Cytochrome b-c1 complex subunit Rieske, mitochondrial (UQCRFS1)
The protein contains 274 amino acids for an estimated molecular weight of 29668 Da.
Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit transmembrane complex that is part of the mitochondrial electron transport chain which drives oxidative phosphorylation (PubMed:31883641). The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. The cytochrome b-c1 complex catalyzes electron transfer from ubiquinol to cytochrome c, linking this redox reaction to translocation of protons across the mitochondrial inner membrane, with protons being carried across the membrane as hydrogens on the quinol. In the process called Q cycle, 2 protons are consumed from the matrix, 4 protons are released into the intermembrane space and 2 electrons are passed to cytochrome c. The Rieske protein is a catalytic core subunit containing a [2Fe-2S] iron-sulfur cluster. It cycles between 2 conformational states during catalysis to transfer electrons from the quinol bound in the Q(0) site in cytochrome b to cytochrome c1 (By similarity). Incorporation of UQCRFS1 is the penultimate step in complex III assembly (PubMed:28673544).', 'Component of the ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 (updated: Feb. 10, 2021)
Protein identification was indicated in the following studies:
- Hegedűs and co-workers. (2015) Inconsistencies in the red blood cell membrane proteome analysis: generation of a database for research and diagnostic applications. Database (Oxford) 1-8.
- Wilson and co-workers. (2016) Comparison of the Proteome of Adult and Cord Erythroid Cells, and Changes in the Proteome Following Reticulocyte Maturation. Mol Cell Proteomics. 15(6), 1938-1946.
- D'Alessandro and co-workers. (2017) Red blood cell proteomics update: is there more to discover? Blood Transfus. 15(2), 182-187.
- Chu and co-workers. (2018) Quantitative mass spectrometry of human reticulocytes reveal proteome-wide modifications during maturation. Br J Haematol. 180(1), 118-133.
Methods
The following articles were analysed to gather the proteome content of erythrocytes.
The gene or protein list provided in the studies were processed using the ID mapping API of Uniprot in September 2018. The number of proteins identified and mapped without ambiguity in these studies is indicated below.
Only Swiss-Prot entries (reviewed) were considered for protein evidence assignation.
| Publication | Identification 1 | Uniprot mapping 2 | Not mapped / Obsolete | TrEMBL | Swiss-Prot |
|---|---|---|---|---|---|
| Goodman (2013) | 2289 (gene list) | 2278 | 53 | 20599 | 2269 |
| Lange (2014) | 1234 | 1234 | 7 | 28 | 1224 |
| Hegedus (2015) | 2638 | 2622 | 0 | 235 | 2387 |
| Wilson (2016) | 1658 | 1528 | 170 | 291 | 1068 |
| d'Alessandro (2017) | 1826 | 1817 | 2 | 0 | 1815 |
| Bryk (2017) | 2090 | 2060 | 10 | 108 | 1942 |
| Chu (2018) | 1853 | 1804 | 55 | 362 | 1387 |
1 as available in the article and/or in supplementary material
2 uniprot mapping returns all protein isoforms as one entry
The compilation of older studies can be retrieved from the Red Blood Cell Collection database.
The data and differentiation stages presented below come from the proteomic study and analysis performed by our partners of the GReX consortium, more details are available in their published work.
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| Variant | Description |
|---|---|
| dbSNP:rs8100724 | |
| MC3DN10 |
No binding partner found
Biological Process
Mitochondrial electron transport, ubiquinol to cytochrome c
Mitochondrial respiratory chain complex III assembly
Respiratory electron transport chain
The reference OMIM entry for this protein is 191327
Ubiquinol-cytochrome c reductase, rieske iron-sulfur; uqcrfs1
DESCRIPTION
The Rieske iron-sulfur protein (UQCRFS1) is a nuclear-encoded subunit of the mammalian cytochrome bc1 complex (complex III) of the mitochondrial respiratory chain. This complex, which transfers electrons from ubiquinol to cytochrome c, has 1 mitochondrial-encoded subunit (cytochrome b; MTCYB; 516020) and 9 to 10 subunits encoded by the nuclear genome (summary by Duncan et al., 1994).GENE FUNCTION
Sanchez et al. (2013) found that overexpression of epitope-tagged human LYRM7 (615831) resulted in elevated UQCRFS1 in the mitochondrial soluble fraction and impaired the assembly of mature complex III. Coimmunoprecipitation assays revealed that LYRM7 and UQCRFS1 interacted in a low molecular mass intermediate. Sanchez et al. (2013) concluded that LYRM7 binds and stabilizes UQCRFS1 in the mitochondrial matrix prior to the incorporation of UQCRFS1 into complex III in the inner mitochondrial membrane by BCS1L (603647).MAPPING
Duncan et al. (1994) used in situ hybridization and somatic cell hybrid mapping to localize the UQCRFS1 gene to 2 sites. They considered it likely that the Rieske iron-sulfur protein gene maps to 22q13 since this region hybridized consistently more strongly than did 19q12-q13.1. One may represent a pseudogene. A different conclusion on the mapping was arrived at by Pennacchio et al. (1995). In their hands, mapping by hybridization to a panel of monochromosomal hybrid cell lines indicated that a UQCRFS1 partial cDNA was derived from either chromosome 19 or chromosome 22. By screening a human chromosome 19-specific genomic cosmid library with a probe from this cDNA sequence, they identified a corresponding cosmid. Portions of this cosmid were sequenced directly. The exon, exon:intron junction, and flanking sequences verified that this cosmid, indeed, contained the genomic locus. Fluorescence in situ hybridization localized the cosmid to 19q12. ... More on the omim web site
Feb. 16, 2021: Protein entry updated
Automatic update: Entry updated from uniprot information.
June 30, 2020: Protein entry updated
Automatic update: OMIM entry 191327 was added.
March 3, 2020: Protein entry updated
Automatic update: Entry updated from uniprot information.
Jan. 22, 2020: Protein entry updated
Automatic update: Entry updated from uniprot information.
Oct. 19, 2018: Additional information
Initial protein addition to the database. This entry was referenced in Bryk and co-workers. (2017).