family_id: PANTHER:PTHR45751
family_name: COPINE FAMILY PROTEIN 1
preferred_name: Plant RGLG ubiquitin ligases and copine-related proteins
summary: The retrieved group includes RGLG RING-type ubiquitin ligases and proteins carrying copine-related
  names. Ligase activity depends on the RING-containing architecture and its E2 partner; membrane association
  and substrate choice differ among paralogs.
functional_coherence: HETEROGENEOUS
coherence_reason: Rice Q6YYC5 has an annotated RING domain and RGLG4 placement. Experiments establish
  ligase activity for RGLG3/RGLG4, supporting that bounded inference. K63-chain formation is a narrower
  E2/E3-dependent reaction and cannot follow merely from general ubiquitin-ligase activity.
subfamilies:
- subfamily_id: PANTHER:PTHR45751:SF16
  label: E3 UBIQUITIN-PROTEIN LIGASE RGLG4
  description: Recorded placement of Q6YYC5. Rice Q6YYC5 has an annotated RING domain and RGLG4 placement.
    Experiments establish ligase activity for RGLG3/RGLG4, supporting that bounded inference. K63-chain
    formation is a narrower E2/E3-dependent reaction and cannot follow merely from general ubiquitin-ligase
    activity.
  representative_members:
  - id: UniProtKB:Q6YYC5
    gene_symbol: Q6YYC5
    organism: Oryza sativa subsp. japonica
    gene_review: genes/ORYSJ/Q6YYC5/Q6YYC5-ai-review.yaml
term_assessments:
- assessed_term:
    id: GO:0070534
    label: protein K63-linked ubiquitination
  scope: UNRESOLVED
  scope_reason: RGLG3 and RGLG4 have demonstrated ubiquitin ligase activity, but the cited activity assay
    does not establish K63 linkage specificity. Linkage choice depends on the E2/E3 combination and chain-extension
    mechanism, not the RING motif alone. K63 transfer to rice or across the family requires an actual
    linkage assay or an experimentally anchored isofunctional branch.
  supported_by:
  - reference_id: PMID:22898498
    supporting_text: "Both RGLG3 and \nRGLG4 possessed ubiquitin ligase activities"
  - reference_id: file:genes/ORYSJ/Q6YYC5/Q6YYC5-uniprot.txt
    supporting_text: DR   InterPro; IPR001841; Znf_RING.
  - reference_id: file:genes/ORYSJ/Q6YYC5/Q6YYC5-uniprot.txt
    supporting_text: FT   DOMAIN          356..389
  - reference_id: file:genes/ORYSJ/Q6YYC5/Q6YYC5-uniprot.txt
    supporting_text: FT                   /note="RING-type"
- assessed_term:
    id: GO:0061630
    label: ubiquitin protein ligase activity
  scope: UNRESOLVED
  scope_reason: Both Arabidopsis RGLG3 and RGLG4 provide direct positive E3 evidence, and the rice RING
    domain is compatible with that reaction. The family also contains proteins with different domain combinations,
    so a copine-like name or shared interaction domain is not sufficient. Retention of the functional
    RING/E2 interface and the complete catalytic branch boundary remain unresolved.
  supported_by:
  - reference_id: PMID:22898498
    supporting_text: "Both RGLG3 and \nRGLG4 possessed ubiquitin ligase activities"
  - reference_id: file:genes/ORYSJ/Q6YYC5/Q6YYC5-uniprot.txt
    supporting_text: DR   InterPro; IPR001841; Znf_RING.
  - reference_id: file:genes/ORYSJ/Q6YYC5/Q6YYC5-uniprot.txt
    supporting_text: FT   DOMAIN          356..389
  - reference_id: file:genes/ORYSJ/Q6YYC5/Q6YYC5-uniprot.txt
    supporting_text: FT                   /note="RING-type"
references:
- id: PMID:22898498
  title: Two novel RING-type ubiquitin ligases, RGLG3 and RGLG4, are essential for jasmonate-mediated
    responses in Arabidopsis.
- id: file:genes/ORYSJ/Q6YYC5/Q6YYC5-uniprot.txt
- id: file:interpro/panther/PTHR45751/PTHR45751-entries.csv
- id: file:interpro/panther/PTHR45751/PTHR45751-paint.tsv
review_status: COMPLETE
reviewed_by: codex
review_date: '2026-09-10'
notes: 'ORYSJ/Q6YYC5: requested accession Q6YYC5; current record Q6YYC5; sequence length 401; source cohort
  ARGO50. Family boundaries were assessed using the fetched member set and the cited domain, literature
  and analytical evidence. Gene-review verdicts and ARBA assertions are not independent validation. PANTHER
  subfamily labels and membership are recorded from the frozen UniProt records and panther.obo; they do
  not by themselves prove functional uniformity within a subfamily. PAINT rows were inspected as ancestral
  assertions, but node placement is not adjudicated without the relevant descendant tree/alignment. No
  residue requirement is encoded without a verified sequence-version anchor. A target-level refutation
  is not a family-wide NOT_APPLICABLE judgment. Exact protein-name-only predictions are treated as family-identification
  hypotheses rather than invented GO predictions.'