P08067 · UCRI_YEAST
- ProteinCytochrome b-c1 complex subunit Rieske, mitochondrial
- GeneRIP1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids215 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit transmembrane complex that is part of the mitochondrial electron transport chain which drives oxidative phosphorylation. 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 (Probable). The Rieske protein is a catalytic core subunit containing a [2Fe-2S] iron-sulfur cluster (PubMed:18390544).
It cycles between 2 conformational states during catalysis to transfer electrons from the quinol bound in the Q0 site in cytochrome b (COB) to cytochrome c1 (CYT1) (Probable) (PubMed:1657998, PubMed:2538628).
It cycles between 2 conformational states during catalysis to transfer electrons from the quinol bound in the Q0 site in cytochrome b (COB) to cytochrome c1 (CYT1) (Probable) (PubMed:1657998, PubMed:2538628).
Miscellaneous
The Rieske protein is a high potential 2Fe-2S protein.
Catalytic activity
- a quinol + 2 Fe(III)-[cytochrome c](out) = a quinone + 2 Fe(II)-[cytochrome c](out) + 2 H+(out)
Cofactor
Note: Binds 1 [2Fe-2S] cluster per subunit.
Features
Showing features for binding site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | mitochondrial inner membrane | |
Cellular Component | mitochondrial respiratory chain complex III | |
Cellular Component | mitochondrion | |
Molecular Function | 2 iron, 2 sulfur cluster binding | |
Molecular Function | metal ion binding | |
Molecular Function | oxidoreductase activity | |
Molecular Function | ubiquinol-cytochrome-c reductase activity | |
Biological Process | aerobic respiration | |
Biological Process | cellular respiration | |
Biological Process | mitochondrial electron transport, ubiquinol to cytochrome c |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameCytochrome b-c1 complex subunit Rieske, mitochondrial
- EC number
- Alternative names
Gene names
Organism names
- Strains
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Saccharomycotina > Saccharomycetes > Saccharomycetales > Saccharomycetaceae > Saccharomyces
Accessions
- Primary accessionP08067
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Mitochondrion inner membrane ; Single-pass membrane protein
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 31-50 | Mitochondrial matrix | ||||
Sequence: KSTYRTPNFDDVLKENNDAD | ||||||
Transmembrane | 51-80 | Helical | ||||
Sequence: KGRSYAYFMVGAMGLLSSAGAKSTVETFIS | ||||||
Topological domain | 81-215 | Mitochondrial intermembrane | ||||
Sequence: SMTATADVLAMAKVEVNLAAIPLGKNVVVKWQGKPVFIRHRTPHEIQEANSVDMSALKDPQTDADRVKDPQWLIMLGICTHLGCVPIGEAGDFGGWFCPCHGSHYDISGRIRKGPAPLNLEIPAYEFDGDKVIVG |
Keywords
- Cellular component
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 157 | Loss of activity. | ||||
Sequence: G → D | ||||||
Mutagenesis | 159 | Loss of activity. | ||||
Sequence: C → S | ||||||
Mutagenesis | 161 | Loss of activity. | ||||
Sequence: H → R | ||||||
Mutagenesis | 163 | Partial loss of activity. | ||||
Sequence: G → D | ||||||
Mutagenesis | 164 | Loss of activity. | ||||
Sequence: C → S | ||||||
Mutagenesis | 166 | Partial loss of activity. | ||||
Sequence: P → L | ||||||
Mutagenesis | 178 | Loss of activity. | ||||
Sequence: C → S or Y | ||||||
Mutagenesis | 179 | Partial loss of activity. | ||||
Sequence: P → L | ||||||
Mutagenesis | 180 | Loss of activity. | ||||
Sequence: C → S | ||||||
Mutagenesis | 181 | Loss of activity. | ||||
Sequence: H → R | ||||||
Mutagenesis | 183 | Loss of activity. | ||||
Sequence: S → L | ||||||
Mutagenesis | 184 | No loss of activity. | ||||
Sequence: H → R | ||||||
Mutagenesis | 186 | Partial loss of activity. | ||||
Sequence: D → N | ||||||
Mutagenesis | 189 | Loss of activity. | ||||
Sequence: G → D | ||||||
Mutagenesis | 195 | No loss of activity. | ||||
Sequence: P → S | ||||||
Mutagenesis | 196 | No loss of activity. | ||||
Sequence: A → T | ||||||
Mutagenesis | 203 | Loss of activity. | ||||
Sequence: P → S |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 1 variant from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for transit peptide, propeptide, chain, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transit peptide | 1-22 | Mitochondrion | ||||
Sequence: MLGIRSSVKTCFKPMSLTSKRL | ||||||
Propeptide | PRO_0000449195 | 23-30 | Removed in mature form | |||
Sequence: ISQSLLAS | ||||||
Chain | PRO_0000030683 | 31-215 | Cytochrome b-c1 complex subunit Rieske, mitochondrial | |||
Sequence: KSTYRTPNFDDVLKENNDADKGRSYAYFMVGAMGLLSSAGAKSTVETFISSMTATADVLAMAKVEVNLAAIPLGKNVVVKWQGKPVFIRHRTPHEIQEANSVDMSALKDPQTDADRVKDPQWLIMLGICTHLGCVPIGEAGDFGGWFCPCHGSHYDISGRIRKGPAPLNLEIPAYEFDGDKVIVG | ||||||
Disulfide bond | 164↔180 | |||||
Sequence: CVPIGEAGDFGGWFCPC |
Post-translational modification
Processed by both the mitochondrial processing peptidase (MPP) and the mitochondrial intermediate protease (MIP). Initially, MPP removes 22 amino acids from the newly imported precursor in the mitochondrial matrix. This proteolytic processing is then followed by a second proteolytic cleavage by MIP, which removes an octapeptide to generate mature-sized RIP1.
Keywords
- PTM
Proteomic databases
Interaction
Subunit
Component of the ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII), a multisubunit enzyme composed of 10 subunits. The complex is composed of 3 respiratory subunits cytochrome b (COB), cytochrome c1 (CYT1) and Rieske protein (RIP1), 2 core protein subunits COR1 and QCR2, and 5 low-molecular weight protein subunits QCR6, QCR7, QCR8, QCR9 and QCR10 (PubMed:10873857, PubMed:11880631, PubMed:1657998, PubMed:18390544, PubMed:2538628, PubMed:30598554).
The complex exists as an obligatory dimer and forms supercomplexes (SCs) in the inner mitochondrial membrane with a monomer or a dimer of cytochrome c oxidase (complex IV, CIV), resulting in 2 different assemblies (supercomplexes III2IV and III2IV2) (PubMed:10764779, PubMed:10775262, PubMed:30598554, PubMed:30598556).
RIP1 interacts with QCR10 on the intermembrane space (IMS) side, and with QCR9 (PubMed:30598554, PubMed:30598556).
The complex exists as an obligatory dimer and forms supercomplexes (SCs) in the inner mitochondrial membrane with a monomer or a dimer of cytochrome c oxidase (complex IV, CIV), resulting in 2 different assemblies (supercomplexes III2IV and III2IV2) (PubMed:10764779, PubMed:10775262, PubMed:30598554, PubMed:30598556).
RIP1 interacts with QCR10 on the intermembrane space (IMS) side, and with QCR9 (PubMed:30598554, PubMed:30598556).
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 90-93 | Hinge | ||||
Sequence: AMAK | ||||||
Domain | 123-214 | Rieske | ||||
Sequence: PHEIQEANSVDMSALKDPQTDADRVKDPQWLIMLGICTHLGCVPIGEAGDFGGWFCPCHGSHYDISGRIRKGPAPLNLEIPAYEFDGDKVIV |
Sequence similarities
Belongs to the Rieske iron-sulfur protein family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length215
- Mass (Da)23,365
- Last updated1988-08-01 v1
- Checksum21981BD8492E86F3
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
M23316 EMBL· GenBank· DDBJ | AAA34980.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M24500 EMBL· GenBank· DDBJ | AAA34981.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U18530 EMBL· GenBank· DDBJ | AAB64501.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY558341 EMBL· GenBank· DDBJ | AAS56667.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BK006939 EMBL· GenBank· DDBJ | DAA07628.1 EMBL· GenBank· DDBJ | Genomic DNA |