id: A0A9L0K7N3
gene_symbol: LOXL3
taxon:
  id: NCBITaxon:9793
  label: Equus asinus
status: COMPLETE
description: Assessment of the single ProtNLM2 GO prediction for donkey LOXL3 (A0A9L0K7N3), judged against
  the donkey GOA record (protein-lysine 6-oxidase activity, copper ion binding, collagen fibril organization,
  extracellular region and broader ARBA/InterPro terms), the human ortholog P58215 and its characterization,
  and a donkey-human alignment (96% identity, catalytic residues conserved). The prediction, peptidyl-lysine
  oxidation, is correct and absent from donkey GOA (COR). The frozen ProtNLM2 output contains no non-GO rows
  (function text or subcellular location) for this accession.
source_documents:
- projects/PROTNLM_EVALUATION/donkey40/donkey40-predictions.tsv
- genes/EQUAS/LOXL3/LOXL3-goa.tsv
- genes/human/LOXL3/LOXL3-uniprot.txt
- genes/EQUAS/LOXL3/LOXL3-bioinformatics/RESULTS.md
predictions:
- source_method: ProtNLM2
  source_version: UniProt API snapshot 2026-10-14
  predicted_term:
    id: GO:0018057
    label: peptidyl-lysine oxidation
  predicted_term_type: GO_BP
  review:
    assessment: COR
    confidence_score: 2
    summary: Human LOXL3 is a protein-lysine 6-oxidase that oxidizes peptidyl lysine residues to allysine in
      collagens and elastin, so it directly performs peptidyl-lysine oxidation; the human gene carries this process
      by IDA, and mouse Loxl3 (same PANTHER subfamily) directly oxidizes fibronectin. The donkey protein keeps the copper-binding histidines and the LTQ-forming lysine and tyrosine,
      with an invariant catalytic domain. Donkey GOA has the molecular function (protein-lysine 6-oxidase activity)
      but no peptidyl-lysine oxidation row, and the MF and BP are in different GO aspects, so this is a novel
      correct process annotation rather than LSP or CNN.
    supported_by:
    - reference_id: file:human/LOXL3/LOXL3-uniprot.txt
      supporting_text: 'FUNCTION: Protein-lysine 6-oxidase that mediates the oxidation of

        CC       peptidyl lysine residues to allysine in target proteins'
    - reference_id: PMID:26954549
      supporting_text: We find that LoxL3 complexes with and directly oxidizes Fibronectin (FN)
    - reference_id: PMID:17018530
      supporting_text: These findings strongly indicate that LOXL3 encodes two variants, LOXL3 and LOXL3-sv1,
        both of which function as amine oxidases with distinct tissue and substrate specificities from one another.
    - reference_id: file:EQUAS/LOXL3/LOXL3-bioinformatics/RESULTS.md
      supporting_text: the lysine tyrosylquinone (LTQ) cofactor residues (human Lys634 and Tyr670 = donkey Lys705
        and Tyr741) are conserved
references:
- id: file:EQUAS/LOXL3/LOXL3-goa.tsv
  title: Donkey LOXL3 GOA annotations
  findings: []
- id: file:human/LOXL3/LOXL3-uniprot.txt
  title: UniProt Swiss-Prot record for human LOXL3 (P58215)
  findings: []
- id: file:EQUAS/LOXL3/LOXL3-bioinformatics/RESULTS.md
  title: 'LOXL3: donkey-human sequence comparison'
  findings: []
- id: PMID:17018530
  title: A tissue-specific variant of the human lysyl oxidase-like protein 3 (LOXL3) functions as an amine oxidase
    with substrate specificity.
  findings: []
- id: PMID:26954549
  title: Localized LoxL3-Dependent Fibronectin Oxidation Regulates Myofiber Stretch and Integrin-Mediated Adhesion.
  findings: []