Gene Ontology annotation through association of InterPro records with GO terms
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Spastic paraplegia and OXPHOS impairment caused by mutations in paraplegin, a nuclear-encoded mitochondrial metalloprotease.
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Paraplegin (the ortholog of ppgn-1) is a nuclear-encoded mitochondrial metalloprotease homologous to the yeast mitochondrial AAA ATPases (AFG3, RCA1, YME1) that combine proteolytic and chaperone-like activities at the inner mitochondrial membrane, and it localizes to mitochondria.
"Paraplegin is highly homologous to the yeast mitochondrial ATPases, AFG3, RCA1, and YME1, which have both proteolytic and chaperon-like activities at the inner mitochondrial membrane."
The m-AAA protease defective in hereditary spastic paraplegia controls ribosome assembly in mitochondria.
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AAA proteases are a conserved family of membrane-bound ATP-dependent proteases that ensure quality control of mitochondrial inner-membrane proteins, and the m-AAA protease processes the ribosomal protein MrpL32 to allow completion of ribosome assembly at the inner membrane.
"AAA proteases comprise a conserved family of membrane bound ATP-dependent proteases that ensures the quality control of mitochondrial inner-membrane proteins."
Translating m-AAA protease function in mitochondria to hereditary spastic paraplegia.
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Paraplegin is a conserved subunit of the ubiquitous, ATP-dependent m-AAA protease in mitochondria, which carries out protein quality control in the inner mitochondrial membrane.
"paraplegin, which is a conserved subunit of the ubiquitous and ATP-dependent m-AAA protease in mitochondria."
Presequence-dependent folding ensures MrpL32 processing by the m-AAA protease in mitochondria.
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m-AAA proteases have dual functions in the inner mitochondrial membrane: regulated processing of specific substrates and quality-control degradation of misfolded polypeptides to peptides.
"m-AAA proteases exert dual functions in the mitochondrial inner membrane: they mediate the processing of specific regulatory proteins and ensure protein quality control degrading misfolded polypeptides to peptides."