Cytochrome b-c1 complex subunit Rieske, mitochondrial precursor

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P13272 (UCRI_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 127. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

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
Cytochrome b-c1 complex subunit 5
Rieske iron-sulfur protein
Short name=RISP
Ubiquinol-cytochrome c reductase iron-sulfur subunit

Cleaved into the following chain:

Cytochrome b-c1 complex subunit 11
Alternative name(s):
Complex III subunit IX
Ubiquinol-cytochrome c reductase 8 kDa protein

Gene names

Name:

UQCRFS1

Organism

Bos taurus (Bovine) [Reference proteome]

Taxonomic identifier

9913 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length	274 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 transit peptide of the Rieske protein seems to form part of the bc1 complex and is considered to be the subunit 11/IX of that complex.
Catalytic activity	QH₂ + 2 ferricytochrome c = Q + 2 ferrocytochrome c + 2 H⁺.
Cofactor	Binds 1 2Fe-2S cluster per subunit.
Subunit structure	The bc1 complex contains 11 subunits: 3 respiratory subunits (cytochrome b, cytochrome c1 and Rieske/UQCRFS1), 2 core proteins (UQCRC1/QCR1 and UQCRC2/QCR2) and 6 low-molecular weight proteins (UQCRH/QCR6, UQCRB/QCR7, UQCRQ/QCR8, UQCR10/QCR9, UQCR11/QCR10 and a cleavage product of Rieske/UQCRFS1).
Subcellular location	Mitochondrion inner membrane; Single-pass membrane protein.
Miscellaneous	The Rieske protein is a high potential 2Fe-2S protein.
Sequence similarities	Contains 1 Rieske domain.
Sequence caution	The sequence AAA30515.1 differs from that shown. Reason: Frameshift at several positions.

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 Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW mitochondrial inner membrane Inferred from sequence or structural similarity. Source: AgBase respiratory chain Inferred from electronic annotation. Source: UniProtKB-KW
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

Chain

1 – 78

Cytochrome b-c1 complex subunit 11

PRO_0000030659

Transit peptide

1 – 78

Mitochondrion Ref.5 Ref.9

Chain

79 – 274

196

Cytochrome b-c1 complex subunit Rieske, mitochondrial

PRO_0000030660

Regions

Transmembrane

103 – 140

Helical

Domain

187 – 272

Rieske

Sites

Metal binding

217

Iron-sulfur (2Fe-2S)

Metal binding

219

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

Metal binding

236

Iron-sulfur (2Fe-2S)

Metal binding

239

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

Amino acid modifications

Disulfide bond

222 ↔ 238

Ref.6

Experimental info

Sequence conflict

150

S → A AA sequence Ref.5

Sequence conflict

269

D → G AA sequence Ref.5

Secondary structure

274

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P13272 [UniParc].

Last modified February 1, 1996. Version 3.
Checksum: 7C5FC17D2A0DD1C9
Show »

FASTA

274

29,547

        10         20         30         40         50         60 
MLSVAARSGP FAPVLSATSR GVAGALRPLV QAAVPATSES PVLDLKRSVL CRESLRGQAA 

        70         80         90        100        110        120 
GRPLVASVSL NVPASVRYSH TDIKVPDFSD YRRPEVLDST KSSKESSEAR KGFSYLVTAT 

       130        140        150        160        170        180 
TTVGVAYAAK NVVSQFVSSM SASADVLAMS KIEIKLSDIP EGKNMAFKWR GKPLFVRHRT 

       190        200        210        220        230        240 
KKEIDQEAAV EVSQLRDPQH DLERVKKPEW VILIGVCTHL GCVPIANAGD FGGYYCPCHG 

       250        260        270 
SHYDASGRIR KGPAPLNLEV PSYEFTSDDM VIVG

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and sequencing of a cDNA encoding the Rieske iron-sulfur protein of bovine heart mitochondrial ubiquinol-cytochrome c reductase." Usui S., Yu L., Yu C.-A. Biochem. Biophys. Res. Commun. 167:575-579(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Heart.
[2]	"The mitochondrial targeting presequence of the Rieske iron-sulfur protein is processed in a single step after insertion into the cytochrome bc1 complex in mammals and retained as a subunit in the complex." Brandt U., Yu L., Yu C.-A., Trumpower B.L. J. Biol. Chem. 268:8387-8390(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], SEQUENCE REVISION. Tissue: Heart.
[3]	NIH - Mammalian Gene Collection (MGC) project Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Crossbred X Angus and Hereford. Tissue: Fetal brain, Fetal cerebellum and Liver.
[4]	"Isolation and amino acid sequence of the 8 kDa DCCD-binding protein of beef heart ubiquinol:cytochrome c reductase." Borchart U., Machleidt W., Schagger H., Link T.A., von Jagow G. FEBS Lett. 191:125-130(1985) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-78. Tissue: Heart.
[5]	"Isolation and amino acid sequence of the 'Rieske' iron sulfur protein of beef heart ubiquinol:cytochrome c reductase." Schaegger H., Borchart U., Machleidt W., Link T.A., von Jagow G. FEBS Lett. 219:161-168(1987) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 79-274.
[6]	"Structure of a water soluble fragment of the 'Rieske' iron-sulfur protein of the bovine heart mitochondrial cytochrome bc1 complex determined by MAD phasing at 1.5-A resolution." Iwata S., Saynovits M., Link T.A., Michel H. Structure 4:567-579(1996) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 148-274.
[7]	"Crystal structure of the cytochrome bc1 complex from bovine heart mitochondria." Xia D., Yu C.A., Kim H., Xia J.Z., Kachurin A.M., Zhang L., Yu L., Deisenhofer J. Science 277:60-66(1997) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
[8]	Erratum Xia D., Yu C.A., Kim H., Xia J.Z., Kachurin A.M., Zhang L., Yu L., Deisenhofer J. Science 278:2037-2037(1997)
[9]	"Complete structure of the 11-subunit bovine mitochondrial cytochrome bc1 complex." Iwata S., Lee J.W., Okada K., Lee J.K., Iwata M., Rasmussen B., Link T.A., Ramaswamy S., Jap B.K. Science 281:64-71(1998) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
[10]	"The crystal structure of mitochondrial cytochrome bc1 in complex with famoxadone: the role of aromatic-aromatic interaction in inhibition." Gao X., Wen X., Yu C., Esser L., Tsao S., Quinn B., Zhang L., Yu L., Xia D. Biochemistry 41:11692-11702(2002) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS).
[11]	"Crystallographic studies of quinol oxidation site inhibitors: a modified classification of inhibitors for the cytochrome bc(1) complex." Esser L., Quinn B., Li Y.F., Zhang M., Elberry M., Yu L., Yu C.A., Xia D. J. Mol. Biol. 341:281-302(2004) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.69 ANGSTROMS).
[12]	"Binding of the respiratory chain inhibitor antimycin to the mitochondrial bc1 complex: a new crystal structure reveals an altered intramolecular hydrogen-bonding pattern." Huang L.S., Cobessi D., Tung E.Y., Berry E.A. J. Mol. Biol. 351:573-597(2005) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
[13]	"Surface-modulated motion switch: capture and release of iron-sulfur protein in the cytochrome bc1 complex." Esser L., Gong X., Yang S., Yu L., Yu C.A., Xia D. Proc. Natl. Acad. Sci. U.S.A. 103:13045-13050(2006) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.26 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M34336 mRNA. Translation: AAA30515.1. Sequence problems.
S58789 mRNA. Translation: AAB26197.1.
BC115994 mRNA. Translation: AAI15995.1.
BC133620 mRNA. Translation: AAI33621.1.
BC133632 mRNA. Translation: AAI33633.1.

IPI

IPI00688782.

PIR

A34660. A46063.

RefSeq

NP_777238.1. NM_174813.2.

UniGene

Bt.265.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1BE3	X-ray	3.00	E	79-274	[»]
			I	1-78	[»]
1BGY	X-ray	3.00	E/Q	79-274	[»]
			I/U	1-78	[»]
1L0L	X-ray	2.35	E	79-274	[»]
			I	1-78	[»]
1L0N	X-ray	2.60	E	79-274	[»]
			I	1-78	[»]
1NTK	X-ray	2.60	E	79-274	[»]
			I	1-57	[»]
1NTM	X-ray	2.40	E	79-274	[»]
			I	1-57	[»]
1NTZ	X-ray	2.60	E	79-274	[»]
			I	1-57	[»]
1NU1	X-ray	3.20	E	79-274	[»]
			I	1-57	[»]
1PP9	X-ray	2.10	E/R	79-274	[»]
			I/V	1-78	[»]
1PPJ	X-ray	2.10	E/R	79-274	[»]
			I/V	1-78	[»]
1QCR	X-ray	2.70	E	79-274	[»]
			I	21-48	[»]
1RIE	X-ray	1.50	A	146-274	[»]
1SQB	X-ray	2.69	E	79-274	[»]
			I	1-78	[»]
1SQP	X-ray	2.70	E	79-274	[»]
			I	1-78	[»]
1SQQ	X-ray	3.00	E	79-274	[»]
			I	1-78	[»]
1SQV	X-ray	2.85	E	79-274	[»]
			I	1-78	[»]
1SQX	X-ray	2.60	E	79-274	[»]
			I	1-78	[»]
2A06	X-ray	2.10	E/R	79-274	[»]
			I/V	1-78	[»]
2FYU	X-ray	2.26	E	79-274	[»]
			I	1-78	[»]
2YBB	electron microscopy	19.00	E/e	79-274	[»]
			I/i	14-78	[»]

DisProt

DP00019.

ProteinModelPortal

P13272.

SMR

P13272. Positions 1-57, 79-274.

ModBase

Search...

Protein-protein interaction databases

IntAct

P13272. 3 interactions.

Protein family/group databases

TCDB

3.D.3.2.1. proton-translocating quinol:cytochrome c reductase (QCR) superfamily.

Proteomic databases

PRIDE

P13272.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

287020.

KEGG

bta:287020.

Organism-specific databases

CTD

7386.

Phylogenomic databases

HOVERGEN

HBG001040.

K00411.

Family and domain databases

Gene3D

1.20.5.270. 1 hit.
2.102.10.10. 1 hit.

InterPro

IPR011070. Globular_prot_asu/bsu.
IPR017941. Rieske_2Fe-2S.
IPR014349. Rieske_Fe-S_prot.
IPR005805. Rieske_Fe-S_prot_C.
IPR015248. Ubiqinol_cyt_c_Rdtase_N.
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.
PF09165. Ubiq-Cytc-red_N. 1 hit.
PF02921. UCR_TM. 1 hit.
[Graphical view]

PRINTS

PR00162. RIESKE.

SUPFAM

SSF56568. AlphaBeta_subunt. 1 hit.
SSF50022. Rieske_dom. 1 hit.

TIGRFAMs

TIGR01416. Rieske_proteo. 1 hit.

PROSITE

PS51296. RIESKE. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P13272.

NextBio

20806543.

Entry information

Entry name

UCRI_BOVIN

Accession

Primary (citable) accession number: P13272
Secondary accession number(s): A3KN53, P07588, Q1LZH6

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1988
Last sequence update:	February 1, 1996
Last modified:	May 1, 2013
This is version 127 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Cleaved into the following chain:

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Family and domain databases

Other

Entry information

Relevant documents