ProtNLM2 External predictions
View prediction review YAML · C28G1.2-protnlm-predictions-review.yaml · Review status: COMPLETE
Serpin structural similarity does not resolve whether C28G1.2 is inhibitory, noninhibitory or collagen-associated. Both emitted inhibitory GO claims remain biologically unverified.
Source documents: genes/worm/C28G1.2/C28G1.2-protnlm-source.json · genes/worm/C28G1.2/C28G1.2-notes.md
Review score: 2 = concordant with evidence; 1 = uncertain; 0 = discordant with evidence. This is an assessment score, not a model probability.
UNC — Uncertain Review score: 1/2
Prediction method: ProtNLM2 · Version: UniProt API snapshot 2026-09-10 · file:worm/C28G1.2/C28G1.2-protnlm-source.json
Review rationale: The serpin fold includes inhibitory and noninhibitory proteins. Neither a target protease nor inhibitory activity is established for C28G1.2, and the compact nematode architecture makes a generic structural match insufficient to transfer an inhibitory process. The available evidence also does not demonstrate loss of every possible inhibitory function.
Supporting Evidence:
- file:worm/C28G1.2/C28G1.2-uniprot.txt: "DOMAIN 96..199"
- PMID:10373004: "Some appear complete, some show extensive deletions, and others appear to contain only the C-terminal part of the known serpin fold"
UNC — Uncertain Review score: 1/2
Prediction method: ProtNLM2 · Version: UniProt API snapshot 2026-09-10 · file:worm/C28G1.2/C28G1.2-protnlm-source.json
Review rationale: No C28G1.2 inhibition experiment, protease specificity or validated inhibitory reactive-center-loop mechanism was found. A high-confidence structural match to a serpin donor is not an assay of this activity, particularly for a compact and divergent sequence. This is unresolved rather than a proven noninhibitory serpin.
Supporting Evidence:
- file:worm/C28G1.2/C28G1.2-uniprot.txt: "DOMAIN 96..199"
- PMID:10373004: "Some appear complete, some show extensive deletions, and others appear to contain only the C-terminal part of the known serpin fold"