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P13271 (QCR8_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 118. 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 8
Alternative name(s):
Complex III subunit 8
Complex III subunit VIII
Ubiquinol-cytochrome c reductase complex 9.5 kDa protein
Ubiquinol-cytochrome c reductase complex ubiquinone-binding protein QP-C
Gene names
Name:UQCRQ
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length82 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 subunit, together with cytochrome b, binds to ubiquinone.

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 UQCRQ/QCR8 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.3 Ref.4
Chain2 – 8281Cytochrome b-c1 complex subunit 8
PRO_0000193543

Amino acid modifications

Modified residue331N6-acetyllysine; alternate By similarity
Modified residue331N6-succinyllysine; alternate By similarity
Cross-link33Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate By similarity

Experimental info

Sequence conflict621W → C AA sequence Ref.3

Secondary structure

............. 82
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P13271 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 38D7E52051EB7FFA

FASTA829,720
        10         20         30         40         50         60 
MGRQFGHLTR VRHVITYSLS PFEQRAFPHY FSKGIPNVLR RTRACILRVA PPFVAFYLVY 

        70         80 
TWGTQEFEKS KRKNPAAYEN DR 

« Hide

References

« Hide 'large scale' references
[1]"Cloning, gene sequencing, and expression of the small molecular mass ubiquinone-binding protein of mitochondrial ubiquinol-cytochrome c reductase."
Yu L., Deng K.-P., Yu C.-A.
J. Biol. Chem. 270:25634-25638(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Heart.
[2]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.
[3]"Isolation and amino acid sequence of the 9.5 kDa protein of beef heart ubiquinol:cytochrome c reductase."
Borchart U., Machleidt W., Schaegger H., Link T.A., von Jagow G.
FEBS Lett. 200:81-86(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-82.
Tissue: Heart.
[4]"The small molecular mass ubiquinone-binding protein (QPc-9.5 kDa) in mitochondrial ubiquinol-cytochrome c reductase: isolation, ubiquinone-binding domain, and immunoinhibition."
Usui S., Yu L., Yu C.A.
Biochemistry 29:4618-4626(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-14 AND 50-58.
[5]"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).
[6]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)
[7]"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).
[8]"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).
[9]"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).
[10]"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).
[11]"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
L06665 mRNA. Translation: AAB03845.1.
BC103110 mRNA. Translation: AAI03111.1.
PIRA24864.
RefSeqNP_777230.1. NM_174805.2.
UniGeneBt.49658.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1BCCX-ray3.16G2-82[»]
1BE3X-ray3.00G2-82[»]
1BGYX-ray3.00G/S2-82[»]
1L0LX-ray2.35G2-82[»]
1L0NX-ray2.60G2-82[»]
1NTKX-ray2.60G2-81[»]
1NTMX-ray2.40G2-81[»]
1NTZX-ray2.60G2-81[»]
1NU1X-ray3.20G2-81[»]
1PP9X-ray2.10G/T2-82[»]
1PPJX-ray2.10G/T2-82[»]
1QCRX-ray2.70G2-71[»]
1SQBX-ray2.69G2-82[»]
1SQPX-ray2.70G2-82[»]
1SQQX-ray3.00G2-82[»]
1SQVX-ray2.85G2-82[»]
1SQXX-ray2.60G2-82[»]
2A06X-ray2.10G/T2-82[»]
2BCCX-ray3.50G2-82[»]
2FYUX-ray2.26G2-82[»]
2YBBelectron microscopy19.00G/g2-82[»]
3BCCX-ray3.70G2-81[»]
ProteinModelPortalP13271.
SMRP13271. Positions 2-82.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP13271. 2 interactions.
STRING9913.ENSBTAP00000040860.

Proteomic databases

PRIDEP13271.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSBTAT00000043278; ENSBTAP00000040860; ENSBTAG00000009479.
GeneID286885.
KEGGbta:286885.

Organism-specific databases

CTD27089.

Phylogenomic databases

eggNOGNOG253869.
GeneTreeENSGT00390000004029.
HOGENOMHOG000205681.
HOVERGENHBG001468.
InParanoidP13271.
KOK00418.
OMARMRHVIT.
OrthoDBEOG7K3TPV.
TreeFamTF300281.

Family and domain databases

Gene3D1.20.5.210. 1 hit.
InterProIPR004205. Cyt_bc1_su8.
[Graphical view]
PANTHERPTHR12119. PTHR12119. 1 hit.
PfamPF02939. UcrQ. 1 hit.
[Graphical view]
ProDomPD331499. UcrQ. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMSSF81508. SSF81508. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP13271.
NextBio20806531.

Entry information

Entry nameQCR8_BOVIN
AccessionPrimary (citable) accession number: P13271
Secondary accession number(s): Q3ZBT9
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 118 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