Gene Ontology annotation through association of InterPro records with GO terms
Annotation inferences using phylogenetic trees
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PANTHER phylogenetic propagation transfers the conserved Rieske-subunit functions across UQCRFS1 orthologues, including oxidoreductase activity (GO:0016491), respiratory chain complex III (GO:0045275), and mitochondrial electron transport, ubiquinol to cytochrome c (GO:0006122).
Gene Ontology annotation based on UniProtKB/Swiss-Prot keyword mapping
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UniProtKB keywords KW-0679 (Respiratory chain), KW-0411 (Iron-sulfur), and KW-0479 (Iron) on UQCRFS1 are mapped to GO:0022904 (respiratory electron transport chain), GO:0051536 (iron-sulfur cluster binding), and GO:0046872 (metal ion binding) respectively.
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Automatic assignment of GO terms using logical inference, based on on inter-ontology links
Electronic Gene Ontology annotations created by ARBA machine learning models
Combined Automated Annotation using Multiple IEA Methods
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Combined automated IEA pipelines annotate UQCRFS1 with quinol- cytochrome-c reductase activity (GO:0008121) and 2 iron, 2 sulfur cluster binding (GO:0051537) from converging UniProt feature, family, and reaction-based evidence.
Phosphoproteome analysis of functional mitochondria isolated from resting human muscle reveals extensive phosphorylation of inner membrane protein complexes and enzymes.
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UQCRFS1 identified by mass spectrometry in mitochondria isolated from human skeletal muscle.
"We performed a phosphoproteomics study of functional mitochondria isolated from human muscle biopsies with the aim to obtain a comprehensive overview of mitochondrial phosphoproteins."
LYRM7/MZM1L is a UQCRFS1 chaperone involved in the last steps of mitochondrial Complex III assembly in human cells.
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LYRM7 (MZM1L) identified as a chaperone for UQCRFS1, binding the Rieske protein in the mitochondrial matrix and stabilizing it prior to translocation into Complex III.
"We conclude that human LYRM7, which we propose to be renamed MZM1L (MZM1-like), works as a human Rieske Fe-S protein (UQCRFS1) chaperone, binding to this subunit within the mitochondrial matrix and stabilizing it prior to its translocation and insertion into the late CIII dimeric intermediate within the mitochondrial inner membrane."
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UQCRFS1 demonstrated to co-migrate with assembled CIII2 and supercomplexes by BN-PAGE.
"LYRM7/MZM1L is a novel human CIII assembly factor involved in the UQCRFS1 insertion step, which enables formation of the mature and functional CIII enzyme."
Mitochondrial Protein Interaction Mapping Identifies Regulators of Respiratory Chain Function.
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UQCRFS1-LYRM7 interaction detected by affinity enrichment mass spectrometry in mitochondrial protein interaction mapping.
"we assessed condition-specific protein-protein interactions for 50 select MXPs using affinity enrichment mass spectrometry."
A Single Adaptable Cochaperone-Scaffold Complex Delivers Nascent Iron-Sulfur Clusters to Mammalian Respiratory Chain Complexes I-III.
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HSC20 co-chaperone binds LYRM7 LYR motif in pre-assembled UQCRFS1-LYRM7 intermediate to facilitate [2Fe-2S] cluster transfer to UQCRFS1.
"Binding of HSC20 to the LYR motif of LYRM7 in a pre-assembled UQCRFS1-LYRM7 intermediate in the mitochondrial matrix facilitates Fe-S cluster transfer to UQCRFS1."
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UQCRFS1 is the penultimate subunit incorporated during Complex III assembly.
"Incorporation of the Rieske protein UQCRFS1 is the penultimate step in CIII assembly, followed only by the insertion of a small supernumerary subunit (UQCR10 in mammalian cells)."
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The Fe-S cluster of UQCRFS1 is essential for Complex III activity.
"The iron-sulfur (Fe-S) cluster of the Rieske protein, UQCRFS1, is essential for Complex III (CIII) activity"
Bi-Allelic UQCRFS1 Variants Are Associated with Mitochondrial Complex III Deficiency, Cardiomyopathy, and Alopecia Totalis.
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Bi-allelic UQCRFS1 variants cause isolated Complex III deficiency with cardiomyopathy, alopecia totalis, and lactic acidosis.
"Affected children presented with low CIII activity in fibroblasts, lactic acidosis, fetal bradycardia, hypertrophic cardiomyopathy, and alopecia totalis."
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Patient fibroblasts showed reduced UQCRFS1 abundance, impaired mitochondrial import, defective CIII assembly, and decreased cellular respiration.
"Studies in proband-derived fibroblasts showed a deleterious effect of the variants on UQCRFS1 protein abundance, mitochondrial import, CIII assembly, and cellular respiration."
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Wild-type UQCRFS1 complementation via lentiviral transduction rescued the cellular phenotype.
"Complementation studies via lentiviral transduction and overexpression of wild-type UQCRFS1 restored mitochondrial function and rescued the cellular phenotype, confirming UQCRFS1 variants as causative for CIII deficiency."
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UQCRFS1 localizes to mitochondria by immunofluorescence; V14D variant causes cytosolic mislocalization.
"Studies in proband-derived fibroblasts showed a deleterious effect of the variants on UQCRFS1 protein abundance, mitochondrial import, CIII assembly, and cellular respiration."
Dual proteome-scale networks reveal cell-specific remodeling of the human interactome.
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UQCRFS1-LYRM7 interaction independently detected in BioPlex 3.0 proteome-scale interaction network.
"Through affinity-purification mass spectrometry, we have created two proteome-scale, cell-line-specific interaction networks."
Quantitative high-confidence human mitochondrial proteome and its dynamics in cellular context.
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UQCRFS1 identified as high-confidence mitochondrial protein.
"We classified >8,000 proteins in mitochondrial preparations of human cells and defined a mitochondrial high-confidence proteome of >1,100 proteins (MitoCoP)."
Multimodal cell maps as a foundation for structural and functional genomics.
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UQCRFS1-LYRM7 interaction detected in multimodal cell mapping study.
"we construct a global map of human subcellular architecture through joint measurement of biophysical interactions and immunofluorescence images for over 5,100 proteins in U2OS osteosarcoma cells."
Electron transfer from ubiquinol to cytochrome c of complex III
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UQCRFS1 participates in the core catalytic reaction of Complex III at the inner membrane.
"The protonmotive Q cycle is the mechanism by which complex III transfers electrons from ubiquinol to cytochrome c, linking this process to translocation of protons across the membrane."
apo-UQCRFS1 binds LYRM7
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Apo-UQCRFS1 binds chaperone LYRM7 in the mitochondrial matrix during Complex III biogenesis.
"the Complex III subunit UQCRFS1 (Rieske protein) binds to and is stabilized by the chaperone LYRM7 (MZM1L)"
2Fe-2S is inserted in UQCRFS1
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The [2Fe-2S] cluster is inserted into UQCRFS1 at the mitochondrial inner membrane during assembly.
"Frataxin (FXN) subunit of the 2Fe-2S transfer complex catalyzes the insertion of one 2Fe-2S cluster in the Complex III subunit UQCRFS1 (Rieske protein) as part of a UQCRFS1:LYRM7 complex."
Unknown peptidase cleaves UQCRFS1 subunit
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UQCRFS1 undergoes proteolytic processing after insertion into Complex III.
"Proteolytic processing is necessary for the correct insertion of UQCRFS1 in the complex III dimer. An unknown peptidase cleaves the N-terminal 78 amino acids of UQCRFS1"
TTC19 clears UQCRFS1 fragments from Complex III
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TTC19 mediates clearance of UQCRFS1-derived fragments from Complex III at the inner membrane.
"N-terminal cleavage fragments of UQCRFS1 are cleared by TTC19, stabilizing the final complex."
Deep research review for UQCRFS1 (Falcon/Edison)
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UQCRFS1 is the catalytic Rieske iron-sulfur subunit of mitochondrial complex III (CIII2), participating in ubiquinol (QH2) oxidation at the Qo site during the Q-cycle and shuttling an electron via its 2Fe-2S cluster to cytochrome c1.
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High-resolution in situ cryo-EM resolved multiple native supercomplex organizations and captured distinct Qo-site Q10/QH2 binding states and corresponding Rieske-domain movements, providing direct structural support for the Q-cycle mechanism (Zheng et al. 2024, Nature).
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UQCRFS1 is the last subunit incorporated into CIII; LYRM7 (MZM1L) chaperones Fe-S cluster insertion, BCS1L translocates the folded ISP into pre-CIII for late-stage incorporation, and TTC19 mediates turnover of N-terminal peptides for CIII integrity.