P08067 (UCRI_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Cytochrome b-c1 complex subunit Rieske, mitochondrial
EC=1.10.2.2

Alternative name(s):
Complex III subunit 5
Rieske iron-sulfur protein
Short name=RISP
Ubiquinol-cytochrome c reductase iron-sulfur subunit

Gene names

Name:	RIP1
Ordered Locus Names:	YEL024W

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

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 a 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 inner membrane; Single-pass membrane protein Ref.10.
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	Membrane Mitochondrion Mitochondrion inner membrane
Domain	Transit peptide Transmembrane Transmembrane helix
Ligand	2Fe-2S Iron Iron-sulfur Metal-binding
Molecular function	Oxidoreductase
PTM	Disulfide bond
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	aerobic respiration Inferred from mutant phenotype Ref.1. Source: SGD mitochondrial electron transport, ubiquinol to cytochrome c Inferred from direct assay Ref.1. Source: SGD
Cellular_component	mitochondrial respiratory chain complex III Inferred from direct assay Ref.8Ref.1. Source: SGD
Molecular_function	2 iron, 2 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW ubiquinol-cytochrome-c reductase activity 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

Transmembrane

49 – 82

34

Helical

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

Ref.10

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

Turn

144 – 146

3

Beta strand

152 – 156

5

Turn

160 – 162

3

Beta strand

167 – 170

4

Turn

171 – 174

4

Beta strand

175 – 178

4

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 [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[4]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[5]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[6]	"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] [Europe PMC] [Abstract] Cited for: MUTAGENESIS.
[7]	"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] [Europe PMC] [Abstract] Cited for: MUTAGENESIS. Strain: D273-10B/A1.
[8]	"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] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
[9]	"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] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.97 ANGSTROMS).
[10]	"Structure of complex III with bound cytochrome c in reduced state and definition of a minimal core interface for electron transfer." Solmaz S.R., Hunte C. J. Biol. Chem. 283:17542-17549(2008) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 31-215 IN THE BC1 COMPLEX, DISULFIDE BOND, SUBCELLULAR LOCATION.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M23316 Genomic DNA. Translation: AAA34980.1.
M24500 Genomic DNA. Translation: AAA34981.1.
U18530 Genomic DNA. Translation: AAB64501.1.
AY558341 Genomic DNA. Translation: AAS56667.1.
BK006939 Genomic DNA. Translation: DAA07628.1.

PIR

A29318.

RefSeq

NP_010890.3. NM_001178839.3.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P08067.

SMR

P08067. Positions 31-215.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-6616N.

IntAct

P08067. 3 interactions.

MINT

MINT-696377.

STRING

4932.YEL024W.

Proteomic databases

PaxDb

P08067.

PeptideAtlas

P08067.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YEL024W; YEL024W; YEL024W.

GeneID

856689.

KEGG

sce:YEL021W.
sce:YEL024W.

Organism-specific databases

CYGD

YEL024w.

SGD

S000000750. RIP1.

Phylogenomic databases

eggNOG

COG0723.

GeneTree

ENSGT00390000001014.

HOGENOM

HOG000255193.

KO

K00411.
K01591.

OMA

PHQYIDD.

OrthoDB

EOG46T69W.

Gene expression databases

Genevestigator

P08067.

GermOnline

YEL024W. Saccharomyces cerevisiae.

Family and domain databases

Gene3D

1.20.5.270. 1 hit.
2.102.10.10. 1 hit.

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]

PANTHER

PTHR10134. PTHR10134. 1 hit.

Pfam

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

PRINTS

PR00162. RIESKE.

SUPFAM

SSF50022. Rieske_dom. 1 hit.

TIGRFAMs

TIGR01416. Rieske_proteo. 1 hit.

PROSITE

PS51296. RIESKE. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P08067.

NextBio

982730.

Entry information

Entry name

UCRI_YEAST

Accession

Primary (citable) accession number: P08067
Secondary accession number(s): D3DLM4

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1988
Last sequence update:	August 1, 1988
Last modified:	May 1, 2013
This is version 145 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program