UniprotKB/SwissProt ID: Q8JZQ2 (Q8JZQ2)
Gene Name:
Afg3l2
Organism: Mus musculus (Mouse)
Function: Catalytic component of the m-AAA protease, a protease that plays a key role in proteostasis of inner mitochondrial membrane proteins, and which is essential for axonal and neuron development (PubMed:16239145, PubMed:18337413, PubMed:22678058, PubMed:27642048, PubMed:30389403). AFG3L2 possesses both ATPase and protease activities: the ATPase activity is required to unfold substrates, threading them into the internal proteolytic cavity for hydrolysis into small peptide fragments (By similarity). The m-AAA protease carries out protein quality control in the inner membrane of the mitochondria by mediating degradation of mistranslated or misfolded polypeptides (By similarity). The m-AAA protease complex also promotes the processing and maturation of mitochondrial proteins, such as MRPL32/bL32m, PINK1 and SP7 (PubMed:16239145). Mediates protein maturation of the mitochondrial ribosomal subunit MRPL32/bL32m by catalyzing the cleavage of the presequence of MRPL32/bL32m prior to assembly into the mitochondrial ribosome (PubMed:16239145). Required for SPG7 maturation into its active mature form after SPG7 cleavage by mitochondrial-processing peptidase (MPP) (By similarity). Required for the maturation of PINK1 into its 52kDa mature form after its cleavage by mitochondrial-processing peptidase (MPP) (By similarity). Acts as a regulator of calcium in neurons by mediating degradation of SMDT1/EMRE before its assembly with the uniporter complex, limiting the availability of SMDT1/EMRE for MCU assembly and promoting efficient assembly of gatekeeper subunits with MCU (By similarity). Promotes the proteolytic degradation of GHITM upon hyperpolarization of mitochondria: progressive GHITM degradation leads to respiratory complex I degradation and broad reshaping of the mitochondrial proteome by AFG3L2 (By similarity). Also acts as a regulator of mitochondrial glutathione homeostasis by mediating cleavage and degradation of SLC25A39 (By similarity). SLC25A39 cleavage is prevented when SLC25A39 binds iron-sulfur (By similarity). Involved in the regulation of OMA1-dependent processing of OPA1 (PubMed:17615298, PubMed:20038678). May act by mediating processing of OMA1 precursor, participating in OMA1 maturation (By similarity)
Other Modifications: View all modification sites in dbPTM
Protein Subcellular Localization: Mitochondrion inner membrane
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