ARSB

Existing Annotations Review

GO Term	Evidence	Action	Reason
GO:0008484 sulfuric ester hydrolase activity	IBA GO_REF:0000033	ACCEPT	Summary: Retain the independently corroborated inherited sulfatase activity. Reason: Human ARSB hydrolyses sulfate esters, independently supported by its established N-acetylgalactosamine-4-sulfatase reaction and human structure. PTN002233267 is the actual inherited node; its tree/MSA/IBD placement remains uninspected. Accept the supported activity without claiming a phylogenetic reconstruction. P15848 in its own descendant evidence is expected and is not circular support. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN002233267 UNRESOLVED Exact ancestral node; tree/MSA/IBD placement was not independently reconstructed. Human enzyme chemistry corroborates the inherited function. Supporting Evidence: PMID:19306108 the enzyme that removes 4-sulfate groups from N-acetylgalactosamine 4-sulfate, which combines with glucuronate to form the disaccharide unit of chondroitin-4-sulfate (C4S).
GO:0003943 N-acetylgalactosamine-4-sulfatase activity	IEA GO_REF:0000003	ACCEPT	Summary: Accept the defining GalNAc-4-sulfatase reaction. Reason: The EC3.1.6.12 mapping names the defining ARSB reaction: hydrolysis of GalNAc 4-sulfate in chondroitin and dermatan sulfate. Human cellular substrate studies and the exact Reactome catalyst independently support this assignment. The original EC source is preserved. Supporting Evidence: PMID:19306108 the enzyme that removes 4-sulfate groups from N-acetylgalactosamine 4-sulfate, which combines with glucuronate to form the disaccharide unit of chondroitin-4-sulfate (C4S).
GO:0004065 arylsulfatase activity	IEA GO_REF:0000117	KEEP AS NON CORE	Summary: Retain aryl-sulfate assay activity as a non-core function. Reason: Arylsulfatase activity is a distinct aryl-sulfate reaction, not a parent synonym for GalNAc-4-sulfatase. Both GO terms have sulfuric ester hydrolase as parent. Preserve the existing assay-substrate activity as non-core in the context of the historical arylsulfatase assays; do not equate its aromatic substrate with physiological CS/DS or pretend the exact ARBA00087504 rule was reconstructed. The PMID8037 quote describes a rat aromatic-substrate assay and is comparative context; the PMID2303452 quote supplies the direct expressed-human-enzyme activity observation. Supporting Evidence: PMID:2303452 Overexpression of ASB in transfected baby hamster kidney (BHK) cells resulted in up to 68-fold higher ASB activity than in untransfected BHK cells. PMID:8037 incubating the gels with p-nitrocatechol sulphate as substrate
GO:0005764 lysosome	IEA GO_REF:0000044	ACCEPT	Summary: Accept lysosomal localization of the processed human enzyme. Reason: The mapped lysosome location agrees with the original human cDNA expressed in BHK cells: the processed human enzyme was found in dense lysosomes. It also agrees with the human Reactome catalyst in lysosomal lumen. Supporting Evidence: PMID:2303452 The 47-kDa ASB form was located in dense lysosomes.
GO:0008484 sulfuric ester hydrolase activity	IEA GO_REF:0000120	ACCEPT	Summary: Retain sulfate-ester hydrolysis supported by human enzyme chemistry. Reason: Combined rat-ortholog/IPR047115 inference agrees with established human sulfate-ester hydrolysis. Retain the broad true activity; do not treat rat donor count as evidence strength or assert that the entire combined rule was independently replayed. Propagation Review Root cause: NO FAILURE CORE Sources checked: UniProtKB:P50430 SUPPORTS TRANSFER The rat Arsb ortholog is compatible with sulfate-ester hydrolysis, independently corroborated for human ARSB by PMID19306108 and the Reactome catalytic reaction. ensembl:ENSRNOP00000014860 SUPPORTS TRANSFER This rat Ensembl protein is part of the same orthology source; it supplies no independent experimental replicate. InterPro:IPR047115 UNRESOLVED The combined mapping includes this InterPro identifier. Its exact member/rule contribution was not replayed; the accepted human catalytic activity does not depend on assuming that replay. Supporting Evidence: PMID:19306108 the enzyme that removes 4-sulfate groups from N-acetylgalactosamine 4-sulfate, which combines with glucuronate to form the disaccharide unit of chondroitin-4-sulfate (C4S).
GO:0009986 cell surface	IEA GO_REF:0000120	UNDECIDED	Summary: The precise source evidence for cell-surface localization remains unresolved. Reason: The assertion combines rat Arsb transfer and SL-0310 cell-surface mapping. The precise original surface-localization experiment underlying those sources has not been recovered. Lysosomal maturation and secretion do not refute an additional surface pool, but neither establishes it. Retain the source assertion unresolved rather than remove it from incomplete evidence. The preserved UniProt cell-surface CC separately cites by-similarity P50429; this is not silently replaced by the P50430 GOA donor. Propagation Review Root cause: UNRESOLVED Sources checked: UniProtKB:P50430 UNRESOLVED Rat Arsb donor P50430 is retained; the original cell-surface assay underlying this donor assertion remains unread. ensembl:ENSRNOP00000014860 UNRESOLVED The original rat Ensembl protein identifier is preserved as part of the same transfer; it is not an independent localization experiment. UniProtKB-SubCell:SL-0310 UNRESOLVED SL-0310 supplies the cell-surface vocabulary mapping, not a source assay. Its underlying localization evidence remains unresolved. Supporting Evidence: file:human/ARSB/ARSB-uniprot.txt surface {ECO:0000250\|UniProtKB:P50429}.
GO:0016787 hydrolase activity	IEA GO_REF:0000043	MODIFY	Summary: Refine generic hydrolase activity to the established substrate-specific activity. Reason: Hydrolase activity is correct but less informative than the established GalNAc-4-sulfatase reaction. Replace the generic keyword-derived function with the specific catalytic activity already supported in this review. Proposed replacements: N-acetylgalactosamine-4-sulfatase activity Supporting Evidence: PMID:19306108 the enzyme that removes 4-sulfate groups from N-acetylgalactosamine 4-sulfate, which combines with glucuronate to form the disaccharide unit of chondroitin-4-sulfate (C4S).
GO:0046872 metal ion binding	IEA GO_REF:0000043	MODIFY	Summary: Refine metal binding to the catalytic calcium cofactor. Reason: The human ARSB structure identifies an active-site calcium ion. Refine metal-ion binding to calcium-ion binding; this is a bound catalytic cofactor, not a separate physiological calcium-signaling function. The exact original abstract was independently read; full structural Methods were not. Proposed replacements: calcium ion binding Supporting Evidence: file:human/ARSB/ARSB-uniprot.txt Binds 1 Ca(2+) ion per subunit. PMID:9032078 The sulfate is bound to a previously undetected metal ion, which we have identified as calcium.
GO:0006914 autophagy	IEA GO_REF:0000107	UNDECIDED	Summary: The exact autophagy participation assertion remains unresolved. Reason: The rat donor trace leads to PMID8037. Its complete abstract reports arylsulfatase A/B activity-ratio changes under treatments promoting autophagy, not an independently resolved step performed by Arsb. The normal cache is abstract-only, and the underlying autophagy-participation claim remains unverified. Keep UNDECIDED rather than turn an unread experiment into a demonstrated false assertion. The paper's historical proposed A-to-B conversion is not adopted as modern ARSB biochemistry; that rejected identity model alone does not falsify every autophagy-related observation in the study. Propagation Review Root cause: UNRESOLVED Sources checked: UniProtKB:P50430 UNRESOLVED P50430 traces to the rat activity-ratio/autophagy source PMID8037; the complete abstract does not settle Arsb process participation. ensembl:ENSRNOP00000014860 UNRESOLVED This rat Ensembl identifier is the accompanying orthology source, not a second autophagy experiment; its source-level limitation is the same unread full paper. Supporting Evidence: PMID:8037 this ratio declines during enhanced autophagocytosis.
GO:0007584 response to nutrient	IEA GO_REF:0000107	KEEP AS NON CORE	Summary: Retain the contextual nutrient-response inference with rat cell and age limits. Reason: The exact rat donor source reports dietary-restriction-associated activity changes, including higher Arsb activity in older restricted Kupffer/endothelial cells; hepatocytes showed no significant dietary effect. This is evidence of a context-dependent nutrient response, not nutrient sensing or a new catalytic role. Retain the existing orthology inference as non-core with rat/cell-age limits, without claiming a human dietary experiment. Propagation Review Root cause: NO FAILURE NON CORE Sources checked: UniProtKB:P50430 SUPPORTS TRANSFER The rat P50430 source has dietary-restriction-associated activity changes in the specified liver cell populations and age groups (PMID2290353). ensembl:ENSRNOP00000014860 SUPPORTS TRANSFER This Ensembl rat protein source accompanies the same orthology inference; it does not add an independent human dietary experiment. Supporting Evidence: PMID:2290353 Rats exposed to dietary restriction (R) showed higher activities of beta-galactosidase, arylsulfatase B and cathepsin D when compared to corresponding A animals with the exception of the younger age group.
GO:0009268 response to pH	IEA GO_REF:0000107	UNDECIDED	Summary: The donor pH-response assertion cannot be fully adjudicated from its abstract. Reason: The PMID6137211 abstract describes rat-enzyme pH-dependent kinetics and ionization; those observations alone do not establish the cell or organism response named by GO0009268. The normal cache explicitly has full_text_available=false: its section labelled Full Text repeats the abstract, while PMC identifies five scanned article pages (603–607). Those pages were not successfully accessed. Retain UNDECIDED for the precise donor-source assertion under the incomplete-evidence rule, without claiming that the unseen paper contains a supporting response experiment. Neither an acidic activity optimum nor absence of a direct pH-sensing role is itself a reason to remove the annotation. Propagation Review Root cause: UNRESOLVED Sources checked: UniProtKB:P50430 UNRESOLVED P50430 traces to rat-enzyme kinetics PMID6137211. Its abstract-only cache cannot fully adjudicate the cellular/organismal response assertion. ensembl:ENSRNOP00000014860 UNRESOLVED The rat Ensembl protein identifies the accompanying transfer source; no independent pH-response experiment is supplied by this identifier. Supporting Evidence: PMID:6137211 The effect of pH on the kinetics of rat liver arylsulphatases A and B is very similar and shows that two groups with pK values of 4.4-4.5 and 5.7-5.8 are important for enzyme activity.
GO:0010976 positive regulation of neuron projection development	IEA GO_REF:0000107	KEEP AS NON CORE	Summary: Retain the neurite-outgrowth consequence as non-core. Reason: PMID24311516 directly tests rat astrocyte/neuron cocultures: astrocyte ARSB knockdown reduces neurite growth, and added recombinant human ARSB attenuates ethanol-induced outgrowth defects. Retain the existing positive neurite-development inference as a supported contextual consequence of substrate remodeling. It is not intrinsic neuron-growth-factor activity or an experiment on human neurons. Propagation Review Root cause: NO FAILURE NON CORE Sources checked: UniProtKB:P50430 SUPPORTS TRANSFER Rat Arsb experiments in astrocyte/neuron coculture and human-enzyme rescue support the contextual neurite-growth consequence (PMID24311516). ensembl:ENSRNOP00000014860 SUPPORTS TRANSFER This rat Ensembl identifier accompanies the same donor experiment; recombinant human enzyme in rat coculture is not a human-neuron assay. Supporting Evidence: PMID:24311516 Neurite outgrowth of hippocampal pyramidal neurons co-cultured with ARSB-silenced astrocytes was reduced when compared to neurite outgrowth in neurons co-cultured with untreated astrocytes and astrocytes transfected with a non-target siRNA (Fig. 8 A–D)
GO:0043627 response to estrogen	IEA GO_REF:0000107	KEEP AS NON CORE	Summary: Retain the source-supported estrogen response as non-core. Reason: The exact donor paper demonstrates dose-dependent estrogen-associated changes in rat cervical arylsulfatase B activity after ovariectomy, with a cycloheximide-sensitive increase at the lower estradiol dose and inhibition at the higher dose. That is a response-compatible observation, not estrogen hydrolysis. Retain the existing orthology response assertion as non-core, explicitly bounded to the source organism and tissue. Propagation Review Root cause: NO FAILURE NON CORE Sources checked: UniProtKB:P50430 SUPPORTS TRANSFER The rat donor evidence includes dose-dependent estradiol effects after ovariectomy and cycloheximide sensitivity (PMID15040). ensembl:ENSRNOP00000014860 SUPPORTS TRANSFER The rat Ensembl identifier carries the same contextual response inference; it does not imply estrogen hydrolysis or an independent human experiment. Supporting Evidence: PMID:15040 Cycloheximide prevented the rise in arylsulphatase B activity occurring after oestrogen injection, suggesting a regulation of cervical arylsulphatase B at the level of protein biosynthesis.
GO:0051597 response to methylmercury	IEA GO_REF:0000107	KEEP AS NON CORE	Summary: Retain the methylmercury-associated activity response as non-core. Reason: The original rat CNS study reports dose/time-dependent inhibition of arylsulfatase B following methylmercuric chloride treatment. This can support the broad existing response annotation; no detoxification, mercury binding or protective catalytic mechanism follows from it. Retain as non-core with the rat experimental boundary. Propagation Review Root cause: NO FAILURE NON CORE Sources checked: UniProtKB:P50430 SUPPORTS TRANSFER The rat CNS experiment reports dose/time-dependent Arsb activity inhibition after methylmercuric chloride treatment (PMID1682910), without a detoxification mechanism. ensembl:ENSRNOP00000014860 SUPPORTS TRANSFER This Ensembl identifier accompanies the same rat tissue response inference; it is not additional evidence of mercury binding or protection. Supporting Evidence: PMID:1682910 a dose and duration dependent inhibition of the enzymes in all CNS areas
GO:0003943 N-acetylgalactosamine-4-sulfatase activity	IDA PMID:18285341 Distinct effects of N-acetylgalactosamine-4-sulfatase and ga...	ACCEPT	Summary: Accept the established GalNAc-4-sulfatase activity. Reason: The original human MCF7 study manipulates ASB expression and measures chondroitin sulfate pools. Its complete abstract identifies ASB as GalNAc-4-sulfatase, while independent human enzyme/structure and Reactome reaction evidence corroborate the established function. Accept the IDA assertion without claiming the unread full paper was a purified-substrate assay. Supporting Evidence: PMID:19306108 the enzyme that removes 4-sulfate groups from N-acetylgalactosamine 4-sulfate, which combines with glucuronate to form the disaccharide unit of chondroitin-4-sulfate (C4S). PMID:18285341 Following silencing of ASB or GALNS, total sGAG, C4S, and CS increased significantly. Following overexpression of ASB or GALNS, total sGAG, C4S, and CS declined significantly.
GO:0030207 chondroitin sulfate proteoglycan catabolic process	IDA PMID:18285341 Distinct effects of N-acetylgalactosamine-4-sulfatase and ga...	ACCEPT	Summary: Accept catalytic participation in chondroitin sulfate degradation. Reason: Human MCF7 ASB silencing increases C4S/CS and overexpression lowers them in the original abstract. ARSB itself performs a desulfation step in this catabolic sequence, independently represented in the actual Reactome catalyst graph. This is catalytic participation, not merely being a consumed substrate. Full original 2008 Methods remain unread. Supporting Evidence: PMID:18285341 Following silencing of ASB or GALNS, total sGAG, C4S, and CS increased significantly. Following overexpression of ASB or GALNS, total sGAG, C4S, and CS declined significantly.
GO:0043202 lysosomal lumen	TAS Reactome:R-HSA-2282889	ACCEPT	Summary: Accept the independently corroborated lysosomal-lumen compartment. Reason: This source event models mutant ARSB in lysosomal lumen. Its exact full nested mutant participant set was not reconstructed. The asserted compartment is independently supported by normal human ARSB maturation and the explicitly inspected active ARSB:Ca2+ lysosomal catalyst. Accept the location without assigning the mutant reaction or the ambiguous C6S summary to wild-type ARSB. Supporting Evidence: PMID:2303452 The 47-kDa ASB form was located in dense lysosomes.
GO:0043202 lysosomal lumen	TAS Reactome:R-HSA-9036065	ACCEPT	Summary: Accept lysosomal lumen without adopting ambiguous mutant-reaction wording. Reason: This mutant-ARSB event asserts lysosomal lumen. Its DS title and cached CS wording are inconsistent, and the full nested mutant set remains uninspected; neither issue disproves the broad compartment. Normal human maturation and the inspected ARSB:Ca2+ catalyst independently corroborate lysosomal lumen. No new substrate claim is inferred from this mutant summary. Supporting Evidence: PMID:2303452 The 47-kDa ASB form was located in dense lysosomes.
GO:0005576 extracellular region	TAS Reactome:R-HSA-6798751	KEEP AS NON CORE	Summary: Retain the modeled extracellular granule-cargo pool as non-core. Reason: The actual azurophil-granule release reaction has ARSB in its granule-lumen input and extracellular output participant sets. This supports a modeled released cargo pool, not a catalytic role in degranulation. Keep the extracellular location non-core and distinguish the graph assertion from newly read direct imaging. The local notes quote is an author-derived record of inspecting the linked Reactome participant entities, not an independent publication or additional experimental replicate. Supporting Evidence: file:human/ARSB/ARSB-notes.md contains ARSB in input set R-HSA-6798742 and extracellular output set R-HSA-6806184, including ARSB granule entity R-HSA-6798774.
GO:0005576 extracellular region	TAS Reactome:R-HSA-6800434	KEEP AS NON CORE	Summary: Retain the modeled extracellular ficolin-rich-granule cargo pool as non-core. Reason: The actual ficolin-rich granule release reaction includes ARSB in the granule-lumen and extracellular participant sets. Preserve this modeled extracellular cargo location as non-core; it does not make ARSB a degranulation effector or establish extracellular catalytic turnover. The local notes quote is an author-derived record of inspecting the linked Reactome participant entities, not an independent publication or additional experimental replicate. Supporting Evidence: file:human/ARSB/ARSB-notes.md similarly contains ARSB in input R-HSA-6800431 and output R-HSA-6806481, with granule entity R-HSA-6800887.
GO:0035578 azurophil granule lumen	TAS Reactome:R-HSA-6798751	KEEP AS NON CORE	Summary: Retain the modeled azurophil-granule lumen location as non-core. Reason: The inspected granule participant set R6798742 includes the ARSB azurophil-lumen entity R6798774. This is coherent cargo localization in a secretion model. Keep non-core; lysosomal glycan desulfation remains the established core activity. The local notes quote is an author-derived record of inspecting the linked Reactome participant entities, not an independent publication or additional experimental replicate. Supporting Evidence: file:human/ARSB/ARSB-notes.md contains ARSB in input set R-HSA-6798742 and extracellular output set R-HSA-6806184, including ARSB granule entity R-HSA-6798774.
GO:1904813 ficolin-1-rich granule lumen	TAS Reactome:R-HSA-6800434	KEEP AS NON CORE	Summary: Retain the modeled ficolin-rich-granule lumen location as non-core. Reason: The inspected ficolin-rich granule input set R6800431 includes ARSB entity R6800887. Preserve the modeled cargo compartment as non-core without inferring that ARSB performs granule exocytosis. The local notes quote is an author-derived record of inspecting the linked Reactome participant entities, not an independent publication or additional experimental replicate. Supporting Evidence: file:human/ARSB/ARSB-notes.md similarly contains ARSB in input R-HSA-6800431 and output R-HSA-6806481, with granule entity R-HSA-6800887.
GO:0003943 N-acetylgalactosamine-4-sulfatase activity	IDA PMID:19306108 Arylsulfatase B regulates colonic epithelial cell migration ...	ACCEPT	Summary: Accept GalNAc-4-sulfate hydrolysis supported by the original human study. Reason: The original human colonic epithelial study explicitly describes removal of the GalNAc 4-sulfate group and measures ASB perturbation and C4S content. This agrees with the established enzyme function. Accept the IDA function while preserving the abstract-only limit; downstream MMP9/RhoA effects are not ARSB catalytic activities. Supporting Evidence: PMID:19306108 the enzyme that removes 4-sulfate groups from N-acetylgalactosamine 4-sulfate, which combines with glucuronate to form the disaccharide unit of chondroitin-4-sulfate (C4S).
GO:0009986 cell surface	ISS GO_REF:0000024	UNDECIDED	Summary: The specific transferred cell-surface localization remains unresolved. Reason: The exact rat P50430 experiment underlying this cell-surface ISS annotation has not been inspected. A normal lysosomal/secretory itinerary is compatible with additional pools but does not itself prove a cell-surface localization. Preserve this source assertion unresolved rather than assuming a localization error. The attached UniProt P50429 cell-surface statement is a separate unresolved by-similarity chain; it is not the original P50430 ISS experiment or evidence that the rat donor assay was read. Propagation Review Root cause: UNRESOLVED Sources checked: UniProtKB:P50430 UNRESOLVED P50430 is the original rat ISS source. Its exact surface-localization experiment remains unread; the separate UniProt P50429 statement is not substituted for it. Supporting Evidence: file:human/ARSB/ARSB-uniprot.txt surface {ECO:0000250\|UniProtKB:P50429}.
GO:0010632 regulation of epithelial cell migration	IMP PMID:19306108 Arylsulfatase B regulates colonic epithelial cell migration ...	KEEP AS NON CORE	Summary: Retain the existing epithelial-migration regulation as a non-core consequence. Reason: The original human NCM460/T84 perturbation study reports inverse effects of ARSB expression on migration, MMP9 and activated RhoA. Keep the existing experimental migration-regulation assertion as a contextual consequence of C4S remodeling, not as a separate core motility or RhoA enzyme function. Full Methods remain unavailable; no new process annotation is manufactured. Supporting Evidence: PMID:19306108 Silencing and overexpression of ASB had inverse effects on MMP9, activated RhoA, and cell migration, as well as the C4S content, in the NCM460 and T84 cells.
GO:0010976 positive regulation of neuron projection development	ISS GO_REF:0000024	KEEP AS NON CORE	Summary: Retain the supported neurite-development consequence as non-core. Reason: The traced rat source and recombinant human enzyme rescue in rat coculture support the existing neurite-development inference. The enzyme changes the sulfated extracellular environment in this context; no direct receptor agonism or human neuron assay is established. Retain the source ISS assertion as non-core. Propagation Review Root cause: NO FAILURE NON CORE Sources checked: UniProtKB:P50430 SUPPORTS TRANSFER P50430 supplies the rat coculture transfer source supported by PMID24311516; the consequence remains contextual rather than a growth-factor molecular function. Supporting Evidence: PMID:24311516 Neurite outgrowth of hippocampal pyramidal neurons co-cultured with ARSB-silenced astrocytes was reduced when compared to neurite outgrowth in neurons co-cultured with untreated astrocytes and astrocytes transfected with a non-target siRNA (Fig. 8 A–D)
GO:0061580 colon epithelial cell migration	IMP PMID:19306108 Arylsulfatase B regulates colonic epithelial cell migration ...	KEEP AS NON CORE	Summary: Retain the observed colonic-cell migration effect as non-core. Reason: Human colonic epithelial migration changes after ASB silencing/overexpression are explicitly reported in the cited study. Retain the existing IMP process as non-core because the directly established ARSB work is glycan desulfation, with migration downstream. This judgment does not propose additional migration terms or claim ARSB is a motor. Supporting Evidence: PMID:19306108 Silencing and overexpression of ASB had inverse effects on MMP9, activated RhoA, and cell migration, as well as the C4S content, in the NCM460 and T84 cells.
GO:0070062 extracellular exosome	HDA PMID:23533145 In-depth proteomic analyses of exosomes isolated from expres...	MARK AS OVER ANNOTATED	Summary: Detected in an extracellular-vesicle proteome, but the detection does not establish that this protein is an EV constituent. Reason: Soluble lysosomal sulfatase. Secreted or lumenal protein (UniProt). MISEV2018 (PMID:30637094) category 5 allows such proteins onto EVs through specific or promiscuous (proteoglycan, lipid) receptors on the EV surface, but asks that their identification be backed by evidence of that association. A bulk EV proteome cannot separate surface binding from co-isolation, and this protein's annotations record no experimental proteoglycan, heparin or lipid binding, and its own review keeps no experimental cell-surface or plasma-membrane pool. (Manual re-review for OMICS_EVIDENCE, 2026-10-10; previous action: UNDECIDED.) Supporting Evidence: file:human/ARSB/ARSB-notes.md the exact ARSB supplementary protein/peptide row remains unread.
GO:0005788 endoplasmic reticulum lumen	TAS Reactome:R-HSA-1614362	KEEP AS NON CORE	Summary: Retain ER-lumen maturation cargo localization as non-core. Reason: The actual SUMF1 reaction uses the arylsulfatase substrate set R1614312, including ARSB entity R1614331 in ER lumen. Here SUMF1 performs active-site maturation and ARSB is its cargo/substrate. The ER location is valid but non-core; no SUMF1 oxidoreductase function or ER-catalytic ARSB glycan degradation is inferred. The local notes quote is an author-derived record of inspecting the linked Reactome participant entities, not an independent publication or additional experimental replicate. Supporting Evidence: file:human/ARSB/ARSB-notes.md has ARSB in its ER-lumen substrate set R-HSA-1614312 through entity R-HSA-1614331.
GO:0043202 lysosomal lumen	TAS Reactome:R-HSA-1606789	ACCEPT	Summary: Accept the lysosomal-lumen site of human ARSB-catalyzed DS desulfation. Reason: The inspected DS reaction R1606789 uses lysosomal ARSB:Ca2+ complex R1606792 with OxA-ARSB component R1606837 linked to human P15848/HGNC714. The input/output graph places the sulfate-removal catalyst in lysosomal lumen. Accept this core compartment. Supporting Evidence: PMID:2303452 The 47-kDa ASB form was located in dense lysosomes. Reactome:R-HSA-1606789 Arylsulfatase B (ARSB) hydrolyses sulfate from N-acetylgalactosamine 4-sulfate units within dermatan sulfate (DS; Gorham & Cantz 1978).
GO:0043202 lysosomal lumen	TAS Reactome:R-HSA-1793207	ACCEPT	Summary: Accept the lysosomal-lumen catalyst location in CS degradation. Reason: The inspected CS reaction R1793207 uses the same human ARSB:Ca2+ lysosomal catalyst. Its cached C4S/C6S wording is broader than the established 4-sulfatase specificity and is not propagated into the review. That substrate ambiguity does not undermine the existing lysosomal-lumen assertion. Supporting Evidence: PMID:19306108 the enzyme that removes 4-sulfate groups from N-acetylgalactosamine 4-sulfate, which combines with glucuronate to form the disaccharide unit of chondroitin-4-sulfate (C4S). PMID:2303452 The 47-kDa ASB form was located in dense lysosomes.
GO:0004065 arylsulfatase activity	TAS PMID:2303452 Phylogenetic conservation of arylsulfatases. cDNA cloning an...	KEEP AS NON CORE	Summary: Retain the existing arylsulfatase assay activity as non-core. Reason: The original human ASB expression paper reports elevated arylsulfatase activity, and the historical activity class encompasses aromatic assay substrates. Keep the existing arylsulfatase function non-core; distinguish it from the physiological GalNAc-4-sulfatase reaction. Full original assay Methods were not recovered, so no uninspected reagent or kinetic specificity is invented. Supporting Evidence: PMID:2303452 Overexpression of ASB in transfected baby hamster kidney (BHK) cells resulted in up to 68-fold higher ASB activity than in untransfected BHK cells. PMID:8037 incubating the gels with p-nitrocatechol sulphate as substrate
GO:0005764 lysosome	TAS PMID:2303452 Phylogenetic conservation of arylsulfatases. cDNA cloning an...	ACCEPT	Summary: Accept the lysosomal location of the human protein. Reason: The original abstract explicitly places processed human ASB in dense lysosomes after expression in BHK cells, and the independent human Reactome reaction locates active ARSB in lysosomal lumen. Preserve the human-protein/hamster-expression-system distinction. Supporting Evidence: PMID:2303452 The 47-kDa ASB form was located in dense lysosomes.
GO:0007040 lysosome organization	TAS PMID:1718978 Mucopolysaccharidosis VI (Maroteaux-Lamy syndrome). An inter...	UNDECIDED	Summary: The source-specific lysosome-organization assertion remains unresolved. Reason: GO0007040 covers lysosome assembly, arrangement or disassembly. The original G137V paper examines human patient fibroblasts and heterologous precursor stability, processing and transport. The complete abstract and selected original Methods/Results were read, but a complete source adjudication for the broader lysosome-organization assertion was not achieved. Retain UNDECIDED, not an assertion that no such experiment exists in the full paper. Supporting Evidence: PMID:1718978 The G137V mutation did not affect the synthesis but severely reduced the stability of the arylsulfatase B precursor.
GO:0007041 lysosomal transport	TAS PMID:2303452 Phylogenetic conservation of arylsulfatases. cDNA cloning an...	MARK AS OVER ANNOTATED	Summary: The cited transport observation establishes ARSB as lysosomal cargo. Reason: The complete PMID2303452 abstract explicitly attributes delivery of human ARSB to the mannose-6-phosphate receptor. In that demonstrated transport step ARSB is the cargo, while the receptor-dependent trafficking machinery performs the directed movement named by GO0007041. Mark the existing TAS process assertion as over-annotated because interpreting this cargo observation as ARSB participation conflates those roles. This is a bounded judgment about the cited observation, not a claim that ARSB can never influence trafficking or that all experiments in the unread full paper have been excluded. The independently supported lysosomal location remains accepted. Supporting Evidence: PMID:2303452 Transport of ASB to the lysosomes was accomplished in a mannose 6-phosphate receptor-dependent manner.
GO:0030209 dermatan sulfate proteoglycan catabolic process	TAS Reactome:R-HSA-1606789	NEW	Summary: Retain the proposal for ARSB-catalyzed dermatan sulfate degradation. Reason: Retain the already-authored proposal for dermatan sulfate catabolism. The actual R1606789 graph names human ARSB:Ca2+ as the enzyme performing GalNAc-4-sulfate hydrolysis, with explicit DS input and desulfated output. Comparator IDUA has human GO0030209 IDA PMID24036510 in MGI, and human IDS is explicitly the catalyst of GO0030209-linked R1793182; these are enzymes performing steps, not consumed substrates. The inspected term parents are proteoglycan catabolism and dermatan sulfate proteoglycan metabolism in the indexed ontology view. No existing original GOA row supplies the DS process. No target match was found in the local GO-CAM index. Supporting Evidence: Reactome:R-HSA-1606789 Arylsulfatase B (ARSB) hydrolyses sulfate from N-acetylgalactosamine 4-sulfate units within dermatan sulfate (DS; Gorham & Cantz 1978).

Gene Description

Existing Annotations Review

Core Functions

Catalyses removal of 4-sulfate groups from N-acetylgalactosamine residues during lysosomal chondroitin sulfate and dermatan sulfate degradation, using a calcium-containing, formylglycine-dependent active site.

References

Suggested Questions for Experts

Deep Research

Cyberian

Falcon

Perplexity

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Notes

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