycosphingolipid catabolic process. Proposed replacements: glycosphingolipid catabolic process Supporting Evidence: file:human/GLA/GLA-notes.md GLA encodes lysosomal alpha-galactosidase A, a glycosyl hydrolase whose core function is hydrolysis of terminal alpha-D-galactose from glycosphingolipids in the lysosomal lumen.
GO:0046479 glycosphingolipid catabolic process	IEA GO_REF:0000117	ACCEPT	Summary: Glycosphingolipid catabolic process captures the core biological process of lysosomal GLA activity. Reason: GLA hydrolyzes Gb3Cer/Gal2Cer and Fabry disease results from impaired glycosphingolipid degradation. Supporting Evidence: file:human/GLA/GLA-notes.md Reactome models the core lysosomal reaction as GLA hydrolyzing saposin-B-mobilized Gb3Cer and Gal2Cer in the lysosomal lumen: file:human/GLA/GLA-deep-research-falcon.md GLA function sits within lysosomal glycosphingolipid catabolism
GO:0005515 protein binding	IPI PMID:21949853 Receptor-mediated endocytosis of α-galactosidase A in human ...	MODIFY	Summary: Sortilin/M6PR/megalin uptake data support receptor binding rather than generic protein binding. Reason: The biologically interpretable function is binding endocytic/sorting receptors during uptake of secreted or therapeutic GLA. Proposed replacements: signaling receptor binding Supporting Evidence: file:human/GLA/GLA-notes.md Recombinant or secreted alpha-Gal A can bind endocytic/sorting receptors for uptake: file:human/GLA/GLA-deep-research-falcon.md Additional uptake routes reported in kidney cells include sortilin and megalin.
GO:0005515 protein binding	IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling...	MARK AS OVER ANNOTATED	Summary: High-throughput interactome evidence gives only a generic protein-binding annotation and does not define GLA function. Reason: Generic protein binding is not informative for a lysosomal enzyme and these high-throughput interactions are not sufficient to add a core or specific GLA molecular function. Supporting Evidence: file:human/GLA/GLA-notes.md Generic protein binding is not informative for GLA.
GO:0005515 protein binding	IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac...	MARK AS OVER ANNOTATED	Summary: High-throughput interactome evidence gives only a generic protein-binding annotation and does not define GLA function. Reason: Generic protein binding is not informative for a lysosomal enzyme and these high-throughput interactions are not sufficient to add a core or specific GLA molecular function. Supporting Evidence: file:human/GLA/GLA-notes.md Generic protein binding is not informative for GLA.
GO:0005515 protein binding	IPI PMID:40205054 Multimodal cell maps as a foundation for structural and func...	MARK AS OVER ANNOTATED	Summary: High-throughput interactome evidence gives only a generic protein-binding annotation and does not define GLA function. Reason: Generic protein binding is not informative for a lysosomal enzyme and these high-throughput interactions are not sufficient to add a core or specific GLA molecular function. Supporting Evidence: file:human/GLA/GLA-notes.md Generic protein binding is not informative for GLA.
GO:0004557 alpha-galactosidase activity	IMP PMID:10838196 Characterization of two alpha-galactosidase mutants (Q279E a...	ACCEPT	Summary: Alpha-galactosidase activity is the core molecular function of GLA. Reason: Multiple biochemical, disease-variant, Reactome, and UniProt lines support EC 3.2.1.22 alpha-galactosidase activity toward alpha-D-galactosides/glycosphingolipids. Supporting Evidence: file:human/GLA/GLA-notes.md GLA encodes lysosomal alpha-galactosidase A, a glycosyl hydrolase whose core function is hydrolysis of terminal alpha-D-galactose from glycosphingolipids in the lysosomal lumen.
GO:0004557 alpha-galactosidase activity	IDA PMID:8804427 Only sphingolipid activator protein B (SAP-B or saposin B) s...	ACCEPT	Summary: Alpha-galactosidase activity is the core molecular function of GLA. Reason: Multiple biochemical, disease-variant, Reactome, and UniProt lines support EC 3.2.1.22 alpha-galactosidase activity toward alpha-D-galactosides/glycosphingolipids. Supporting Evidence: file:human/GLA/GLA-notes.md GLA encodes lysosomal alpha-galactosidase A, a glycosyl hydrolase whose core function is hydrolysis of terminal alpha-D-galactose from glycosphingolipids in the lysosomal lumen.
GO:0046479 glycosphingolipid catabolic process	IMP PMID:10838196 Characterization of two alpha-galactosidase mutants (Q279E a...	ACCEPT	Summary: Glycosphingolipid catabolic process captures the core biological process of lysosomal GLA activity. Reason: GLA hydrolyzes Gb3Cer/Gal2Cer and Fabry disease results from impaired glycosphingolipid degradation. Supporting Evidence: file:human/GLA/GLA-notes.md Reactome models the core lysosomal reaction as GLA hydrolyzing saposin-B-mobilized Gb3Cer and Gal2Cer in the lysosomal lumen:
GO:0046479 glycosphingolipid catabolic process	IDA PMID:8804427 Only sphingolipid activator protein B (SAP-B or saposin B) s...	ACCEPT	Summary: Glycosphingolipid catabolic process captures the core biological process of lysosomal GLA activity. Reason: GLA hydrolyzes Gb3Cer/Gal2Cer and Fabry disease results from impaired glycosphingolipid degradation. Supporting Evidence: file:human/GLA/GLA-notes.md Reactome models the core lysosomal reaction as GLA hydrolyzing saposin-B-mobilized Gb3Cer and Gal2Cer in the lysosomal lumen:
GO:0005576 extracellular region	TAS Reactome:R-HSA-6798751	KEEP AS NON CORE	Summary: Reactome extracellular-region placement is compatible with neutrophil degranulation/exocytosis but is not the core GLA location. Reason: Extracellular release is a localization/trafficking observation; the catalytic role is lysosomal glycosphingolipid catabolism. Supporting Evidence: file:human/GLA/GLA-notes.md Extracellular-region, extracellular-exosome, and azurophil-granule annotations are best treated as non-core localization/trafficking observations; they do not change the core function from lysosomal glycosphingolipid catabolism.
GO:0035578 azurophil granule lumen	TAS Reactome:R-HSA-6798751	KEEP AS NON CORE	Summary: Azurophil-granule lumen placement is a specialized neutrophil granule localization and not the core site of GLA activity. Reason: Azurophil granules are lysosome-related secretory granules, whereas the conserved function is lysosomal lumen glycosphingolipid degradation. Supporting Evidence: file:human/GLA/GLA-notes.md Extracellular-region, extracellular-exosome, and azurophil-granule annotations are best treated as non-core localization/trafficking observations; they do not change the core function from lysosomal glycosphingolipid catabolism.
GO:0004557 alpha-galactosidase activity	IDA PMID:27211852 A novel mutation of α-galactosidase A gene causes Fabry dise...	ACCEPT	Summary: Alpha-galactosidase activity is the core molecular function of GLA. Reason: Multiple biochemical, disease-variant, Reactome, and UniProt lines support EC 3.2.1.22 alpha-galactosidase activity toward alpha-D-galactosides/glycosphingolipids. Supporting Evidence: file:human/GLA/GLA-notes.md GLA encodes lysosomal alpha-galactosidase A, a glycosyl hydrolase whose core function is hydrolysis of terminal alpha-D-galactose from glycosphingolipids in the lysosomal lumen.
GO:0070062 extracellular exosome	HDA PMID:23533145 In-depth proteomic analyses of exosomes isolated from expres...	KEEP AS NON CORE	Summary: High-throughput detection in urinary/prostatic exosome preparations is a non-core extracellular-vesicle localization. Reason: Exosome proteomics can capture secreted lysosomal enzymes, but it does not define the core compartment where GLA acts. Supporting Evidence: file:human/GLA/GLA-notes.md Extracellular-region, extracellular-exosome, and azurophil-granule annotations are best treated as non-core localization/trafficking observations; they do not change the core function from lysosomal glycosphingolipid catabolism.
GO:0043202 lysosomal lumen	TAS Reactome:R-HSA-1605736	ACCEPT	Summary: Reactome lysosomal-lumen annotation accompanies the modeled Gb3Cer hydrolysis reaction. Reason: The lysosomal lumen is the physiologically central compartment for GLA glycosphingolipid hydrolysis. Supporting Evidence: file:human/GLA/GLA-notes.md The physiologically central compartment is the lysosomal lumen.
GO:0043202 lysosomal lumen	TAS Reactome:R-HSA-9841189	ACCEPT	Summary: Reactome lysosomal-lumen annotation accompanies the modeled Gal2Cer hydrolysis reaction. Reason: The lysosomal lumen is the physiologically central compartment for GLA glycosphingolipid hydrolysis. Supporting Evidence: file:human/GLA/GLA-notes.md The physiologically central compartment is the lysosomal lumen.
GO:0046477 glycosylceramide catabolic process	ISS GO_REF:0000024	MODIFY	Summary: Glycosylceramide catabolic process is narrower/less appropriate than the established glycosphingolipid catabolic role for GLA. Reason: Human GLA acts on glycosphingolipids such as Gb3Cer and Gal2Cer; the replacement term captures that broader, well-supported pathway. Proposed replacements: glycosphingolipid catabolic process Supporting Evidence: file:human/GLA/GLA-notes.md Reactome models the core lysosomal reaction as GLA hydrolyzing saposin-B-mobilized Gb3Cer and Gal2Cer in the lysosomal lumen:
GO:0004557 alpha-galactosidase activity	IMP PMID:16372133 Comparison of the effects of agalsidase alfa and agalsidase ...	ACCEPT	Summary: Alpha-galactosidase activity is the core molecular function of GLA. Reason: Multiple biochemical, disease-variant, Reactome, and UniProt lines support EC 3.2.1.22 alpha-galactosidase activity toward alpha-D-galactosides/glycosphingolipids. Supporting Evidence: file:human/GLA/GLA-notes.md GLA encodes lysosomal alpha-galactosidase A, a glycosyl hydrolase whose core function is hydrolysis of terminal alpha-D-galactose from glycosphingolipids in the lysosomal lumen.
GO:0045019 negative regulation of nitric oxide biosynthetic process	ISS GO_REF:0000024	MARK AS OVER ANNOTATED	Summary: Nitric oxide biosynthesis regulation is a downstream disease/orthology phenotype, not a direct core process of the GLA hydrolase. Reason: The accessible evidence supports lysosomal glycosphingolipid degradation; NO regulation should not be represented as a human GLA core biological process. Supporting Evidence: file:human/GLA/GLA-notes.md Nitric-oxide and nitric-oxide-synthase regulation annotations are downstream Fabry-disease/orthology phenotypes rather than direct activities of the lysosomal hydrolase; they should not be represented as core biological processes for human GLA.
GO:0051001 negative regulation of nitric-oxide synthase activity	ISS GO_REF:0000024	MARK AS OVER ANNOTATED	Summary: Nitric-oxide synthase activity regulation is a downstream disease/orthology phenotype, not a direct process executed by GLA. Reason: The core biology is lysosomal glycosphingolipid catabolism, and NOS regulation is too indirect for a core GLA annotation. Supporting Evidence: file:human/GLA/GLA-notes.md Nitric-oxide and nitric-oxide-synthase regulation annotations are downstream Fabry-disease/orthology phenotypes rather than direct activities of the lysosomal hydrolase; they should not be represented as core biological processes for human GLA.
GO:0003824 catalytic activity	IDA PMID:39940 Studies on human liver alpha-galactosidases. I. Purification...	MODIFY	Summary: Catalytic activity is too generic for the purified alpha-galactosidase A assay evidence. Reason: The direct assay supports the specific alpha-galactosidase activity term rather than generic catalytic activity. Proposed replacements: alpha-galactosidase activity Supporting Evidence: file:human/GLA/GLA-notes.md GLA encodes lysosomal alpha-galactosidase A, a glycosyl hydrolase whose core function is hydrolysis of terminal alpha-D-galactose from glycosphingolipids in the lysosomal lumen.
GO:0004557 alpha-galactosidase activity	IDA PMID:39940 Studies on human liver alpha-galactosidases. I. Purification...	ACCEPT	Summary: Alpha-galactosidase activity is the core molecular function of GLA. Reason: Multiple biochemical, disease-variant, Reactome, and UniProt lines support EC 3.2.1.22 alpha-galactosidase activity toward alpha-D-galactosides/glycosphingolipids. Supporting Evidence: file:human/GLA/GLA-notes.md GLA encodes lysosomal alpha-galactosidase A, a glycosyl hydrolase whose core function is hydrolysis of terminal alpha-D-galactose from glycosphingolipids in the lysosomal lumen.
GO:0005102 signaling receptor binding	IDA PMID:1332979 Overexpression of human alpha-galactosidase A results in its...	KEEP AS NON CORE	Summary: Mannose-6-phosphate receptor binding is supported for secreted recombinant enzyme uptake/targeting, but it is not the core catalytic function. Reason: Receptor binding is a trafficking/uptake property of secreted or therapeutic enzyme; GLA remains primarily a lysosomal hydrolase. Supporting Evidence: file:human/GLA/GLA-notes.md Recombinant or secreted alpha-Gal A can bind endocytic/sorting receptors for uptake:
GO:0005515 protein binding	IPI PMID:1332979 Overexpression of human alpha-galactosidase A results in its...	MODIFY	Summary: Generic protein binding masks the more specific mannose-6-phosphate receptor binding/lysosomal targeting evidence. Reason: The supported interaction is receptor binding by the secreted enzyme, not an unqualified protein-binding function. Proposed replacements: signaling receptor binding Supporting Evidence: file:human/GLA/GLA-notes.md Recombinant or secreted alpha-Gal A can bind endocytic/sorting receptors for uptake:
GO:0005515 protein binding	IPI PMID:6313412 ConA-mediated binding and uptake of purified alpha-galactosi...	REMOVE	Summary: ConA-mediated uptake uses an exogenous plant lectin and should not be treated as an endogenous GLA protein-binding function. Reason: The interaction is an experimental delivery/stabilization condition rather than a physiological human molecular function of GLA. Supporting Evidence: file:human/GLA/GLA-notes.md The ConA-mediated uptake study used concanavalin A to stabilize and deliver purified enzyme to Fabry fibroblasts, so a GO protein-binding annotation to ConA should not be treated as an endogenous GLA function
GO:0005576 extracellular region	IMP PMID:1332979 Overexpression of human alpha-galactosidase A results in its...	KEEP AS NON CORE	Summary: Extracellular region is supported for overexpressed/secreted enzyme but is secondary to lysosomal targeting. Reason: The paper describes selective secretion of overexpressed GLA while also showing lysosomal targeting; secretion is not the core location. Supporting Evidence: file:human/GLA/GLA-notes.md GLA enters the secretory/lysosomal trafficking pathway as a precursor and can be secreted under some conditions:
GO:0005576 extracellular region	IDA PMID:3029062 Synthesis and processing of alpha-galactosidase A in human f...	KEEP AS NON CORE	Summary: Secretion of precursor enzyme under NH4Cl/I-cell fibroblast conditions supports extracellular occurrence but not the core GLA location. Reason: This is a trafficking/secretion observation for a lysosomal enzyme rather than its catalytic compartment. Supporting Evidence: file:human/GLA/GLA-notes.md GLA enters the secretory/lysosomal trafficking pathway as a precursor and can be secreted under some conditions:
GO:0005737 cytoplasm	IMP PMID:1332979 Overexpression of human alpha-galactosidase A results in its...	REMOVE	Summary: The overexpression study localizes GLA aggregates to TGN and lysosomes and does not support cytoplasmic localization. Reason: Cytoplasm is inconsistent with the accessible localization evidence for this signal-peptide-containing lysosomal lumen enzyme. Supporting Evidence: file:human/GLA/GLA-notes.md Cytoplasm annotations are not supported by the accessible GLA evidence reviewed here; the direct localization papers support lysosome/lysosomal lumen, secretory trafficking, extracellular secretion/uptake, and overexpression-associated TGN aggregates instead.
GO:0005764 lysosome	IMP PMID:1332979 Overexpression of human alpha-galactosidase A results in its...	ACCEPT	Summary: Immunogold labeling of overexpressed enzyme in lysosomes supports lysosomal localization. Reason: This matches the established lysosomal hydrolase role of GLA. Supporting Evidence: file:human/GLA/GLA-notes.md The physiologically central compartment is the lysosomal lumen.
GO:0005764 lysosome	TAS PMID:3029062 Synthesis and processing of alpha-galactosidase A in human f...	ACCEPT	Summary: Fibroblast biosynthesis/processing data support delivery of mature alpha-galactosidase A to lysosomes. Reason: Processing and lysosomal delivery are part of the normal biogenesis of this lysosomal hydrolase. Supporting Evidence: file:human/GLA/GLA-notes.md GLA enters the secretory/lysosomal trafficking pathway as a precursor and can be secreted under some conditions:
GO:0005794 Golgi apparatus	IMP PMID:1332979 Overexpression of human alpha-galactosidase A results in its...	MARK AS OVER ANNOTATED	Summary: Golgi/TGN signal in this paper reflects overexpression-associated aggregation during trafficking, not a stable core localization. Reason: The TGN crystals arose under high overexpression and are better treated as a trafficking/overexpression phenotype than as a normal GLA cellular component. Supporting Evidence: file:human/GLA/GLA-notes.md Overexpression in CHO cells caused TGN and lysosomal crystalline aggregates and selective secretion; the authors explicitly proposed that aggregates forming in the acidic TGN are secreted when unable to bind M6P receptors, making Golgi/TGN accumulation an overexpression phenotype rather than the core location
GO:0009311 oligosaccharide metabolic process	IDA PMID:39940 Studies on human liver alpha-galactosidases. I. Purification...	KEEP AS NON CORE	Summary: Purified-enzyme work with oligosaccharide substrates supports a broader substrate range but not the main physiological process. Reason: This substrate-scope observation is secondary to the disease-relevant glycosphingolipid catabolic function. Supporting Evidence: file:human/GLA/GLA-notes.md GLA encodes lysosomal alpha-galactosidase A, a glycosyl hydrolase whose core function is hydrolysis of terminal alpha-D-galactose from glycosphingolipids in the lysosomal lumen.
GO:0016787 hydrolase activity	TAS PMID:7911050 Molecular basis of Fabry disease: mutations and polymorphism...	MODIFY	Summary: Hydrolase activity is too generic for a lysosomal alpha-galactosidase with known EC 3.2.1.22 activity. Reason: The annotation should use alpha-galactosidase activity to capture the specific enzymatic function. Proposed replacements: alpha-galactosidase activity Supporting Evidence: file:human/GLA/GLA-notes.md GLA encodes lysosomal alpha-galactosidase A, a glycosyl hydrolase whose core function is hydrolysis of terminal alpha-D-galactose from glycosphingolipids in the lysosomal lumen.
GO:0042803 protein homodimerization activity	IDA PMID:6256390 Affinity purification of alpha-galactosidase A from human sp...	KEEP AS NON CORE	Summary: Protein homodimerization is directly supported for purified GLA and describes the active enzyme state. Reason: Homodimerization is a structural property important for the enzyme but not the primary molecular activity captured in the core function. Supporting Evidence: file:human/GLA/GLA-notes.md Purified human alpha-galactosidase A is a homodimeric enzyme:
GO:0046479 glycosphingolipid catabolic process	TAS PMID:2160973 Alpha-galactosidase A gene rearrangements causing Fabry dise...	ACCEPT	Summary: Glycosphingolipid catabolic process captures the core biological process of lysosomal GLA activity. Reason: GLA hydrolyzes Gb3Cer/Gal2Cer and Fabry disease results from impaired glycosphingolipid degradation. Supporting Evidence: file:human/GLA/GLA-notes.md Reactome models the core lysosomal reaction as GLA hydrolyzing saposin-B-mobilized Gb3Cer and Gal2Cer in the lysosomal lumen:

Gene Description

Existing Annotations Review

Core Functions

Hydrolyzes terminal alpha-D-galactose residues from lysosomal glycosphingolipids, especially globotriaosylceramide (Gb3Cer) and Gal2Cer, as a saposin-B-dependent homodimeric alpha-galactosidase A in the lysosomal lumen.

References

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Falcon

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Notes

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