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P00129 (QCR7_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 123. 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 7
Alternative name(s):
Complex III subunit 7
Complex III subunit VII
QP-C
Ubiquinol-cytochrome c reductase complex 14 kDa protein
Gene names
Name:UQCRB
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length111 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

This is a component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is part of the mitochondrial respiratory chain. This component is involved in redox-linked proton pumping.

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.

Sequence similarities

Belongs to the UQCRB/QCR7 family.

Caution

Was originally (Ref.2) thought to be the ubiquinone-binding protein (QP-C).

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.2
Chain2 – 111110Cytochrome b-c1 complex subunit 7
PRO_0000193523

Amino acid modifications

Modified residue21N-acetylalanine Ref.2
Modified residue191N6-acetyllysine By similarity
Modified residue781N6-acetyllysine; alternate By similarity
Modified residue781N6-succinyllysine; alternate By similarity
Modified residue831N6-acetyllysine By similarity
Modified residue881N6-acetyllysine; alternate By similarity
Modified residue881N6-succinyllysine; alternate By similarity
Modified residue961N6-acetyllysine By similarity

Experimental info

Sequence conflict571N → D AA sequence Ref.2

Secondary structure

.................. 111
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P00129 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 2D89B44D53DA494B

FASTA11113,476
        10         20         30         40         50         60 
MAGRPAVSAS SRWLEGIRKW YYNAAGFNKL GLMRDDTIHE NDDVKEAIRR LPENLYNDRV 

        70         80         90        100        110 
FRIKRALDLS MRQQILPKEQ WTKYEEDKSY LEPYLKEVIR ERKEREEWAK K 

« Hide

References

« Hide 'large scale' references
[1]NIH - Mammalian Gene Collection (MGC) project
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Hereford.
Tissue: Heart ventricle.
[2]"Complete amino acid sequence of the ubiquinone binding protein (QP-C), a protein similar to the 14,000-dalton subunit of the yeast ubiquinol-cytochrome c reductase complex."
Wakabayashi S., Takao T., Shimonishi Y., Kuramitsu S., Matsubara H., Wang T., Zhang Z., King T.E.
J. Biol. Chem. 260:337-343(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-111.
[3]"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).
[4]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)
[5]"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).
[6]"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).
[7]"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).
[8]"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).
[9]"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
BC103057 mRNA. Translation: AAI03058.1.
PIRUYBO. A00122.
RefSeqNP_001029969.1. NM_001034797.2.
UniGeneBt.49002.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1BCCX-ray3.16F2-108[»]
1BE3X-ray3.00F2-111[»]
1BGYX-ray3.00F/R2-111[»]
1L0LX-ray2.35F2-111[»]
1L0NX-ray2.60F2-111[»]
1NTKX-ray2.60F2-111[»]
1NTMX-ray2.40F2-111[»]
1NTZX-ray2.60F2-111[»]
1NU1X-ray3.20F2-111[»]
1PP9X-ray2.10F/S2-111[»]
1PPJX-ray2.10F/S2-111[»]
1QCRX-ray2.70F9-111[»]
1SQBX-ray2.69F2-111[»]
1SQPX-ray2.70F2-111[»]
1SQQX-ray3.00F2-111[»]
1SQVX-ray2.85F2-111[»]
1SQXX-ray2.60F2-111[»]
2A06X-ray2.10F/S2-111[»]
2BCCX-ray3.50F2-108[»]
2FYUX-ray2.26F2-111[»]
2YBBelectron microscopy19.00F/f2-111[»]
3BCCX-ray3.70F2-108[»]
ProteinModelPortalP00129.
SMRP00129. Positions 3-111.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-1082N.
IntActP00129. 3 interactions.
STRING9913.ENSBTAP00000001993.

Proteomic databases

PRIDEP00129.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSBTAT00000001993; ENSBTAP00000001993; ENSBTAG00000001521.
GeneID616871.
KEGGbta:616871.

Organism-specific databases

CTD7381.

Phylogenomic databases

eggNOGNOG235867.
GeneTreeENSGT00390000012916.
HOGENOMHOG000188221.
HOVERGENHBG002984.
InParanoidP00129.
KOK00417.
OMAQWVKYEE.
OrthoDBEOG7VDXR7.
TreeFamTF105035.

Family and domain databases

Gene3D1.10.1090.10. 1 hit.
InterProIPR003197. QCR7.
[Graphical view]
PANTHERPTHR12022. PTHR12022. 1 hit.
PfamPF02271. UCR_14kD. 1 hit.
[Graphical view]
PIRSFPIRSF000022. Bc1_14K. 1 hit.
ProDomPD008153. Cyt_bd_ubiquinol_oxidase_14kDa. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMSSF81524. SSF81524. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP00129.
NextBio20900361.

Entry information

Entry nameQCR7_BOVIN
AccessionPrimary (citable) accession number: P00129
Secondary accession number(s): Q3SZ83
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 123 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