Search results for TIMM17A

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Protein (2 results from a total of 2)

Identifier: R-HSA-1252118
Species: Homo sapiens
Compartment: mitochondrial inner membrane
Primary external reference: UniProt: TIMM17A: Q99595
Identifier: R-HSA-1955376
Species: Homo sapiens
Compartment: mitochondrial intermembrane space
Primary external reference: UniProt: TIMM17A: Q99595

Reaction (2 results from a total of 2)

Identifier: R-HSA-9839064
Species: Homo sapiens
Compartment: mitochondrial inner membrane
YME1L1 (YME1L, i-AAA+) is a homohexameric zinc metalloprotease that is anchored in the inner membrane and protrudes into the mitochondrial intermembrane space (Coppola et al. 2000, Shah et al. 2000, Wai et al. 2016). Substrate proteins of YME1L1 initially bind conserved helices at the N-terminal end of the ATPase domain and at the C-terminal domain of the protease domain (inferred from the yeast homolog in Graef et al. 2007). The substrate protein is unfolded and translocated processively in an ATP-dependent reaction to a central pore formed by the protease domains of the YME1L1 complex.
YME1L1 binds, unfolds, and degrades specific inner membrane proteins (MacVicar et al. 2019). These include components of the mitochondrial import apparatus: TIMM17A (Rainbolt et al. 2013), TIMM22 (MacVicar et al. 2019), and improperly folded TIMM9 and TIMM10 (inferred from yeast homologs in Baker et al. 2012). Substrates of YME1L1 also include components of the respiratory chain: MT‑ND1 and MT‑CO4 (Stiburek et al. 2012, Cesnekova et al. 2018), unassembled MT‑CO2 (inferred from yeast homologs in Nakai et al. 1995), and subunits of respiratory chain complex I (Cesnekova et al. 2018) such as unassembled NDUFB6 (Stiburek et al. 2012, Cesnekova et al. 2018). YME1L1 also degrades the protease OMA1 (Rainbolt et al. 2016), a stress-activated ATP-independent protease that can act reciprocally to YME1L1, and OPA1 (Cesnekova et al. 2018), a dynamin-like protein that controls mitochondrial morphology.
Identifier: R-HSA-9839146
Species: Homo sapiens
Compartment: mitochondrial inner membrane
YME1L1 (YME1L, i-AAA) is a hexameric metalloprotease that is anchored in the inner membrane and protrudes into the mitochondrial intermembrane space (Coppola et al. 2000, Shah et al. 2000, Wai et al. 2016). Each monomer of YME1L1 contains a membrane-proximal ATPase and protein unfolding domain and a membrane-distal protease domain (inferred from the yeast homolog in Puchades et al. 2017). The substrate protein enters a central channel formed by the ATPase domains, where it is unfolded and translocated into the pore formed by the protease domains (inferred from the yeast homolog in Puchades et al. 2017). Within the protease pore, it is hydrolyzed by zinc cofactors bound to the protease domains (inferred from the yeast homolog in Puchades et al. 2017).
YME1L1 binds, unfolds, and degrades specific inner membrane proteins (MacVicar et al. 2019). These include components of the mitochondrial import apparatus: TIMM17A (Rainbolt et al. 2013), TIMM22 (MacVicar et al. 2019), and improperly folded TIMM9 and TIMM10 (inferred from yeast homologs in Baker et al. 2012). Substrates of YME1l1 also include components of the respiratory chain: MT‑ND1 and MT‑CO4 (Stiburek et al. 2012, Cesnekova et al. 2018), unassembled MT‑CO2 (inferred from yeast homologs in Nakai et al. 1995), and subunits of respiratory chain complex I (Cesnekova et al. 2018) such as unassembled NDUFB6 (Stiburek et al. 2012, Cesnekova et al. 2018). YME1L1 also degrades the protease OMA1 (Rainbolt et al. 2016), a stress-activated ATP-independent protease that can act reciprocally to YME1L1, and OPA1 (Cesnekova et al. 2018), a dynamin-like protein that controls mitochondrial morphology.
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