ProtNLM2 External predictions
View prediction review YAML · EFR3A-protnlm-predictions-review.yaml · Review status: COMPLETE
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
Review score: 2 = concordant with evidence; 1 = uncertain; 0 = discordant with evidence. This is an assessment score, not a model probability.
UNC — Uncertain Review score: 1/2
Prediction method: ProtNLM2 · Version: UniProt API snapshot 2026-09-08
Review rationale: Human EFR3A recruits PI4KA through a palmitoylated membrane anchor. The horse sequence aligns at 98.24% identity downstream but lacks human residues2–26, including the Cys6–Cys9 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.
Supporting Evidence:
- file:human/EFR3A/EFR3A-uniprot.txt: "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}."
- file:HORSE/EFR3A/EFR3A-bioinformatics/RESULTS.md: "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."
- file:HORSE/EFR3A/EFR3A-bioinformatics/alignment.txt: "target 0 MPTRVCCCCSALRPRYKRLVDNIFPEDPKDGLVKTDMEKLTFYAVSAPEKLDRIGSYLAE 0 |-------------------------..||||||.||||||||||||||||||||||||| query 0 M-------------------------IDKDGLVKADMEKLTFYAVSAPEKLDRIGSYLAE"
- PMID:23229899: "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-PI4KIIIα to the plasma membrane (Fig. S2)."