P08067 · UCRI_YEAST

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).

Miscellaneous

The Rieske protein is a high potential 2Fe-2S protein.

Catalytic activity

Cofactor

[2Fe-2S] cluster (UniProtKB | Rhea| CHEBI:190135 )

Note: Binds 1 [2Fe-2S] cluster per subunit.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site159[2Fe-2S] cluster (UniProtKB | ChEBI)
Binding site161[2Fe-2S] cluster (UniProtKB | ChEBI)
Binding site178[2Fe-2S] cluster (UniProtKB | ChEBI)
Binding site181[2Fe-2S] cluster (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentmitochondrial inner membrane
Cellular Componentmitochondrial respiratory chain complex III
Cellular Componentmitochondrion
Molecular Function2 iron, 2 sulfur cluster binding
Molecular Functionmetal ion binding
Molecular Functionoxidoreductase activity
Molecular Functionubiquinol-cytochrome-c reductase activity
Biological Processaerobic respiration
Biological Processcellular respiration
Biological Processmitochondrial electron transport, ubiquinol to cytochrome c

Keywords

Enzyme and pathway databases

Protein family/group databases

    • 3.D.3.3.1the proton-translocating quinol:cytochrome c reductase (qcr) superfamily

Names & Taxonomy

Protein names

  • Recommended name
    Cytochrome b-c1 complex subunit Rieske, mitochondrial
  • EC number
  • Alternative names
    • Complex III subunit 5
    • Rieske iron-sulfur protein (RISP)
    • Ubiquinol-cytochrome c oxidoreductase iron-sulfur subunit

Gene names

    • Name
      RIP1
    • Ordered locus names
      YEL024W

Organism names

Accessions

  • Primary accession
    P08067
  • Secondary accessions
    • D3DLM4

Proteomes

Organism-specific databases

Subcellular Location

Features

Showing features for topological domain, transmembrane.

TypeIDPosition(s)Description
Topological domain31-50Mitochondrial matrix
Transmembrane51-80Helical
Topological domain81-215Mitochondrial intermembrane

Keywords

Phenotypes & Variants

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis157Loss of activity.
Mutagenesis159Loss of activity.
Mutagenesis161Loss of activity.
Mutagenesis163Partial loss of activity.
Mutagenesis164Loss of activity.
Mutagenesis166Partial loss of activity.
Mutagenesis178Loss of activity.
Mutagenesis179Partial loss of activity.
Mutagenesis180Loss of activity.
Mutagenesis181Loss of activity.
Mutagenesis183Loss of activity.
Mutagenesis184No loss of activity.
Mutagenesis186Partial loss of activity.
Mutagenesis189Loss of activity.
Mutagenesis195No loss of activity.
Mutagenesis196No loss of activity.
Mutagenesis203Loss of activity.

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.

Go to variant viewer

PTM/Processing

Features

Showing features for transit peptide, propeptide, chain, disulfide bond.

TypeIDPosition(s)Description
Transit peptide1-22Mitochondrion
PropeptidePRO_000044919523-30Removed in mature form
ChainPRO_000003068331-215Cytochrome b-c1 complex subunit Rieske, mitochondrial
Disulfide bond164↔180

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

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).
View interactors in UniProtKB
View CPX-567 in Complex Portal

Protein-protein interaction databases

Miscellaneous

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region90-93Hinge
Domain123-214Rieske

Sequence similarities

Belongs to the Rieske iron-sulfur protein family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    215
  • Mass (Da)
    23,365
  • Last updated
    1988-08-01 v1
  • Checksum
    21981BD8492E86F3
MLGIRSSVKTCFKPMSLTSKRLISQSLLASKSTYRTPNFDDVLKENNDADKGRSYAYFMVGAMGLLSSAGAKSTVETFISSMTATADVLAMAKVEVNLAAIPLGKNVVVKWQGKPVFIRHRTPHEIQEANSVDMSALKDPQTDADRVKDPQWLIMLGICTHLGCVPIGEAGDFGGWFCPCHGSHYDISGRIRKGPAPLNLEIPAYEFDGDKVIVG

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
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

Genome annotation databases

Similar Proteins

Disclaimer

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