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P13272 (UCRI_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 137. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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:

  1. Cytochrome b-c1 complex subunit 11
    Alternative name(s):
    Complex III subunit IX
    Ubiquinol-cytochrome c reductase 8 kDa protein
Gene names
Name:UQCRFS1
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length274 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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

Quinol + 2 ferricytochrome c = quinone + 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 7878Cytochrome b-c1 complex subunit 11
PRO_0000030659
Transit peptide1 – 7878Mitochondrion Ref.5 Ref.9
Chain79 – 274196Cytochrome b-c1 complex subunit Rieske, mitochondrial
PRO_0000030660

Regions

Transmembrane103 – 14038Helical
Domain187 – 27286Rieske

Sites

Metal binding2171Iron-sulfur (2Fe-2S)
Metal binding2191Iron-sulfur (2Fe-2S); via pros nitrogen
Metal binding2361Iron-sulfur (2Fe-2S)
Metal binding2391Iron-sulfur (2Fe-2S); via pros nitrogen

Amino acid modifications

Disulfide bond222 ↔ 238 Ref.6

Experimental info

Sequence conflict1501S → A AA sequence Ref.5
Sequence conflict2691D → G AA sequence Ref.5

Secondary structure

................................................................ 274
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P13272 [UniParc].

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

FASTA27429,547
        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' 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.
PIRA34660. A46063.
RefSeqNP_777238.1. NM_174813.2.
UniGeneBt.265.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1BCCX-ray3.16A192-195[»]
E79-274[»]
1BE3X-ray3.00E79-274[»]
I1-78[»]
1BGYX-ray3.00E/Q79-274[»]
I/U1-78[»]
1L0LX-ray2.35E79-274[»]
I1-78[»]
1L0NX-ray2.60E79-274[»]
I1-78[»]
1NTKX-ray2.60E79-274[»]
I1-57[»]
1NTMX-ray2.40E79-274[»]
I1-57[»]
1NTZX-ray2.60E79-274[»]
I1-57[»]
1NU1X-ray3.20E79-274[»]
I1-57[»]
1PP9X-ray2.10E/R79-274[»]
I/V1-78[»]
1PPJX-ray2.10E/R79-274[»]
I/V1-78[»]
1QCRX-ray2.70E79-274[»]
I21-48[»]
1RIEX-ray1.50A146-274[»]
1SQBX-ray2.69E79-274[»]
I1-78[»]
1SQPX-ray2.70E79-274[»]
I1-78[»]
1SQQX-ray3.00E79-274[»]
I1-78[»]
1SQVX-ray2.85E79-274[»]
I1-78[»]
1SQXX-ray2.60E79-274[»]
I1-78[»]
2A06X-ray2.10E/R79-274[»]
I/V1-78[»]
2FYUX-ray2.26E79-274[»]
I1-78[»]
2YBBelectron microscopy19.00E/e79-274[»]
I/i14-78[»]
ProteinModelPortalP13272.
SMRP13272. Positions 1-57, 79-274.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP13272. 3 interactions.

Protein family/group databases

TCDB3.D.3.2.1. the proton-translocating quinol:cytochrome c reductase (qcr) superfamily.

Proteomic databases

PRIDEP13272.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID287020.
KEGGbta:287020.

Organism-specific databases

CTD7386.

Phylogenomic databases

HOVERGENHBG001040.
KOK00411.

Family and domain databases

Gene3D1.20.5.270. 1 hit.
2.102.10.10. 1 hit.
InterProIPR011070. 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]
PANTHERPTHR10134. PTHR10134. 1 hit.
PfamPF00355. Rieske. 1 hit.
PF09165. Ubiq-Cytc-red_N. 1 hit.
PF02921. UCR_TM. 1 hit.
[Graphical view]
PRINTSPR00162. RIESKE.
SUPFAMSSF50022. SSF50022. 1 hit.
SSF56568. SSF56568. 1 hit.
TIGRFAMsTIGR01416. Rieske_proteo. 1 hit.
PROSITEPS51296. RIESKE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP13272.
NextBio20806543.

Entry information

Entry nameUCRI_BOVIN
AccessionPrimary (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: April 16, 2014
This is version 137 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references