GFER

FAD-linked sulfhydryl oxidase ALR

205 amino acids

Isoform 2: May act as an autocrine hepatotrophic growth factor promoting liver regeneration.

23.449 kDa

MAAPGERGRFHGGNLFFLPGGARSEMMDDLATDARGRGAGRRDAAASASTPAQAPTSDSPVAEDASRRRPCRACVDFKTWMRTQQKRDTKFREDCPPDREELGRHSWAVLHTLAAYYPDLPTPEQQQDMAQFIHLFSKFYPCEECAEDLRKRLCRNHPDTRTRACFTQWLCHLHNEVNRKLGKPDFDCSKVDERWRDGWKDGSCD

Gfer

FAD-linked sulfhydryl oxidase ALR

198 amino acids

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. May have a function in liver regeneration and spermatogenesis.

22.837 kDa

MAAPSEPAGFPRGSRFSFLPGGAHSEMTDDLVTDARGRGARHRKDNAPAAAPAPKGLEHGKRPCRACVDFKSWMRTQQKRDIKFREDCPQDREELGRNTWAFLHTLAAYYPDMPTPEQQQDMAQFIHIFSKFYPCEECAEDIRKRIDRSQPDTSTRVSFSQWLCRLHNEVNRKLGKPDFDCSRVDERWRDGWKDGSCD

Gfer

FAD-linked sulfhydryl oxidase ALR

198 amino acids

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 (By similarity).

22.877 kDa

MAAPSEPAGFPRGSRFSFLPGGARSEMTDDLVTDARGRGARHRDDTTPAAAPAPQGLEHGKRPCRACVDFKSWMRTQQKRDIKFREDCPQDREELGRHTWAFLHTLAAYYPDRPTPEQQQDMAQFIHIFSKFYPCEECAEDIRKRIGRNQPDTSTRVSFSQWLCRLHNEVNRKLGKPDFDCSRVDERWRDGWKDGSCD