id: A0A8C4M6Z6
gene_symbol: TGFBR3
taxon:
  id: NCBITaxon:9793
  label: Equus asinus
status: COMPLETE
description: Assessment of the single ProtNLM2 GO prediction for donkey TGFBR3 (A0A8C4M6Z6, betaglycan),
  89.5% identical to human TGFBR3. Extracellular region is correct, reflecting the shed soluble ectodomain,
  and is absent from donkey GOA (COR). ProtNLM2 also emitted subcellular locations Extracellular matrix,
  Secreted and Extracellular space (not scored); these match the soluble form, but the output omits the
  primary cell-membrane (single-pass type I) location. No function text was emitted.
source_documents:
- projects/PROTNLM_EVALUATION/donkey40/donkey40-predictions.tsv
- genes/EQUAS/TGFBR3/TGFBR3-goa.tsv
- genes/EQUAS/TGFBR3/TGFBR3-bioinformatics/human-Q03167-uniprot.txt
- genes/EQUAS/TGFBR3/TGFBR3-bioinformatics/RESULTS.md
predictions:
- source_method: ProtNLM2
  source_version: UniProt API snapshot 2026-10-14
  predicted_term:
    id: GO:0005576
    label: extracellular region
  predicted_term_type: GO_CC
  review:
    assessment: COR
    confidence_score: 2
    summary: Betaglycan exists both as a membrane-bound receptor and as a soluble form in serum and extracellular
      matrix; the soluble ectodomain is released by proteolytic shedding mediated by MT1-MMP (PMID:14672946),
      and the human gene review keeps extracellular region as a non-core location. The
      donkey protein conserves the signal peptide, ZP domain and transmembrane helix, so the same membrane-bound
      and shed forms are expected. The donkey GOA has plasma membrane and external side of plasma membrane
      but not extracellular region, so the prediction adds a correct location. It is a secondary location;
      the primary site of receptor function is the plasma membrane.
    supported_by:
    - reference_id: file:EQUAS/TGFBR3/TGFBR3-bioinformatics/human-Q03167-uniprot.txt
      supporting_text: as a membrane-bound form and as soluble form in serum and in the
    - reference_id: PMID:14672946
      supporting_text: A soluble form of betaglycan can be released by proteolytic cleavage (also known
        as shedding) of the membrane-bound form, yielding soluble betaglycan.
    - reference_id: file:EQUAS/TGFBR3/TGFBR3-bioinformatics/RESULTS.md
      supporting_text: 'TRANSMEM Helical: human [788, 809] MY -> donkey [773, 794] MY'
references:
- id: file:EQUAS/TGFBR3/TGFBR3-bioinformatics/human-Q03167-uniprot.txt
  title: UniProt record for human TGFBR3 (Q03167)
  findings: []
- id: file:EQUAS/TGFBR3/TGFBR3-bioinformatics/RESULTS.md
  title: 'TGFBR3: donkey-human sequence comparison'
  findings: []
- id: PMID:14672946
  title: The shedding of betaglycan is regulated by pervanadate and mediated by membrane type matrix metalloprotease-1.
  findings: []