Literature summary for 3.4.24.B18 extracted from

Koppen, M.; Bonn, F.; Ehses, S.; Langer, T.
Autocatalytic processing of m-AAA protease subunits in mitochondria (2009), Mol. Biol. Cell, 20, 4216-4224.

Search for more literature for 3.4.24.B18

Cloned(Commentary)

Cloned (Comment)	Organism
paraplegin, AFG3L1 and AFG3L2, His-tagged versions expressed in yeast	Mus musculus

Protein Variants

Protein Variants	Comment	Organism
additional information	truncated variants of paraplegin	Mus musculus

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
mitochondrial inner membrane	-	Mus musculus	5743	-

Organism

Organism	UniProt	Comment	Textmining
Mus musculus	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
immobilized metal ion affinity chromatography (Ni2+)	Mus musculus

Subunits

Subunits	Comment	Organism
More	subunits: paraplegin, AFG3L1 and AFG3L2; AFG3L1 forms homo-oligomeric complexes as well as hetero-oligomeric complexes with AFG3L2 and paraplegin; the mitochondrial processing peptidase MPP generates an intermediate form of AFG3L2 that is matured autocatalytically; AFG3L1 or AFG3L2 are also required for maturation of newly imported paraplegin subunits after their cleavage by MPP, mammalian m-AAA proteases can act as processing enzymes in vivo and reveal overlapping activities of AFG3L1 and AFG3L2	Mus musculus

Synonyms

Synonyms	Comment	Organism
m-AAA protease	-	Mus musculus

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Release 2023.1 (January 2023)