Tout-velu is an exostosin-family glycosyltransferase associated with heparan-sulfate synthesis. The native 299-residue PC isoform retains the C-terminal glycosyltransferase region but lacks the N-terminal membrane anchor and the other glycosyltransferase domain found in full-length Ttv. Its catalytic competence, intracellular targeting and contribution to glycan synthesis remain unresolved.
Summary: The source protein is a C-terminal isoform lacking the N-terminal membrane anchor of full-length Ttv.
Reason: The source protein is a C-terminal isoform lacking the N-terminal membrane anchor of full-length Ttv. It might associate with membranes through other proteins, but this has not been demonstrated. The full-length membrane annotation does not independently establish ER-membrane residence for PC; the correct compartment remains unresolved.
Supporting Evidence:
file:DROME/ttv/ttv-bioinformatics/RESULTS.md
The C-terminal glycosyltransferase-region active-site Asp670 maps to target Asp209, and the source-record nucleotide-sugar/metal-binding residues in this region are retained.
Summary: The native short PC product retains a C-terminal glycosyltransferase region but lacks the N-terminal region needed for the full-length domain architecture and membrane targeting.
Reason: The native short PC product retains a C-terminal glycosyltransferase region but lacks the N-terminal region needed for the full-length domain architecture and membrane targeting. Catalytic potential remains plausible, but no exact-isoform assay establishes native activity, trafficking or participation in glycan synthesis. Keep this annotation undecided rather than transfer all full-length Ttv properties.
Supporting Evidence:
file:DROME/ttv/ttv-bioinformatics/RESULTS.md
The C-terminal glycosyltransferase-region active-site Asp670 maps to target Asp209, and the source-record nucleotide-sugar/metal-binding residues in this region are retained.
Summary: The source protein is a C-terminal isoform lacking the N-terminal membrane anchor of full-length Ttv.
Reason: The source protein is a C-terminal isoform lacking the N-terminal membrane anchor of full-length Ttv. It might associate with membranes through other proteins, but this has not been demonstrated. The full-length membrane annotation does not independently establish ER-membrane residence for PC; the correct compartment remains unresolved.
Supporting Evidence:
file:DROME/ttv/ttv-bioinformatics/RESULTS.md
The C-terminal glycosyltransferase-region active-site Asp670 maps to target Asp209, and the source-record nucleotide-sugar/metal-binding residues in this region are retained.
Summary: The native short PC product retains a C-terminal glycosyltransferase region but lacks the N-terminal region needed for the full-length domain architecture and membrane targeting.
Reason: The native short PC product retains a C-terminal glycosyltransferase region but lacks the N-terminal region needed for the full-length domain architecture and membrane targeting. Catalytic potential remains plausible, but no exact-isoform assay establishes native activity, trafficking or participation in glycan synthesis. Keep this annotation undecided rather than transfer all full-length Ttv properties.
Supporting Evidence:
file:DROME/ttv/ttv-bioinformatics/RESULTS.md
The C-terminal glycosyltransferase-region active-site Asp670 maps to target Asp209, and the source-record nucleotide-sugar/metal-binding residues in this region are retained.
EXT1 and EXT2, where each protein monomer contains distinct GT47 (GT-B fold) and GT64 (GT-A fold) glycosyltransferase domains.
GO:1901135 carbohydrate derivative metabolic process
IEA GO_REF:0000117
UNDECIDED
Summary: The native short PC product retains a C-terminal glycosyltransferase region but lacks the N-terminal region needed for the full-length domain architecture and membrane targeting.
Reason: The native short PC product retains a C-terminal glycosyltransferase region but lacks the N-terminal region needed for the full-length domain architecture and membrane targeting. Catalytic potential remains plausible, but no exact-isoform assay establishes native activity, trafficking or participation in glycan synthesis. Keep this annotation undecided rather than transfer all full-length Ttv properties.
Supporting Evidence:
file:DROME/ttv/ttv-bioinformatics/RESULTS.md
The C-terminal glycosyltransferase-region active-site Asp670 maps to target Asp209, and the source-record nucleotide-sugar/metal-binding residues in this region are retained.
These computational predictions are reviewed separately from the GOA annotation set used for this review. The assessments below are from this project and do not constitute official GO annotations or endorsement by GO/UniProt. They are not included in the existing annotation review above.
The native short Ttv isoform retains a conserved C-terminal GT64 glycosyltransferase domain, but its autonomous activity and physiological access to substrates are unverified.
Review rationale: D5SHU8 is the 299-residue ttv-PC isoform, not the full-length 760-residue protein. The retained C-terminal region contains the annotated catalytic Asp and multiple ligand-binding residues, so short length does not justify categorical refutation of glycosyltransferase activity. However, the other domain and N-terminal targeting/anchor region are absent, and the current data do not establish folding, complex support or substrate access in PC. An equivalent electronic annotation exists but adds no independent validation. OpenScientist found the broad parent term defensible by homology but still cautioned that catalytic evidence is from full-length Ttv, not isolated D5SHU8. Target-specific activity or a convincing domain-level functional analysis is missing; UNC preserves this distinction.
Supporting Evidence:
file:DROME/ttv/ttv-bioinformatics/RESULTS.md: "The C-terminal glycosyltransferase-region active-site Asp670 maps to target Asp209, and the source-record nucleotide-sugar/metal-binding residues in this region are retained."