Human FUCA1 (P04066; HGNC:4006) is a 466-residue tissue alpha-L-fucosidase. Its 31-residue signal peptide and mature chain are processing features. The common Arg281/Gln281 alleles and experimental residues 6–466 construct are not alternate splice products.
PMID:19666478(https://pubmed.ncbi.nlm.nih.gov/19666478/) explicitly characterizes human FUCA1 alongside FUCA2. Its infection-associated secretion and adhesion conclusions concern FUCA2. PMID:4074382(https://pubmed.ncbi.nlm.nih.gov/4074382/) supplies human fibroblast activity/processing evidence through the accessible abstract; it does not establish a cytosolic enzyme.
PMID:9741689(https://pubmed.ncbi.nlm.nih.gov/9741689/) separates bovine kidney purified-enzyme assays from human fibroblast glycolipid turnover. The existing ISS donor Q2KIM0 is bovine FUCA1 and has an IDA annotation to this paper. NAGA acts before efficient defucosylation of the tested linear intermediate. FUCA1 is not described as efficiently hydrolysing every branched blood-group substrate.
PMID:27491075(https://pubmed.ncbi.nlm.nih.gov/27491075/) is a mouse knockout study. Its storage data support conserved core-defucosylation biology; AGA steric inhibition is cited background. The inherited human IMP/NEW row is archived rather than repeated as a human experiment. A separate IC annotation now infers human process participation from established catalytic activity and the explicit human lysosomal reaction; the mouse study remains corroboration rather than a human IMP experiment. Comparator queries found human MAN2B1 and GLB1 annotations to this process; FUCA1 catalyses a step rather than merely being a substrate. No local GO-CAM index hit was found for P04066/FUCA1.
All three IBA rows follow the actual PTHR10030 AN0/PTN000003123 ancestor to human AN252/PTN002467369, whose sequence exactly matches P04066. Self-donor evidence is legitimate grounding. A fly NOT/IRD is outside that path; two other-species sequence discrepancies are retained explicitly. No human loss is inferred from them.
Fucose metabolism reaches carbohydrate metabolism through hexose and monosaccharide metabolism, all by is_a. The broad carbohydrate metabolic process annotation (GO:0005975; IEA; GO_REF:0000002) is TOO_GENERAL; its former glycoprotein replacement is not retained. The verified lysosomal lumen part_of lysosome relation preserves both claims: the root-organelle policy retains lysosome as informative even when lumen is known. The longer path to cytoplasm contains part_of and supports the separate cytoplasm TOO_GENERAL judgment. Glycoprotein, glycoside and glycolipid catabolism are not treated as ancestors of one another.
The exact HuRI records support three CIB1, three MED10 and five UBQLN2 two-hybrid records using FUCA1 residues 6–466. Positive assay associations remain non-core; no native lysosomal complex or orthogonal mammalian validation is inferred.
The original lysosomal reaction identifies FUCA1 tetramer as catalyst. The granule event contains exact human P04066 input/output members, distinct from FUCA2. These establish modeled cargo locations, not an exocytosis role. Human lymphoid-cell secretion in PMID:1873910(https://pubmed.ncbi.nlm.nih.gov/1873910/) remains culture-specific.
Original PMID:19056867(https://pubmed.ncbi.nlm.nih.gov/19056867/) Table 1 lists FUCA1 with Pep 1 and ID 1. Retain its original urine extension and non-core detection. The recovered original supplementary Table 2 of PMID:23533145(https://pubmed.ncbi.nlm.nih.gov/23533145/) identifies P04066/FUCA1 at row 197 of SI Table 2, separate from FUCA2, with five unique peptides in each of four analysis columns. These are duplicate analyses of two pooled clinical groups. Retain the existing EPS-urine exosome annotation as non-core preparation-level detection. The article's soluble-protein/contaminant caveat limits interpretation: cell of origin, vesicle topology, disease-specific expression and a role in exosome biogenesis are not established. The exact workbook was recovered through the official BioStudies article record; its target cells and headers were independently replayed.
The inherited review has 26 rows: 25 current machine contexts and one authored NEW assertion. All 29 original quotation associations remain in the complete inherited archive. The active projection keeps inherited quotation text attached to the same annotation or core; the retired row's three associations remain historical. No new quotation is authored. The one current NEW annotation is a separately justified IC inference; the former human IMP assertion remains historical. Source files, existing history and GOA remain immutable. Genuine native acquisition preserved these source bytes. Current review decisions and archived prior assertions are distinguished in the evidence map; validation and history outcomes are recorded in the notes.
The existing review was preserved during native acquisition. Its 25-row GOA snapshot, UniProt record, 14 existing sources and provider artifacts were unchanged. The missing four-row PAINT slice was obtained from retained source caches; all three incoming IBD assertions match the inspected target lineage. The evidence map archives the inherited 26-row review, all 16 GOA columns and the actual mapping to 25 reviewed original contexts. The retired authored row and its three quotation associations remain historical; 26 original quotation associations remain active. The original urine extension is restored. Fresh QuickGO requests add only the requested synonym metadata, with both dated and current original objects retained. Actual validation and history outcomes are recorded in the notes.
The glycoprotein-catabolism IC proposal infers participation from human alpha-L-fucosidase activity (GO:0004560) in lysosomal lumen (GO:0043202), with the explicit human Reactome catalyst/substrate reaction. FUCA1 performs the hydrolysis itself. Human biochemical and patient-cell evidence establish enzyme identity; mouse knockout storage provides separate corroboration. The inference does not assert that those human papers directly measured glycoprotein turnover. MAN2B1 and GLB1 are positive same-role comparators, including a MAN2B1 IC annotation from glycosidase activity. Official ancestry shows no redundant parent/child relationship to the existing fucose, glycoside or glycolipid process annotations. The local GO-CAM index has no FUCA1 entry. Core defucosylation permits subsequent AGA cleavage; the mouse paper cites that biochemical mechanism as prior work.
The normal caches for PMID:9741689 and PMID:19056867 are abstract-only; their indicated original sections/tables were accessible and read. The PMID:23533145 cache contains XML-extracted main text, while its supplementary workbook was independently recovered. These reference assessments concern the specific supporting claims below, not uninspected sections:
The public evidence map contains the literal urine scope at original_contexts[23].extensions for QuickGO annotation UniProtKB:P04066!58678521: part_of UBERON:0001088. Its normalized form is in machine_contexts.restored_extensions. The 16-column GOA export does not encode extension fields. current_reviewed_contexts and machine_contexts.actual_mapping describe the 25 original contexts; current_authored_annotations holds the new IC row. inherited_review, retired_authored_annotations and quotation_conservation retain the original provenance, including all 29 quotation associations (26 active and three historical).
The reviewed amendment passed default validation, strict GOA reconciliation, native history validation and the status audit. Status remains DRAFT with four advisories: three deliberate generic-binding contexts and the unused inherited research file. The original sources and quotation ledger remain unchanged.