FARS2/O95363 encodes the monomeric mitochondrial phenylalanyl-tRNA synthetase. The reviewed enzyme activity activates phenylalanine with ATP and charges tRNA(Phe), directly supplying aminoacylated tRNA for mitochondrial translation (PMID:10329163, PMID:19549855, PMID:22833457). The core combines that activity with translation-associated aminoacylation and curated matrix placement.
All 107 imported annotation contexts were assessed: 22 ACCEPT, 81 KEEP_AS_NON_CORE and four MODIFY. Three imports of the obsolete phenylalanyl-tRNA aminoacylation term and the tRNA-processing assertion are refined to GO:0006418 while preserving their original source fields. The conserved function is supported; obsoletion is a vocabulary issue rather than a PAINT propagation failure. There are no PENDING or NEW annotations and no publication quotations were added.
The user's standing project convention retains supported generic binding as non-core when no evidence-backed specific replacement is established. Exact PMID-specific FARS2/partner source records support all 81 interaction annotations. No partner's catalytic or signaling role is assigned to FARS2. The retained generic-binding advisories keep the review's machine status DRAFT despite every imported context having a decision.
Direct human mitochondrial proteomics and rat COXIV colocalization support mitochondrion. Matrix placement is a more precise curated inference traced to UniProt/ortholog and Reactome sources, not a separately measured compartment in those experiments. Cytoplasm includes organelles; it is not evidence of a cytosolic FARS2 product.
The official protein is a 451-residue precursor. UniProt does not establish alternative natural products or an exact cleavage boundary. RefSeq/Ensembl models and recombinant constructs were inspected as product context and were not converted into natural isoforms. No synthetic O95363-1 or guessed processing position was introduced.
See the source guide for original article URLs, complete reference scopes, exact target tables, primary-access limitations and database provenance. The binding record table preserves partner and source identifiers without implying physiological functions. The research provider attempt failed; these notes and the guide are authored evidence summaries, not fabricated provider output.
Canonical checks pass, including strict GOA matching, ontology/component validation, computed status and rendering of 216 narratives. Status remains DRAFT with exactly 81 supported generic-binding advisories and no unfinished annotations. All 17 selected machine and normal files remain exact. Fifteen normal sources include the exact accepted shared PTHR11538 entries and metadata from PR #2049, with a separately preserved PAINT file; authentic newer alternatives and seven unused discovery publications stay private. The binding-record table accompanies its source guide. Rendered HTML was checked privately. Unrelated workspace files remain unchanged.
The five broad assertions for nucleotide binding, aminoacyl-tRNA ligase activity, tRNA charging and cytoplasm are now TOO_GENERAL, each entailed by a positively retained strict descendant. This preserves the scientific claims and source-specific limits while separating term specificity from source validity. The revised counts are 17 ACCEPT, 81 KEEP_AS_NON_CORE, four MODIFY and five TOO_GENERAL; no imported context is pending and no annotation is added. The matrix inference is explicit in the core, alongside the independently supported mitochondrion location.
The current binding records replace the historical TSV mentioned above. Conversion preserves all 81 rows and all fields, including exact partner accessions, record identifiers, empty author-release fields and caveats; PSI-MI methods are YAML lists. The prior history record is append-only and remains unchanged. A new history entry belongs to the final canonical follow-up.
The primary 2009 enzyme experiments motivate a bounded question about cellular meta-tyrosine incorporation, with a proposed test that distinguishes aminoacylation and translational incorporation from post-translational oxidation. No new GO activity or process follows from the in-vitro alternative-substrate result. The standalone description, all 107 source objects, all 17 whole reference objects, all 81 binding reviews, zero-quotation boundary, product boundary and immutable source files are preserved.