GLT8D1 is a Golgi-associated type-II membrane glycosyltransferase. A purified human catalytic-domain construct transfers galactose in vitro; its efficient physiological substrates remain unknown. Its donor and acceptor specificity may depend on molecular context. The natural short splice product has not been functionally resolved.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0000139 Golgi membrane | EXP PMID:34746377 Genetic and Functional Analysis of Glycosyltransferase 8 Dom... | ACCEPT | Reason: Full-length FLAG-tagged human WT GLT8D1 colocalized with a Golgi marker in transfected HEK293T cells; I290M instead accumulated in the ER. This supports the curated Golgi placement, with membrane association corroborated by the predicted UniProt signal anchor. Microscopy does not resolve bilayer topology, and the result is not generalized to every isoform or variant (PMID:34746377). Supporting Evidence: PMID:34746377 WT or the R92C variant protein signals overlapped largely with the Golgi marker |
| GO:0000139 Golgi membrane | IEA GO_REF:0000044 | ACCEPT | Reason: The UniProt SL-0134 mapping agrees with WT human Golgi localization and the predicted N-terminal signal anchor. Retain Golgi membrane without treating microscopy as direct bilayer-topology measurement or generalizing to the short isoform. |
| GO:0005794 Golgi apparatus | IBA GO_REF:0000033 | ACCEPT | Reason: PAINT assigns Golgi apparatus activity to eukaryotic AN1/PTN001012071; the target descends from this node. The human entry is legitimately among the experimental descendants used by the curator, alongside mapped Arabidopsis GATL proteins with Golgi IDA records. This supports conserved Golgi activity and agrees with direct GLT8D1 localization; keep the incoming is_active_in qualifier distinct from located_in membrane annotations. |
| GO:0016020 membrane | HDA PMID:19946888 Defining the membrane proteome of NK cells. | TOO GENERAL | Reason: Golgi membrane (GO:0000139), independently supported elsewhere in this review, entails membrane. Mark this broad term TOO_GENERAL. The YTS proteomics target table and peptides remain inaccessible; this disposition does not verify the original HDA identification, plasma-membrane residence or isoform specificity (PMID:19946888). Supporting Evidence: |
| GO:0016757 glycosyltransferase activity | IEA GO_REF:0000002 | MODIFY | Reason: Refine to UDP-galactosyltransferase activity: human 52β371 transferred galactose from UDP-galactose in LCβMS/MS assays. Native substrates, linkage and natural short-isoform function remain unresolved. Proposed replacements: UDP-galactosyltransferase activity Supporting Evidence: PMID:38066107 GLT8D1 displayed glycosyltransferase activity from UDP-galactose onto N-acetylgalactosamine file:human/GLT8D1/GLT8D1-uniprot.txt UDP-galactose onto GalNAc and GlcNAc structures. |
| GO:0046527 glucosyltransferase activity | IBA GO_REF:0000033 | KEEP AS NON CORE | Reason: PAINT places the positive glucosyltransferase assertion at PTHR13778 AN0/PTN004435860, ancestral to human AN57/PTN002492649. Its experimentally grounded donors are bacterial LPS enzymes P19817 (Salmonella waaJ), P27128 (E. coli waaO) and P27129 (E. coli waaJ). The separate bacteria-restricted LPS-process assertion does not taxonomically restrict this ancestral molecular function. Full-length UDP-glucose assays measure UDP release without a defined acceptor or identified glucosylated product (PMID:35198895). Soluble human 52β371 did not hydrolyze UDP-glucose; the panel measured hydrolysis, not glucose transfer (PMID:38066107). Retain this ancestral annotation as a non-core additional specificity. |
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Download this section (compressed HTML)Q: Which endogenous donor and acceptor define GLT8D1 activity, and does the natural Q68CQ7-2 splice product retain catalytic function?
Experiment: Compare full-length Q68CQ7-1 and Q68CQ7-2 in membrane-compatible assays with candidate native acceptors and direct product identification.
Hypothesis: Construct context and acceptor structure may distinguish native activity from low-efficiency screening reactions.
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