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UniProtKB/Swiss-Prot entry P08067


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name UCRI_YEAST
Primary accession number P08067
Secondary accession numbers None
Integrated into Swiss-Prot on August 1, 1988
Sequence was last modified on August 1, 1988 (Sequence version 1)
Annotations were last modified on    September 2, 2008 (Entry version 100)
Name and origin of the protein
Protein name Cytochrome b-c1 complex subunit Rieske, mitochondrial [Precursor]
Synonyms EC 1.10.2.2
Ubiquinol-cytochrome c reductase iron-sulfur subunit
Rieske iron-sulfur protein
RISP
Complex III subunit 5
Gene name
Name: RIP1
OrderedLocusNames: YEL024W
From
Saccharomyces cerevisiae (Baker's yeast) [TaxID: 4932] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 64665 / S288c / DC5;
PubMed=3036836 [NCBI, ExPASy, EBI, Israel, Japan]
Beckmann J.D., Ljungdahl P.O., Lopez J.L., Trumpower B.L.;
"Isolation and characterization of the nuclear gene encoding the Rieske iron-sulfur protein (RIP1) from Saccharomyces cerevisiae.";
J. Biol. Chem. 262:8901-8909(1987).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND MUTAGENESIS.
PubMed=2645276 [NCBI, ExPASy, EBI, Israel, Japan]
Beckmann J.D., Ljungdahl P.O., Trumpower B.L.;
"Mutational analysis of the mitochondrial Rieske iron-sulfur protein of Saccharomyces cerevisiae. I. Construction of a RIP1 deletion strain and isolation of temperature-sensitive mutants.";
J. Biol. Chem. 264:3713-3722(1989).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204511 / S288c / AB972;
PubMed=9169868 [NCBI, ExPASy, EBI, Israel, Japan]
Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E., Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S., Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X., Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y., Botstein D., Davis R.W.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome V.";
Nature 387:78-81(1997).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
DOI=10.1101/gr.6037607; PubMed=17322287 [NCBI, ExPASy, EBI, Israel, Japan]
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J., Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J.;
"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae.";
Genome Res. 17:536-543(2007).
[5]
MUTAGENESIS.
PubMed=1657998 [NCBI, ExPASy, EBI, Israel, Japan]
Graham L.A., Trumpower B.L.;
"Mutational analysis of the mitochondrial Rieske iron-sulfur protein of Saccharomyces cerevisiae. III. Import, protease processing, and assembly into the cytochrome bc1 complex of iron-sulfur protein lacking the iron-sulfur cluster.";
J. Biol. Chem. 266:22485-22492(1991).
[6]
MUTAGENESIS.
STRAIN=D273-10B/A1;
DOI=10.1016/0022-2836(89)90352-5; PubMed=2538628 [NCBI, ExPASy, EBI, Israel, Japan]
Gatti D.L., Meinhardt S.W., Ohnishi T., Tzagoloff A.;
"Structure and function of the mitochondrial bc1 complex. A mutational analysis of the yeast Rieske iron-sulfur protein.";
J. Mol. Biol. 205:421-435(1989).
[7]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
DOI=10.1016/S0969-2126(00)00152-0; PubMed=10873857 [NCBI, ExPASy, EBI, Israel, Japan]
Hunte C., Koepke J., Lange C., Rossmanith T., Michel H.;
"Structure at 2.3 A resolution of the cytochrome bc1 complex from the yeast Saccharomyces cerevisiae co-crystallized with an antibody Fv fragment.";
Structure 8:669-684(2000).
[8]
X-RAY CRYSTALLOGRAPHY (2.97 ANGSTROMS).
DOI=10.1073/pnas.052704699; PubMed=11880631 [NCBI, ExPASy, EBI, Israel, Japan]
Lange C., Hunte C.;
"Crystal structure of the yeast cytochrome bc1 complex with its bound substrate cytochrome c.";
Proc. Natl. Acad. Sci. U.S.A. 99:2800-2805(2002).
Comments
  • FUNCTION: Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is part of the mitochondrial respiratory chain that generates an electrochemical potential coupled to ATP synthesis. The complex couples electron transfer from ubiquinol to cytochrome c.
  • CATALYTIC ACTIVITY: QH2 + 2 ferricytochrome c = Q + 2 ferrocytochrome c + 2 H+.
  • COFACTOR: Binds 1 2Fe-2S cluster per subunit.
  • SUBUNIT: Fungal cytochrome b-c1 complex contains 10 subunits; 3 respiratory subunits, 2 core proteins and 5 low-molecular weight proteins. Cytochrome b-c1 complex is a homodimer.
  • SUBCELLULAR LOCATION: Mitochondrion.
  • MISCELLANEOUS: The Rieske protein is a high potential 2Fe-2S protein.
  • SIMILARITY: Contains 1 Rieske domain.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M23316; AAA34980.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M24500; AAA34981.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U18530; AAB64501.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY558341; AAS56667.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A29318; A29318.
RefSeq NP_010890.1; -.
3D structure databases
PDB
1EZV; X-ray; 2.30 A; E=31-215.[ExPASy / RCSB / EBI]
1KB9; X-ray; 2.30 A; E=31-215.[ExPASy / RCSB / EBI]
1KYO; X-ray; 2.97 A; E/P=31-215.[ExPASy / RCSB / EBI]
1P84; X-ray; 2.50 A; E=31-215.[ExPASy / RCSB / EBI]
2IBZ; X-ray; 2.30 A; E=31-215.[ExPASy / RCSB / EBI]
3CX5; X-ray; 1.90 A; E/P=31-215.[ExPASy / RCSB / EBI]
3CXH; X-ray; 2.50 A; E/P=31-215.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1EZV; -.
1KB9; -.
1KYO; -.
1P84; -.
2IBZ; -.
3CX5; -.
3CXH; -.
ModBase P08067.
Protein-protein interaction databases
DIP DIP:6616N; -.
IntAct P08067; -.
Organism-specific databases
CYGD YEL024w; -.
SGD S000000750; RIP1.
Yeast-GFP YEL024W.
Gene expression databases
ArrayExpress P08067; -.
GermOnline YEL024W; Saccharomyces cerevisiae.
Ontologies
GO
GO:0005750; Cellular component: mitochondrial respiratory chain complex III (inferred from direct assay from SGD).
GO:0009060; Biological process: aerobic respiration (inferred from mutant phenotype from SGD).
GO:0006122; Biological process: mitochondrial electron transport, ubiquinol to cytochrome c (inferred from direct assay from SGD).
QuickGo view.
Family and domain databases
InterPro IPR014349; Rieske.
IPR005805; Rieske_C.
IPR006317; Rieske_proteo.
IPR005806; Rieske_reg.
IPR004192; UCR_TM_region.
Graphical view of domain structure.
Gene3D G3DSA:2.102.10.10; Rieske_reg; 1.
PANTHER PTHR10134; Rieske; 1.
Pfam PF00355; Rieske; 1.
PF02921; UCR_TM; 1.
Pfam graphical view of domain structure.
PRINTS PR00162; RIESKE.
TIGRFAMs TIGR01416; Rieske_proteo; 1.
PROSITE PS51296; RIESKE; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS P08067.
Proteomic databases
PeptideAtlas P08067; -.
Genome annotation databases
Ensembl YEL024W; Saccharomyces cerevisiae. [Contig view]
GeneID 856689; -.
GenomeReviews U00092_GR; YEL024W.
KEGG sce:YEL024W; -.
NMPDR fig|4932.3.peg.1944; -.
Phylogenomic databases
HOGENOM P08067; -.
Other
LinkHub P08067; -.
ProtoNet P08067.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
2Fe-2S; 3D-structure; Complete proteome; Electron transport; Iron; Iron-sulfur; Metal-binding; Mitochondrion; Oxidoreductase; Respiratory chain; Transit peptide; Transport.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
TRANSIT   1    30  30     Mitochondrion. 
CHAIN   31   215  185     Cytochrome b-c1 complex subunit Rieske, mitochondrial. PRO_0000030683
DOMAIN   123   214  92     Rieske. 
METAL   159   159        Iron-sulfur (2Fe-2S). 
METAL   161   161        Iron-sulfur (2Fe-2S); via pros nitrogen. 
METAL   178   178        Iron-sulfur (2Fe-2S). 
METAL   181   181        Iron-sulfur (2Fe-2S); via pros nitrogen. 
DISULFID   164   180        By similarity. 
MUTAGEN   157   157        G->D: Loss of activity. 
MUTAGEN   159   159        C->S: Loss of activity. 
MUTAGEN   161   161        H->R: Loss of activity. 
MUTAGEN   163   163        G->D: Partial loss of activity. 
MUTAGEN   164   164        C->S: Loss of activity. 
MUTAGEN   166   166        P->L: Partial loss of activity. 
MUTAGEN   178   178        C->S,Y: Loss of activity. 
MUTAGEN   179   179        P->L: Partial loss of activity. 
MUTAGEN   180   180        C->S: Loss of activity. 
MUTAGEN   181   181        H->R: Loss of activity. 
MUTAGEN   183   183        S->L: Loss of activity. 
MUTAGEN   184   184        H->R: No loss of activity. 
MUTAGEN   186   186        D->N: Partial loss of activity. 
MUTAGEN   189   189        G->D: Loss of activity. 
MUTAGEN   195   195        P->S: No loss of activity. 
MUTAGEN   196   196        A->T: No loss of activity. 
MUTAGEN   203   203        P->S: Loss of activity. 
TURN   40    42  3      
STRAND   46    48  3      
HELIX   51    80  30      
HELIX   86    88  3      
STRAND   94    97  4      
HELIX   98   100  3      
STRAND   106   111  6      
STRAND   114   120  7      
HELIX   123   130  8      
HELIX   134   136  3      
HELIX   143   146  4      
STRAND   152   156  5      
TURN   160   162  3      
STRAND   174   178  5      
TURN   179   182  4      
STRAND   183   185  3      
STRAND   191   195  5      
STRAND   205   208  4      
STRAND   211   214  4      
Sequence information
Length: 215 AA [This is the length of the unprocessed precursor] Molecular weight: 23365 Da [This is the MW of the unprocessed precursor] CRC64: 21981BD8492E86F3 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MLGIRSSVKT CFKPMSLTSK RLISQSLLAS KSTYRTPNFD DVLKENNDAD KGRSYAYFMV 

        70         80         90        100        110        120 
GAMGLLSSAG AKSTVETFIS SMTATADVLA MAKVEVNLAA IPLGKNVVVK WQGKPVFIRH 

       130        140        150        160        170        180 
RTPHEIQEAN SVDMSALKDP QTDADRVKDP QWLIMLGICT HLGCVPIGEA GDFGGWFCPC 

       190        200        210 
HGSHYDISGR IRKGPAPLNL EIPAYEFDGD KVIVG 

P08067 in FASTA format

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