Literature summary for 3.4.24.64 extracted from

Jobling, R.K.; Assoum, M.; Gakh, O.; Blaser, S.; Raiman, J.A.; Mignot, C.; Roze, E.; Duerr, A.; Brice, A.; Levy, N.; Prasad, C.; Paton, T.; Paterson, A.D.; Roslin, N.M.; Marshall, C.R.; Desvignes, J.P.; Roeckel-Trevisiol, N.; Scherer, S.W.; Rouleau, G.A.; Megarbane, A.; Isaya, G.; Delague, V.; Yoon, G.
PMPCA mutations cause abnormal mitochondrial protein processing in patients with non-progressive cerebellar ataxia (2015), Brain, 138, 1505-1517 .

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining

Organism	UniProt	Comment	Textmining
Homo sapiens	Q10713 AND O75439	Q10713: mitochondrial-processing peptidase subunit alpha, O75439: mitochondrial-processing peptidase subunit beta	-

Source Tissue	Comment	Organism	Textmining

General Information	Comment	Organism
physiological function	primary enzyme responsible for the maturation of the vast majority of nuclear-encoded mitochondrial proteins, which is necessary for life at the cellular level. Analysis of lymphoblastoid cells and fibroblasts from patients homozygous for the PMPCA p.Ala377Thr, a mutation in the alpha subunit of mitochondrial processing peptidase and carriers demonstrate that the mutation impacts both the level of the alpha subunit encoded by PMPCA and the function of mitochondrial processing peptidase. This mutation impacts the maturation process of frataxin, the protein which is depleted in Friedreich ataxia	Homo sapiens

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Release 2023.1 (January 2023)