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Protein

Cytochrome b-c1 complex subunit 7

Gene

QCR7

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is part of the mitochondrial respiratory chain that generates an electrochemical potential coupled to ATP synthesis. The complex couples electron transfer from ubiquinol to cytochrome c. QCR7 is involved in redox-linked proton pumping.

GO - Biological processi

  • aerobic respiration Source: SGD
  • hydrogen ion transmembrane transport Source: GOC
  • mitochondrial electron transport, ubiquinol to cytochrome c Source: SGD
  • mitochondrial respiratory chain complex III assembly Source: SGD
Complete GO annotation...

Keywords - Biological processi

Electron transport, Respiratory chain, Transport

Enzyme and pathway databases

BioCyciYEAST:YDR529C-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Cytochrome b-c1 complex subunit 7
Alternative name(s):
Complex III subunit 7
Complex III subunit VII
Ubiquinol-cytochrome c reductase c reductase complex 14 kDa protein
Gene namesi
Name:QCR7
Synonyms:CRO1, UCR7
Ordered Locus Names:YDR529C
ORF Names:D9719.32
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome IV

Organism-specific databases

EuPathDBiFungiDB:YDR529C.
SGDiS000002937. QCR7.

Subcellular locationi

GO - Cellular componenti

  • mitochondrial respiratory chain complex III Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion inner membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 127127Cytochrome b-c1 complex subunit 7PRO_0000193539Add
BLAST

Proteomic databases

MaxQBiP00128.

Interactioni

Subunit structurei

Fungal cytochrome b-c1 complex contains 10 subunits; 3 respiratory subunits, 2 core proteins and 5 low-molecular weight proteins. Cytochrome b-c1 complex is a homodimer.

Protein-protein interaction databases

BioGridi32578. 65 interactions.
DIPiDIP-2061N.
IntActiP00128. 7 interactions.
MINTiMINT-555250.

Structurei

Secondary structure

1
127
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi5 – 1713Combined sources
Helixi19 – 3618Combined sources
Helixi38 – 414Combined sources
Helixi45 – 484Combined sources
Helixi54 – 629Combined sources
Helixi65 – 8319Combined sources
Helixi90 – 923Combined sources
Helixi96 – 983Combined sources
Helixi104 – 12118Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1EZVX-ray2.30F3-127[»]
1KB9X-ray2.30G3-127[»]
1KYOX-ray2.97G/R2-127[»]
1P84X-ray2.50G3-127[»]
2IBZX-ray2.30F1-127[»]
3CX5X-ray1.90G/R2-127[»]
3CXHX-ray2.50G/R2-127[»]
4PD4X-ray3.04G2-127[»]
ProteinModelPortaliP00128.
SMRiP00128. Positions 2-127.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00128.

Family & Domainsi

Sequence similaritiesi

Belongs to the UQCRB/QCR7 family.Curated

Phylogenomic databases

GeneTreeiENSGT00390000012916.
HOGENOMiHOG000188221.
InParanoidiP00128.
KOiK00417.
OMAiERADWDH.
OrthoDBiEOG7HHX4K.

Family and domain databases

Gene3Di1.10.1090.10. 1 hit.
InterProiIPR003197. QCR7.
[Graphical view]
PANTHERiPTHR12022. PTHR12022. 1 hit.
PfamiPF02271. UCR_14kD. 1 hit.
[Graphical view]
PIRSFiPIRSF000022. Bc1_14K. 1 hit.
ProDomiPD008153. Cyt_bd_ubiquinol_oxidase_14kDa. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF81524. SSF81524. 1 hit.

Sequencei

Sequence statusi: Complete.

P00128-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPQSFTSIAR IGDYILKSPV LSKLCVPVAN QFINLAGYKK LGLKFDDLIA
60 70 80 90 100
EENPIMQTAL RRLPEDESYA RAYRIIRAHQ TELTHHLLPR NEWIKAQEDV
110 120
PYLLPYILEA EAAAKEKDEL DNIEVSK
Length:127
Mass (Da):14,565
Last modified:October 1, 1996 - v2
Checksum:i1F1BA3DB6C4067B4
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti92 – 921E → Q in CAA25064 (PubMed:6319130).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X00256 Genomic DNA. Translation: CAA25064.1.
U33057 Genomic DNA. Translation: AAB64968.1.
BK006938 Genomic DNA. Translation: DAA12360.1.
PIRiS69584. RDBYUN.
RefSeqiNP_010818.1. NM_001180837.1.

Genome annotation databases

EnsemblFungiiYDR529C; YDR529C; YDR529C.
GeneIDi852142.
KEGGisce:YDR529C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X00256 Genomic DNA. Translation: CAA25064.1.
U33057 Genomic DNA. Translation: AAB64968.1.
BK006938 Genomic DNA. Translation: DAA12360.1.
PIRiS69584. RDBYUN.
RefSeqiNP_010818.1. NM_001180837.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1EZVX-ray2.30F3-127[»]
1KB9X-ray2.30G3-127[»]
1KYOX-ray2.97G/R2-127[»]
1P84X-ray2.50G3-127[»]
2IBZX-ray2.30F1-127[»]
3CX5X-ray1.90G/R2-127[»]
3CXHX-ray2.50G/R2-127[»]
4PD4X-ray3.04G2-127[»]
ProteinModelPortaliP00128.
SMRiP00128. Positions 2-127.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32578. 65 interactions.
DIPiDIP-2061N.
IntActiP00128. 7 interactions.
MINTiMINT-555250.

Proteomic databases

MaxQBiP00128.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYDR529C; YDR529C; YDR529C.
GeneIDi852142.
KEGGisce:YDR529C.

Organism-specific databases

EuPathDBiFungiDB:YDR529C.
SGDiS000002937. QCR7.

Phylogenomic databases

GeneTreeiENSGT00390000012916.
HOGENOMiHOG000188221.
InParanoidiP00128.
KOiK00417.
OMAiERADWDH.
OrthoDBiEOG7HHX4K.

Enzyme and pathway databases

BioCyciYEAST:YDR529C-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP00128.
PROiP00128.

Family and domain databases

Gene3Di1.10.1090.10. 1 hit.
InterProiIPR003197. QCR7.
[Graphical view]
PANTHERiPTHR12022. PTHR12022. 1 hit.
PfamiPF02271. UCR_14kD. 1 hit.
[Graphical view]
PIRSFiPIRSF000022. Bc1_14K. 1 hit.
ProDomiPD008153. Cyt_bd_ubiquinol_oxidase_14kDa. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF81524. SSF81524. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The biosynthesis of the ubiquinol-cytochrome c reductase complex in yeast. DNA sequence analysis of the nuclear gene coding for the 14-kDa subunit."
    de Haan M., van Loon A.P.G.M., Kreike J., Vaessen R.T.M.J., Grivell L.A.
    Eur. J. Biochem. 138:169-177(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 28383 / FL100 / VTT C-80102.
  2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
    Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T.
    , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
    Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  6. "Structure at 2.3 A resolution of the cytochrome bc1 complex from the yeast Saccharomyces cerevisiae co-crystallized with an antibody Fv fragment."
    Hunte C., Koepke J., Lange C., Rossmanith T., Michel H.
    Structure 8:669-684(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 3-127.
  7. "Crystal structure of the yeast cytochrome bc1 complex with its bound substrate cytochrome c."
    Lange C., Hunte C.
    Proc. Natl. Acad. Sci. U.S.A. 99:2800-2805(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.97 ANGSTROMS) OF 2-127.
  8. "Structure of the yeast cytochrome bc1 complex with a hydroxyquinone anion Qo site inhibitor bound."
    Palsdottir H., Lojero C.G., Trumpower B.L., Hunte C.
    J. Biol. Chem. 278:31303-31311(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 3-127.

Entry informationi

Entry nameiQCR7_YEAST
AccessioniPrimary (citable) accession number: P00128
Secondary accession number(s): D6VTF0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: October 1, 1996
Last modified: July 6, 2016
This is version 155 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 10100 molecules/cell in log phase SD medium.1 Publication

Caution

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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome IV
    Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.