Cytochrome b-c1 complex subunit 7

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P00129 (QCR7_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 114. 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 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

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	111 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	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).

Ontologies

Keywords
Biological process	Electron transport Respiratory chain Transport
Cellular component	Membrane Mitochondrion Mitochondrion inner membrane
PTM	Acetylation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	mitochondrial electron transport, ubiquinol to cytochrome c Inferred from electronic annotation. Source: InterPro
Cellular_component	mitochondrial respiratory chain complex III Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed Ref.2

Chain

2 – 111

110

Cytochrome b-c1 complex subunit 7

PRO_0000193523

Amino acid modifications

Modified residue

N-acetylalanine Ref.2

Modified residue

N6-acetyllysine By similarity

Experimental info

Sequence conflict

N → D AA sequence Ref.2

Secondary structure

111

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P00129 [UniParc].

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

111

13,476

        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' referencesShow '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.

IPI

IPI00703716.

PIR

UYBO. A00122.

RefSeq

NP_001029969.1. NM_001034797.2.

UniGene

Bt.49002.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1BCC	X-ray	3.16	F	2-108	[»]
1BE3	X-ray	3.00	F	2-111	[»]
1BGY	X-ray	3.00	F/R	2-111	[»]
1L0L	X-ray	2.35	F	2-111	[»]
1L0N	X-ray	2.60	F	2-111	[»]
1NTK	X-ray	2.60	F	2-110	[»]
1NTM	X-ray	2.40	F	2-110	[»]
1NTZ	X-ray	2.60	F	2-110	[»]
1NU1	X-ray	3.20	F	2-110	[»]
1PP9	X-ray	2.10	F/S	2-111	[»]
1PPJ	X-ray	2.10	F/S	2-111	[»]
1QCR	X-ray	2.70	F	9-111	[»]
1SQB	X-ray	2.69	F	2-111	[»]
1SQP	X-ray	2.70	F	2-111	[»]
1SQQ	X-ray	3.00	F	2-111	[»]
1SQV	X-ray	2.85	F	2-111	[»]
1SQX	X-ray	2.60	F	2-111	[»]
2A06	X-ray	2.10	F/S	2-111	[»]
2BCC	X-ray	3.50	F	2-108	[»]
2FYU	X-ray	2.26	F	2-111	[»]
2YBB	electron microscopy	19.00	F/f	2-111	[»]
3BCC	X-ray	3.70	F	2-108	[»]

ProteinModelPortal

P00129.

SMR

P00129. Positions 3-111.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-1082N.

IntAct

P00129. 3 interactions.

STRING

9913.ENSBTAP00000001993.

Proteomic databases

PRIDE

P00129.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSBTAT00000001993; ENSBTAP00000001993; ENSBTAG00000001521.

GeneID

616871.

KEGG

bta:616871.

Organism-specific databases

CTD

7381.

Phylogenomic databases

eggNOG

NOG235867.

GeneTree

ENSGT00390000012916.

HOGENOM

HOG000188221.

HOVERGEN

HBG002984.

InParanoid

P00129.

K00417.

OMA

MRDDTIH.

OrthoDB

EOG4GHZQS.

Family and domain databases

Gene3D

1.10.1090.10. 1 hit.

InterPro

IPR003197. QCR7.
[Graphical view]

PANTHER

PTHR12022. PTHR12022. 1 hit.

Pfam

PF02271. UCR_14kD. 1 hit.
[Graphical view]

PIRSF

PIRSF000022. Bc1_14K. 1 hit.

ProDom

PD008153. Cyt_bd_ubiquinol_oxidase_14kDa. 1 hit.
[Graphical view] [Entries sharing at least one domain]

SUPFAM

SSF81524. Cyt_bd_Ubol_Oase_14kDa-su. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

P00129.

NextBio

20900361.

Entry information

Entry name

QCR7_BOVIN

Accession

Primary (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:	May 1, 2013
This is version 114 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

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Amino acid modifications

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Family and domain databases

Other

Entry information

Relevant documents