GFER

Chr 16AR

growth factor, augmenter of liver regeneration

ENSG00000127554 UniProt: P55789 OMIM: 600924

GFER encodes a FAD-dependent sulfhydryl oxidase that regenerates disulfide bonds in the mitochondrial chaperone CHCHD4/MIA40, which is essential for protein folding in the mitochondrial intermembrane space. Autosomal recessive mutations cause mitochondrial progressive myopathy with congenital cataract and developmental delay, affecting muscle, eye, and neurodevelopmental systems from early life.

OMIM ResearchSummary from RefSeq, OMIM, UniProt

FAD-dependent sulfhydryl oxidase that regenerates the redox-active disulfide bonds in CHCHD4/MIA40, a chaperone essential for disulfide bond formation and protein folding in the mitochondrial intermembrane space. The reduced form of CHCHD4/MIA40 forms a transient intermolecular disulfide bridge with GFER/ERV1, resulting in regeneration of the essential disulfide bonds in CHCHD4/MIA40, while GFER/ERV1 becomes re-oxidized by donating electrons to cytochrome c or molecular oxygen

OMIM ResearchGenerating clinical summary…

Primary Disease Associations & Inheritance

Myopathy, mitochondrial progressive, with congenital cataract and developmental delayMIM #613076

Clinical highlights

Gene-disease validity (ClinGen)

mitochondrial disease · ARDefinitivesufficient evidence for diagnostic panels

Interpreting a novel variant

Loss of function is the curated mechanism (Gene2Phenotype), though the gene is not strongly LoF-constrained in the population — weigh truncating variants against that tolerance.Curated gene-level mechanism — a prior for triage, not a per-variant call.

Active trials

Pubs (1 yr)

—

P/LP submissions

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P/LP missense

1.65

LOEUF

LOF

Mechanism· G2P

Some data sources returned errors (1)

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