rgn (M9PFV8): evidence and ProtNLM claim review

Regeneration is a secretory-pathway C-type-lectin-domain protein implicated in imaginal-disc regeneration. Genetic perturbation affects blastema formation and growth, while its ligand specificity and the relationship between the 808-residue isoform and its inferred trans-Golgi localization remain unresolved.

Exact input: M9PFV8, 808 residues. The accession was fetched explicitly with the gene-directory alias; no canonical-sequence substitution is made.

Raw emitted predictions: rgn-predictions-source.json. Source features: rgn-uniprot.txt, with an exact extraction in rgn-sequence-evidence.json.

Sequence and domain evidence

These are sequence/domain observations or explicitly named feature predictions, not measurements of biological function. ARBA assertions and ProtNLM-derived UniProt names are not counted as validation.

DR   InterPro; IPR001304; C-type_lectin-like.
DR   InterPro; IPR016186; C-type_lectin-like/link_sf.
DR   InterPro; IPR016187; CTDL_fold.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   DOMAIN          70..199
FT                   /note="C-type lectin"
FT                   /evidence="ECO:0000259|PROSITE:PS50041"

ProtNLM claims

The snapshot emits names and location/keyword statements, with no GO or EC prediction for this target. Each actual statement is assessed below; no GO term has been substituted for it. Categories follow the function-prediction rubric, with nonspecific “uncharacterized” names marked UNC because they contain no testable function. CNN records an independently supported existing annotation; it does not assert a particular training-set composition.

Kind Verbatim emitted statement Assessment Evidence and limitation
Name C-type lectin domain-containing protein CNN PROSITE identifies a C-type lectin-like domain at residues 70-199; PMID:18485344 independently describes the signal sequence and CTLD in Rgn. The domain claim is supported without assigning carbohydrate specificity.
Location Secreted (SL-0243) UNC The signal peptide and lectin domain make secretion plausible, and PMID:18485344 independently discusses this architecture. However, the exact long isoform has curated trans-Golgi/vesicle assertions and no direct secretion assay; secretory-pathway entry does not establish release as a soluble extracellular protein.

Literature evidence

Annotation decisions

Research provenance

Genuine external literature research is requested through the repository Falcon wrapper, with perplexity-lite configured as fallback. Provider output is retained separately as rgn-deep-research-<provider>.md; its source leads are checked against the underlying publications and exact sequence record.