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FDX2

Chr 19p13.2

ferredoxin 2

Aliases:
MGC19604
MANE:
ENST00000393708.3

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Predicted protein structure

Clinical relevance (Genomics England PanelApp)

Diagnostic Grade (Green)

  • Acute rhabdomyolysis

    BIALLELIC, autosomal or pseudoautosomal
  • Likely inborn error of metabolism

    BIALLELIC, autosomal or pseudoautosomal
  • Mitochondrial disorders

    BIALLELIC, autosomal or pseudoautosomal
  • Possible mitochondrial disorder - nuclear genes

    BIALLELIC, autosomal or pseudoautosomal
  • Rhabdomyolysis and metabolic muscle disorders

    BIALLELIC, autosomal or pseudoautosomal
  • Undiagnosed metabolic disorders

    BIALLELIC, autosomal or pseudoautosomal

Disease associations (Open Targets)

  • Mitochondrial myopathy

    0.75
  • congenital adrenal hyperplasia

    0.37
  • rheumatoid arthritis

    0.35
  • inborn mitochondrial myopathy

    0.30
  • hereditary disease

    0.27
  • COVID-19

    0.09
  • Crohn disease

    0.08
  • psoriasis

    0.07
  • sclerosing cholangitis

    0.07
  • autoimmune disease

    0.07

Score is the Open Targets composite evidence score (0-1). Higher = stronger gene-disease association.

Protein function (UniProt)

Ferredoxin-2, mitochondrial

Electron donor, of the core iron-sulfur cluster (ISC) assembly complex, that acts to reduce the persulfide into sulfide during [2Fe-2S] clusters assembly on the scaffolding protein ISCU (PubMed:28001042). The core iron-sulfur cluster (ISC) assembly complex is involved in the de novo synthesis of a [2Fe-2S] cluster, the first step of the mitochondrial iron-sulfur protein biogenesis (By similarity). This process is initiated by the cysteine desulfurase complex (NFS1:LYRM4:NDUFAB1) that produces persulfide which is delivered on the scaffold protein ISCU in a FXN-dependent manner (By similarity). Then this complex is stabilized by FDX2 which provides reducing equivalents to accomplish the [2Fe-2S] cluster assembly (By similarity). Finally, the [2Fe-2S] cluster is transferred from ISCU to chaperone proteins, including HSCB, HSPA9 and GLRX5 (By similarity). Essential for coenzyme Q biosynthesis: together with FDXR, transfers the electrons required for the hydroxylation reaction performed by COQ6 (PubMed:38425362)

Data sources: HGNC (CC BY 4.0), AlphaFold (CC BY 4.0, Jumper et al. Nature 2021), Genomics England PanelApp (CC BY 4.0), ClinGen, Open Targets (CC0), UniProt.

Not for sole clinical decision-making. Always verify against primary sources.