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Protein

Cytochrome b-c1 complex subunit 1, mitochondrial

Gene

COR1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 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. COR1 may mediate formation of the complex between cytochromes c and c1.

GO - Molecular functioni

GO - Biological processi

  • aerobic respiration Source: SGD
  • hydrogen ion transmembrane transport Source: GOC
Complete GO annotation...

Keywords - Biological processi

Electron transport, Respiratory chain, Transport

Enzyme and pathway databases

BioCyciYEAST:YBL045C-MONOMER.
BRENDAi2.3.1.9. 6758.

Protein family/group databases

MEROPSiM16.973.

Names & Taxonomyi

Protein namesi
Recommended name:
Cytochrome b-c1 complex subunit 1, mitochondrial
Alternative name(s):
Complex III subunit 1
Core protein I
Ubiquinol-cytochrome-c reductase complex core protein 1
Gene namesi
Name:COR1
Synonyms:QCR1
Ordered Locus Names:YBL045C
ORF Names:YBL0403
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:YBL045C.
SGDiS000000141. COR1.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion inner membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 2626MitochondrionAdd
BLAST
Chaini27 – 457431Cytochrome b-c1 complex subunit 1, mitochondrialPRO_0000026788Add
BLAST

Proteomic databases

MaxQBiP07256.
PeptideAtlasiP07256.

PTM databases

iPTMnetiP07256.

Interactioni

Subunit structurei

Fungi 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.

Binary interactionsi

WithEntry#Exp.IntActNotes
QCR2P072575EBI-19922,EBI-19929

Protein-protein interaction databases

BioGridi32652. 133 interactions.
DIPiDIP-2635N.
IntActiP07256. 17 interactions.
MINTiMINT-424492.

Structurei

Secondary structure

1
457
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi30 – 4213Combined sources
Beta strandi47 – 5610Combined sources
Helixi59 – 613Combined sources
Turni64 – 685Combined sources
Helixi69 – 779Combined sources
Helixi80 – 889Combined sources
Beta strandi92 – 976Combined sources
Beta strandi102 – 1087Combined sources
Helixi110 – 1123Combined sources
Helixi113 – 12412Combined sources
Turni129 – 1324Combined sources
Helixi134 – 15421Combined sources
Helixi156 – 16813Combined sources
Turni169 – 1713Combined sources
Helixi173 – 1753Combined sources
Helixi182 – 1865Combined sources
Helixi190 – 20011Combined sources
Helixi203 – 2053Combined sources
Beta strandi206 – 2138Combined sources
Helixi216 – 2238Combined sources
Beta strandi247 – 2526Combined sources
Beta strandi256 – 26611Combined sources
Helixi275 – 28511Combined sources
Beta strandi287 – 2893Combined sources
Helixi295 – 2973Combined sources
Helixi302 – 3076Combined sources
Turni308 – 3103Combined sources
Beta strandi313 – 3219Combined sources
Beta strandi326 – 33510Combined sources
Helixi340 – 35617Combined sources
Helixi360 – 37819Combined sources
Helixi383 – 39715Combined sources
Helixi403 – 41210Combined sources
Helixi415 – 42511Combined sources
Turni426 – 4283Combined sources
Beta strandi432 – 4387Combined sources
Beta strandi440 – 4423Combined sources
Helixi445 – 4506Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1EZVX-ray2.30A27-457[»]
1KB9X-ray2.30A27-457[»]
1KYOX-ray2.97A/L27-457[»]
1P84X-ray2.50A27-457[»]
2IBZX-ray2.30A27-457[»]
3CX5X-ray1.90A/L27-457[»]
3CXHX-ray2.50A/L27-457[»]
4PD4X-ray3.04A27-457[»]
ProteinModelPortaliP07256.
SMRiP07256. Positions 27-457.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP07256.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

HOGENOMiHOG000242450.
InParanoidiP07256.
KOiK00414.
OMAiPYNNGVS.
OrthoDBiEOG7BW0TR.

Family and domain databases

Gene3Di3.30.830.10. 2 hits.
InterProiIPR011249. Metalloenz_LuxS/M16.
IPR011237. Pept_M16_dom.
IPR011765. Pept_M16_N.
IPR007863. Peptidase_M16_C.
[Graphical view]
PfamiPF00675. Peptidase_M16. 1 hit.
PF05193. Peptidase_M16_C. 1 hit.
[Graphical view]
SUPFAMiSSF63411. SSF63411. 2 hits.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P07256-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLRTVTSKTV SNQFKRSLAT AVATPKAEVT QLSNGIVVAT EHNPSAHTAS
60 70 80 90 100
VGVVFGSGAA NENPYNNGVS NLWKNIFLSK ENSAVAAKEG LALSSNISRD
110 120 130 140 150
FQSYIVSSLP GSTDKSLDFL NQSFIQQKAN LLSSSNFEAT KKSVLKQVQD
160 170 180 190 200
FEENDHPNRV LEHLHSTAFQ NTPLSLPTRG TLESLENLVV ADLESFANNH
210 220 230 240 250
FLNSNAVVVG TGNIKHEDLV NSIESKNLSL QTGTKPVLKK KAAFLGSEVR
260 270 280 290 300
LRDDTLPKAW ISLAVEGEPV NSPNYFVAKL AAQIFGSYNA FEPASRLQGI
310 320 330 340 350
KLLDNIQEYQ LCDNFNHFSL SYKDSGLWGF STATRNVTMI DDLIHFTLKQ
360 370 380 390 400
WNRLTISVTD TEVERAKSLL KLQLGQLYES GNPVNDANLL GAEVLIKGSK
410 420 430 440 450
LSLGEAFKKI DAITVKDVKA WAGKRLWDQD IAIAGTGQIE GLLDYMRIRS

DMSMMRW
Length:457
Mass (Da):50,228
Last modified:April 1, 1988 - v1
Checksum:iAE58739EFB695254
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J02636 Genomic DNA. Translation: AAA34508.1.
X78214 Genomic DNA. Translation: CAA55050.1.
Z35806 Genomic DNA. Translation: CAA84865.1.
AY693047 Genomic DNA. Translation: AAT93066.1.
BK006936 Genomic DNA. Translation: DAA07073.1.
PIRiA25351.
RefSeqiNP_009508.1. NM_001178285.1.

Genome annotation databases

EnsemblFungiiYBL045C; YBL045C; YBL045C.
GeneIDi852235.
KEGGisce:YBL045C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J02636 Genomic DNA. Translation: AAA34508.1.
X78214 Genomic DNA. Translation: CAA55050.1.
Z35806 Genomic DNA. Translation: CAA84865.1.
AY693047 Genomic DNA. Translation: AAT93066.1.
BK006936 Genomic DNA. Translation: DAA07073.1.
PIRiA25351.
RefSeqiNP_009508.1. NM_001178285.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1EZVX-ray2.30A27-457[»]
1KB9X-ray2.30A27-457[»]
1KYOX-ray2.97A/L27-457[»]
1P84X-ray2.50A27-457[»]
2IBZX-ray2.30A27-457[»]
3CX5X-ray1.90A/L27-457[»]
3CXHX-ray2.50A/L27-457[»]
4PD4X-ray3.04A27-457[»]
ProteinModelPortaliP07256.
SMRiP07256. Positions 27-457.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32652. 133 interactions.
DIPiDIP-2635N.
IntActiP07256. 17 interactions.
MINTiMINT-424492.

Protein family/group databases

MEROPSiM16.973.

PTM databases

iPTMnetiP07256.

Proteomic databases

MaxQBiP07256.
PeptideAtlasiP07256.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYBL045C; YBL045C; YBL045C.
GeneIDi852235.
KEGGisce:YBL045C.

Organism-specific databases

EuPathDBiFungiDB:YBL045C.
SGDiS000000141. COR1.

Phylogenomic databases

HOGENOMiHOG000242450.
InParanoidiP07256.
KOiK00414.
OMAiPYNNGVS.
OrthoDBiEOG7BW0TR.

Enzyme and pathway databases

BioCyciYEAST:YBL045C-MONOMER.
BRENDAi2.3.1.9. 6758.

Miscellaneous databases

EvolutionaryTraceiP07256.
NextBioi970775.
PROiP07256.

Family and domain databases

Gene3Di3.30.830.10. 2 hits.
InterProiIPR011249. Metalloenz_LuxS/M16.
IPR011237. Pept_M16_dom.
IPR011765. Pept_M16_N.
IPR007863. Peptidase_M16_C.
[Graphical view]
PfamiPF00675. Peptidase_M16. 1 hit.
PF05193. Peptidase_M16_C. 1 hit.
[Graphical view]
SUPFAMiSSF63411. SSF63411. 2 hits.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Assembly of the mitochondrial membrane system. Characterization of COR1, the structural gene for the 44-kilodalton core protein of yeast coenzyme QH2-cytochrome c reductase."
    Tzagoloff A., Wu M., Crivellone M.
    J. Biol. Chem. 261:17163-17169(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "The sequence of a 22.4 kb DNA fragment from the left arm of yeast chromosome II reveals homologues to bacterial proline synthetase and murine alpha-adaptin, as well as a new permease and a DNA-binding protein."
    de Wergifosse P., Jacques B., Jonniaux J.-L., Purnelle B., Skala J., Goffeau A.
    Yeast 10:1489-1496(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. "Complete DNA sequence of yeast chromosome II."
    Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C., Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M., Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M., Cziepluch C.
    , Demolis N., Delaveau T., Doignon F., Domdey H., Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D., Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N., Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J., Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C., Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P., Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y., Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F., Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E., Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M., Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B., Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L., Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M., Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S., Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K., Mewes H.-W., Kleine K.
    EMBO J. 13:5795-5809(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  5. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  6. "Yeast mitochondrial dehydrogenases are associated in a supramolecular complex."
    Grandier-Vazeille X., Bathany K., Chaignepain S., Camougrand N., Manon S., Schmitter J.-M.
    Biochemistry 40:9758-9769(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  7. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  8. "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).
  9. "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).

Entry informationi

Entry nameiQCR1_YEAST
AccessioniPrimary (citable) accession number: P07256
Secondary accession number(s): D6VPV3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: April 1, 1988
Last modified: May 11, 2016
This is version 168 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 19300 molecules/cell in log phase SD medium.1 Publication

Caution

Does not seem to have a protease activity as it lack the zinc-binding site.Curated

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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