Search Results
Overview
| Uniprot ID | Q8JZQ2 |
|---|---|
| Protein Name | Mitochondrial inner membrane m-AAA protease component AFG3L2 |
| Gene Name | Afg3l2 |
| Organism | Mus musculus |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 121 | GGKRRGKKEDSHWWS |
| 307 | DEIDVKFKDVAGCEE |
| 330 | VNFLKNPKQYQDLGA |
| 487 | KGRASIFKVHLRPLK |
| 558 | VIGGLEKKTQVLQPE |
| 792 | EEKKEKEKEEPLNEK |
| 90 | GKKASEPKEAVGEKK |
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). Also acts as a regulator of carnitine biosynthesis by mediating cleavage and degradation of SLC25A45 (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)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0005745 | m-AAA complex |
| Cellular Component | GO:0005743 | mitochondrial inner membrane |
| Cellular Component | GO:0005739 | mitochondrion |
| Cellular Component | GO:0033011 | perinuclear theca |
| Cellular Component | GO:0120238 | sperm glycocalyx |
| Cellular Component | GO:0120212 | sperm head-tail coupling apparatus |
| Cellular Component | GO:0097225 | sperm midpiece |
| Cellular Component | GO:0097228 | sperm principal piece |
| Molecular Function | GO:0005524 | ATP binding |
| Molecular Function | GO:0016887 | ATP hydrolysis activity |
| Molecular Function | GO:0004176 | ATP-dependent peptidase activity |
| Molecular Function | GO:0140567 | membrane protein dislocase activity |
| Molecular Function | GO:0004222 | metalloendopeptidase activity |
| Molecular Function | GO:0008237 | metallopeptidase activity |
| Molecular Function | GO:0008270 | zinc ion binding |
| Biological Process | GO:0007409 | axonogenesis |
| Biological Process | GO:0036444 | calcium import into the mitochondrion |
| Biological Process | GO:0072753 | cellular response to glutathione |
| Biological Process | GO:0042407 | cristae formation |
| Biological Process | GO:0160007 | glutathione import into mitochondrion |
| Biological Process | GO:0033619 | membrane protein proteolysis |
| Biological Process | GO:0051560 | mitochondrial calcium ion homeostasis |
| Biological Process | GO:0008053 | mitochondrial fusion |
| Biological Process | GO:0034982 | mitochondrial protein processing |
| Biological Process | GO:0141164 | mitochondrial protein quality control |
| Biological Process | GO:0007005 | mitochondrion organization |
| Biological Process | GO:0055001 | muscle cell development |
| Biological Process | GO:0042552 | myelination |
| Biological Process | GO:0021675 | nerve development |
| Biological Process | GO:0007528 | neuromuscular junction development |
| Biological Process | GO:0016540 | protein autoprocessing |
| Biological Process | GO:0030163 | protein catabolic process |
| Biological Process | GO:0051604 | protein maturation |
| Biological Process | GO:0016485 | protein processing |
| Biological Process | GO:0006508 | proteolysis |
| Biological Process | GO:0110097 | regulation of calcium import into the mitochondrion |
| Biological Process | GO:0040014 | regulation of multicellular organism growth |
| Biological Process | GO:0060013 | righting reflex |
Reference
[1] Zhuo W, Zhang M, Tan J, Gao Y, Wang Y et al.. Lysine lactylation analysis of proteins in the heart of the Kawasaki disease mouse model.. Front Cell Dev Biol 13:1550220. 2025. PMID: 40114965.
[2] Wu D, Tang Y, Li X, Xiong S, Zhang Z et al.. Characterization of protein lactylation in healthy and ischemic mouse hearts.. Front Cardiovasc Med 12:1644886. 2025. PMID: 41089239.