id: A0A3B6GK97
gene_symbol: A0A3B6GK97
taxon:
  id: NCBITaxon:4565
  label: Triticum aestivum
status: COMPLETE
description: >-
  The deposited patatin-like sequence lacks the catalytic serine region. Intrinsic lipase activity is
  contradicted for this sequence, and participation in lipid catabolism is unresolved.
source_documents:
  - genes/WHEAT/A0A3B6GK97/A0A3B6GK97-uniprot.txt
  - genes/WHEAT/A0A3B6GK97/A0A3B6GK97-goa.tsv
  - publications/PMID_12779324.md
  - genes/WHEAT/A0A3B6GK97/A0A3B6GK97-bioinformatics/RESULTS.md
predictions:
  - source_method: ProtNLM2
    source_version: UniProt 2024_06 pilot
    predicted_term:
      id: GO:0016298
      label: lipase activity
    predicted_term_type: GO_MF
    review:
      assessment: NPI
      error_type: DOMAIN_ARCHITECTURE_MISMATCH
      confidence_score: 0
      summary: >-
        The existing reproducible sequence alignment and motif scan place this protein with plant patatins
        but show a missing N-terminal catalytic region, including the serine nucleophile and oxyanion
        block. Structural and mutational work establishes the patatin Ser-Asp catalytic dyad (PMID:12779324),
        so the missing serine region argues against lipase activity in the deposited 302-residue sequence.
        This is target-specific contrary evidence despite the more specific lipase IBAs in the cached
        UniProt record. Whether the deficiency reflects an incomplete gene model or a biological inactive
        protein remains unresolved.
      supported_by:
        - reference_id: file:WHEAT/A0A3B6GK97/A0A3B6GK97-uniprot.txt
          supporting_text: >-
            ID   A0A3B6GK97_WHEAT        Unreviewed;       302 AA. ... DR   GO; GO:0004620; F:glycerophospholipase
            activity; IBA:GO_Central. ... DR   GO; GO:0047372; F:monoacylglycerol lipase activity; IBA:GO_Central.
            ... DR   InterPro; IPR016035; Acyl_Trfase/lysoPLipase. ... DR   InterPro; IPR002641; PNPLA_dom.
            ... FT   DOMAIN          1..134 ... FT                   /note="PNPLA"
        - reference_id: PMID:12779324
          supporting_text: >-
            Ser77 and Asp215 were critical for both esterase and bioactivity
        - reference_id: file:WHEAT/A0A3B6GK97/A0A3B6GK97-bioinformatics/RESULTS.md
          supporting_text: >-
            the modeled 302-aa sequence lacks the entire N-terminal half of the patatin catalytic domain
            ... serine nucleophile elbow (G-T-S-T-G)** are absent.
  - source_method: ProtNLM2
    source_version: UniProt 2024_06 pilot
    predicted_term:
      id: GO:0016042
      label: lipid catabolic process
    predicted_term_type: GO_BP
    review:
      assessment: UNC
      confidence_score: 1
      summary: >-
        The reproducible alignment supports a patatin-family relationship but shows that the deposited
        sequence lacks the catalytic serine region. Thus, lipid hydrolysis by the encoded protein cannot
        be assumed from family membership. The predicted biological process could still apply through
        a noncatalytic role or to a corrected full-length gene model, neither of which is established
        by the inspected evidence. Lipid catabolic process is not present as an equivalent annotation
        in the cached records and remains uncertain.
      supported_by:
        - reference_id: file:WHEAT/A0A3B6GK97/A0A3B6GK97-uniprot.txt
          supporting_text: >-
            ID   A0A3B6GK97_WHEAT        Unreviewed;       302 AA. ... DR   GO; GO:0004620; F:glycerophospholipase
            activity; IBA:GO_Central. ... DR   GO; GO:0047372; F:monoacylglycerol lipase activity; IBA:GO_Central.
            ... DR   InterPro; IPR016035; Acyl_Trfase/lysoPLipase. ... DR   InterPro; IPR002641; PNPLA_dom.
            ... FT   DOMAIN          1..134 ... FT                   /note="PNPLA"
        - reference_id: file:WHEAT/A0A3B6GK97/A0A3B6GK97-bioinformatics/RESULTS.md
          supporting_text: >-
            the modeled 302-aa sequence lacks the entire N-terminal half of the patatin catalytic domain
            ... serine nucleophile elbow (G-T-S-T-G)** are absent.
references:
  - id: file:WHEAT/A0A3B6GK97/A0A3B6GK97-uniprot.txt
    title: A0A3B6GK97-uniprot.txt
  - id: PMID:12779324
    title: The crystal structure, mutagenesis, and activity studies reveal that patatin is a lipid
      acyl hydrolase with a Ser-Asp catalytic dyad.
  - id: file:WHEAT/A0A3B6GK97/A0A3B6GK97-bioinformatics/RESULTS.md
    title: RESULTS.md