Literature summary for 1.8.3.2 extracted from

Sztolsztener, M.E.; Brewinska, A.; Guiard, B.; Chacinska, A.
Disulfide bond formation: sulfhydryl oxidase ALR controls mitochondrial biogenesis of human MIA40 (2013), Traffic, 14, 309-320.

Search for more literature for 1.8.3.2

Application

Application	Comment	Organism
medicine	mutation R194H has been isolated from a rare autosomal recessive myopathy connected with the development of cataract and respiratory-chain deficiency. In a Saccharomyces cerevisiae model, under restrictive conditions, the presence of the mutant form of human ALR, R194H, impairs the accumulation of human Mia40 and other mitochondrial intermembrane space proteins	Homo sapiens

Protein Variants

Protein Variants	Comment	Organism
R194H	mutation isolated from a rare autosomal recessive myopathy connected with the development of cataract and respiratory-chain deficiency. In a Saccharomyces cerevisiae model, under restrictive conditions, the presence of the mutant form of human ALR, R194H, impairs the accumulation of human Mia40 and other mitochondrial intermembrane space proteins	Homo sapiens

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
mitochondrion	protein Alr is required for mitochondrial biogenesis of human Mia40, which is responsible for the import and oxidative folding of proteins destined for the intermembrane space of mitochondria	Homo sapiens	5739	-

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	P55789	-	-

Synonyms

Synonyms	Comment	Organism
ALR	-	Homo sapiens
Erv1	-	Homo sapiens
FAD-linked sulfhydryl oxidase ALR	-	Homo sapiens

General Information

General Information	Comment	Organism
physiological function	protein Alr is able to substitute for the function of Saccharomyces cerevisiae Erv1. Alr is required for mitochondrial biogenesis of human Mia40, which is responsible for the import and oxidative folding of proteins destined for the intermembrane space of mitochondria. The defective accumulation of human Mia40 in mitochondria in a recently identified disease that is caused by amino acid exchange in Alr	Homo sapiens

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Release 2023.1 (January 2023)