Reviewed, UniProtKB/Swiss-Prot P08067 (UCRI_YEAST)

Names and origin

Protein names

Recommended name:
    Cytochrome b-c1 complex subunit Rieske, mitochondrial
    EC=1.10.2.2
Alternative name(s):
    Ubiquinol-cytochrome c reductase iron-sulfur subunit
    Rieske iron-sulfur protein
      Short name=RISP
    Complex III subunit 5

Gene names

Name:	RIP1
Ordered Locus Names:	YEL024W

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	215 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (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 structure	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.
Sequence similarities	Contains 1 Rieske domain.

Ontologies

Keywords
Biological process	Electron transport Respiratory chain Transport
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	2Fe-2S Iron Iron-sulfur Metal-binding
Molecular function	Oxidoreductase
PTM	Disulfide bond
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	aerobic respiration Ref.1 Inferred from mutant phenotype. Source: SGD mitochondrial electron transport, ubiquinol to cytochrome c Ref.1 Inferred from direct assay. Source: SGD transport Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	mitochondrial respiratory chain complex III Ref.1 Ref.7 Inferred from direct assay. Source: SGD
Molecular function	2 iron, 2 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW ubiquinol-cytochrome-c reductase activity Ref.1 Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – 30

30

Mitochondrion

Chain

31 – 215

185

Cytochrome b-c1 complex subunit Rieske, mitochondrial

PRO_0000030683

Regions

Domain

123 – 214

92

Rieske

Sites

Metal binding

159

1

Iron-sulfur (2Fe-2S)

Metal binding

161

1

Iron-sulfur (2Fe-2S); via pros nitrogen

Metal binding

178

1

Iron-sulfur (2Fe-2S)

Metal binding

181

1

Iron-sulfur (2Fe-2S); via pros nitrogen

Amino acid modifications

Disulfide bond

164 ↔ 180

By similarity

Experimental info

Mutagenesis

157

1

G → D: Loss of activity.

Mutagenesis

159

1

C → S: Loss of activity.

Mutagenesis

161

1

H → R: Loss of activity.

Mutagenesis

163

1

G → D: Partial loss of activity.

Mutagenesis

164

1

C → S: Loss of activity.

Mutagenesis

166

1

P → L: Partial loss of activity.

Mutagenesis

178

1

C → S or Y: Loss of activity.

Mutagenesis

179

1

P → L: Partial loss of activity.

Mutagenesis

180

1

C → S: Loss of activity.

Mutagenesis

181

1

H → R: Loss of activity.

Mutagenesis

183

1

S → L: Loss of activity.

Mutagenesis

184

1

H → R: No loss of activity.

Mutagenesis

186

1

D → N: Partial loss of activity.

Mutagenesis

189

1

G → D: Loss of activity.

Mutagenesis

195

1

P → S: No loss of activity.

Mutagenesis

196

1

A → T: No loss of activity.

Mutagenesis

203

1

P → S: Loss of activity.

Secondary structure

1

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215

Helix Strand Turn

Details...

Turn

40 – 42

3

Beta strand

46 – 48

3

Helix

51 – 80

30

Helix

86 – 88

3

Beta strand

94 – 97

4

Helix

98 – 100

3

Beta strand

106 – 111

6

Beta strand

114 – 120

7

Helix

123 – 130

8

Helix

134 – 136

3

Helix

143 – 146

4

Beta strand

152 – 156

5

Turn

160 – 162

3

Beta strand

174 – 178

5

Turn

179 – 182

4

Beta strand

183 – 185

3

Beta strand

191 – 195

5

Beta strand

205 – 208

4

Beta strand

211 – 214

4

Sequences

	Sequence		Length	Mass (Da)
	P08067-1 [UniParc]. Last modified August 1, 1988. Version 1. Checksum: 21981BD8492E86F3	FASTA	215	23,365
	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

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Isolation and characterization of the nuclear gene encoding the Rieske iron-sulfur protein (RIP1) from Saccharomyces cerevisiae." Beckmann J.D., Ljungdahl P.O., Lopez J.L., Trumpower B.L. J. Biol. Chem. 262:8901-8909(1987) [PubMed: 3036836] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 64665 / S288c / DC5.
[2]	"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." Beckmann J.D., Ljungdahl P.O., Trumpower B.L. J. Biol. Chem. 264:3713-3722(1989) [PubMed: 2645276] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], MUTAGENESIS.
[3]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome V." 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. Nature 387:78-81(1997) [PubMed: 9169868] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[4]	"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae." 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. Genome Res. 17:536-543(2007) [PubMed: 17322287] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[5]	"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." Graham L.A., Trumpower B.L. J. Biol. Chem. 266:22485-22492(1991) [PubMed: 1657998] [Abstract] Cited for: MUTAGENESIS.
[6]	"Structure and function of the mitochondrial bc1 complex. A mutational analysis of the yeast Rieske iron-sulfur protein." Gatti D.L., Meinhardt S.W., Ohnishi T., Tzagoloff A. J. Mol. Biol. 205:421-435(1989) [PubMed: 2538628] [Abstract] Cited for: MUTAGENESIS. Strain: D273-10B/A1.
[7]	"Structure at 2.3 A resolution of the cytochrome bc1 complex from the yeast Saccharomyces cerevisiae co-crystallized with an antibody Fv fragment." Hunte C., Koepke J., Lange C., Rossmanith T., Michel H. Structure 8:669-684(2000) [PubMed: 10873857] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
[8]	"Crystal structure of the yeast cytochrome bc1 complex with its bound substrate cytochrome c." Lange C., Hunte C. Proc. Natl. Acad. Sci. U.S.A. 99:2800-2805(2002) [PubMed: 11880631] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.97 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

M23316 Genomic DNA. Translation: AAA34980.1.
M24500 Genomic DNA. Translation: AAA34981.1.
U18530 Genomic DNA. Translation: AAB64501.1.
AY558341 Genomic DNA. Translation: AAS56667.1.

PIR

A29318.

RefSeq

NP_010890.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1EZV	X-ray	2.30	E	31-215	[»]
1KB9	X-ray	2.30	E	31-215	[»]
1KYO	X-ray	2.97	E/P	31-215	[»]
1P84	X-ray	2.50	E	31-215	[»]
2IBZ	X-ray	2.30	E	31-215	[»]
3CX5	X-ray	1.90	E/P	31-215	[»]
3CXH	X-ray	2.50	E/P	31-215	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:6616N.

IntAct

P08067. 3 interactions.

STRING

P08067.

Protein family/group databases

TCDB

3.D.3.3.1. proton-translocating quinol:cytochrome c reductase (QCR) superfamily.
9.A.14.1.1. nuclear pore complex (NPC) family.

Proteomic databases

PeptideAtlas

P08067.

Genome annotation databases

Ensembl

YEL024W; YEL024W; YEL024W; Saccharomyces cerevisiae. [Genome view]

GeneID

856689.

KEGG

sce:YEL024W.

NMPDR

fig|4932.3.peg.1944.

Organism-specific databases

CYGD

YEL024w.

SGD

S000000750. RIP1.

Phylogenomic databases

HOGENOM

P08067.

OMA

KGRSYAY

OrthoDB

EOG9MCZGN

Enzyme and pathway databases

BRENDA

1.10.2.2. 250.

Gene expression databases

ArrayExpress

P08067.

Genevestigator

P08067.

GermOnline

YEL024W. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR017941. Rieske_2Fe-2S.
IPR014349. Rieske_Fe-S_prot.
IPR005805. Rieske_Fe-S_prot_C.
IPR006317. Ubiquinol_cyt_c_Rdtase_Fe-S-su.
IPR004192. Ubiquinol_cyt_Rdtase_TM.
[Graphical view]

Gene3D

G3DSA:2.102.10.10. Rieske_reg. 1 hit.

PANTHER

PTHR10134. Rieske. 1 hit.

Pfam

PF00355. Rieske. 1 hit.
PF02921. UCR_TM. 1 hit.
[Graphical view]

PRINTS

PR00162. RIESKE.

TIGRFAMs

TIGR01416. Rieske_proteo. 1 hit.

PROSITE

PS51296. RIESKE. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

982730.

Entry information

Entry name

UCRI_YEAST

Accession

Primary (citable) accession number: P08067

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1988
Last sequence update:	August 1, 1988
Last modified:	November 24, 2009
This is version 113 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)