id: A0A9L0S4L8
gene_symbol: EFR3A
taxon:
  id: NCBITaxon:9796
  label: Equus caballus
status: COMPLETE
description: Assessment of 1 ProtNLM GO predictions for the selected horse EFR3A protein, using mammalian
  experimental findings and an explicit comparison of the horse sequence.
source_documents:
- genes/human/EFR3A/EFR3A-uniprot.txt
- genes/HORSE/EFR3A/EFR3A-bioinformatics/RESULTS.md
- projects/PROTNLM_EVALUATION/mammal-benchmark/horse40-predictions.csv
- genes/HORSE/EFR3A/EFR3A-bioinformatics/alignment.txt
predictions:
- source_method: ProtNLM2
  source_version: UniProt API snapshot 2026-09-08
  predicted_term:
    id: GO:0072659
    label: protein localization to plasma membrane
  predicted_term_type: GO_BP
  review:
    assessment: UNC
    confidence_score: 1
    summary: "Human EFR3A recruits PI4KA through a palmitoylated membrane anchor. The horse sequence aligns\
      \ at 98.24% identity downstream but lacks human residues2\u201326, including the Cys6\u2013Cys9\
      \ palmitoylation cluster whose mutation relocates human EFR3A to the cytosol (PMID:23229899; PMID:25380825).\
      \ Thus high overall similarity does not establish plasma-membrane recruitment for this exact protein\
      \ model. Alternative initiation or an incomplete gene model could reconcile the sequences, but neither\
      \ is demonstrated here. The prediction remains unresolved rather than being transferred from the\
      \ human gene label. Training-set membership is unknown."
    supported_by:
    - reference_id: file:human/EFR3A/EFR3A-uniprot.txt
      supporting_text: 'CC   -!- FUNCTION: Component of a complex required to localize

        CC       phosphatidylinositol 4-kinase (PI4K) to the plasma membrane

        CC       (PubMed:23229899, PubMed:25608530, PubMed:26571211). The complex acts

        CC       as a regulator of phosphatidylinositol 4-phosphate (PtdIns(4)P)

        CC       synthesis (Probable). In the complex, EFR3A probably acts as the

        CC       membrane-anchoring component (PubMed:23229899). Also involved in

        CC       responsiveness to G protein-coupled receptors; it is however unclear

        CC       whether this role is direct or indirect (PubMed:25380825).

        CC       {ECO:0000269|PubMed:23229899, ECO:0000269|PubMed:25380825,

        CC       ECO:0000269|PubMed:25608530, ECO:0000305}.'
    - reference_id: file:HORSE/EFR3A/EFR3A-bioinformatics/RESULTS.md
      supporting_text: The horse sequence A0A9L0S4L8 (796 residues) aligns to human Q14156 (821 residues)
        with 98.24% identity across 796 paired residues. Paired coverage is 96.95% of the human sequence
        and 100.0% of the horse sequence.
    - reference_id: file:HORSE/EFR3A/EFR3A-bioinformatics/alignment.txt
      supporting_text: "target            0 MPTRVCCCCSALRPRYKRLVDNIFPEDPKDGLVKTDMEKLTFYAVSAPEKLDRIGSYLAE\n\
        \                  0 |-------------------------..||||||.|||||||||||||||||||||||||\nquery     \
        \        0 M-------------------------IDKDGLVKADMEKLTFYAVSAPEKLDRIGSYLAE"
    - reference_id: PMID:23229899
      supporting_text: "Accordingly, a bioorthogonal metabolic labeling approach (Hang et al., 2011) revealed\
        \ that FLAG-tagged EFR3A and EFR3B were palmitoylated at the N-terminal Cys-rich motif (Fig. 4\
        \ B). Importantly, palmitoylation-deficient mutants (C6S/C7S/C8S/C9S for EFR3A and C5S/C7S/C8S\
        \ for EFR3B) were localized in the cytosol (Fig. 4 C), and the EFR3B palmitoylation-deficient\
        \ mutant was unable to recruit tagged TTC7B and M1-PI4KIII\u03B1 to the plasma membrane (Fig.\
        \ S2)."
references:
- id: file:human/EFR3A/EFR3A-uniprot.txt
  title: UniProt record for human EFR3A
  findings: []
- id: file:HORSE/EFR3A/EFR3A-bioinformatics/RESULTS.md
  title: "EFR3A: horse\u2013human sequence comparison"
  findings: []
- id: file:HORSE/EFR3A/EFR3A-bioinformatics/alignment.txt
  title: EFR3A pairwise alignment
  findings: []
- id: PMID:23229899
  title: "PtdIns4P synthesis by PI4KIII\u03B1 at the plasma membrane and its impact on plasma membrane\
    \ identity."
  findings: []