id: Q18287
gene_symbol: C28G1.2
taxon:
  id: NCBITaxon:6239
  label: Caenorhabditis elegans
status: COMPLETE
description: 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
references:
- id: GO_REF:0000033
  title: Annotation inferences using phylogenetic trees
  findings: []
- id: PMID:10373004
  title: Serpins in the Caenorhabditis elegans genome.
  findings:
  - statement: Primary comparative sequence analysis documents unusual nematode serpin architectures.
      The available abstract does not identify C28G1.2 specifically or demonstrate its function.
    supporting_text: 'Some appear

      complete, some show extensive deletions, and others appear to contain only the

      C-terminal part of the known serpin fold'
  full_text_unavailable: true
  reference_review:
    relevance: HIGH
    correctness: VERIFIED
    review_notes: Primary report checked against the cached abstract/full text; the evidence scope is
      stated in the finding.
- id: file:worm/C28G1.2/C28G1.2-uniprot.txt
  title: UniProt sequence and serpin-domain annotation for Q18287
- id: file:worm/C28G1.2/C28G1.2-prediction-donor.json
  title: UniProt identification of the collagen-chaperone donor
- id: file:worm/C28G1.2/C28G1.2-protnlm-source.json
  title: Frozen exact-input ProtNLM output and UniProt sequence for Q18287
predictions:
- source_method: ProtNLM2
  source_version: UniProt API snapshot 2026-09-10
  source_reference_id: file:worm/C28G1.2/C28G1.2-protnlm-source.json
  predicted_term:
    id: GO:0010466
    label: negative regulation of peptidase activity
  predicted_term_type: GO_BP
  review:
    assessment: UNC
    confidence_score: 1
    summary: 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.
    supported_by:
    - &id001
      reference_id: file:worm/C28G1.2/C28G1.2-uniprot.txt
      supporting_text: DOMAIN          96..199
    - &id002
      reference_id: PMID:10373004
      supporting_text: 'Some appear

        complete, some show extensive deletions, and others appear to contain only the

        C-terminal part of the known serpin fold'
- source_method: ProtNLM2
  source_version: UniProt API snapshot 2026-09-10
  source_reference_id: file:worm/C28G1.2/C28G1.2-protnlm-source.json
  predicted_term:
    id: GO:0004867
    label: serine-type endopeptidase inhibitor activity
  predicted_term_type: GO_MF
  review:
    assessment: UNC
    confidence_score: 1
    summary: 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.
    supported_by:
    - *id001
    - *id002