Cytochrome b-c1 complex subunit 1, mitochondrial precursor - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

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P07256 (QCR1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 131. History...

Clusters with 100%, 90%, 50% identity |

Documents (5) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

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 names

Name:	COR1
Synonyms:	QCR1
Ordered Locus Names:	YBL045C
ORF Names:	YBL0403

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	457 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	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.
Subunit structure	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.
Subcellular location	Mitochondrion inner membrane Ref.6.
Miscellaneous	Present with 19300 molecules/cell in log phase SD medium. Ref.7
Sequence similarities	Belongs to the peptidase M16 family. UQCRC1/QCR1 subfamily.
Caution	Does not seem to have a protease activity as it lack the zinc-binding site.

Ontologies

Keywords
Biological process	Electron transport Respiratory chain Transport
Cellular component	Membrane Mitochondrion Mitochondrion inner membrane
Domain	Transit peptide
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	aerobic respiration Inferred from mutant phenotype. Source: SGD electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW proteolysis Inferred from electronic annotation. Source: InterPro transport Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	mitochondrial respiratory chain complex III Inferred from direct assay Ref.9 Ref.1. Source: SGD
Molecular function	metalloendopeptidase activity Inferred from electronic annotation. Source: InterPro protein binding Inferred from physical interaction. Source: IntAct zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
QCR2	P07257	5	EBI-19922,EBI-19929

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – 26

Mitochondrion

Chain

27 – 457

431

Cytochrome b-c1 complex subunit 1, mitochondrial

PRO_0000026788

Amino acid modifications

Modified residue

140

Phosphothreonine Ref.8

Secondary structure

457

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P07256 [UniParc].

Last modified April 1, 1988. Version 1.
Checksum: AE58739EFB695254
Show »

FASTA

457

50,228

        10         20         30         40         50         60 
MLRTVTSKTV SNQFKRSLAT AVATPKAEVT QLSNGIVVAT EHNPSAHTAS VGVVFGSGAA 

        70         80         90        100        110        120 
NENPYNNGVS NLWKNIFLSK ENSAVAAKEG LALSSNISRD FQSYIVSSLP GSTDKSLDFL 

       130        140        150        160        170        180 
NQSFIQQKAN LLSSSNFEAT KKSVLKQVQD FEENDHPNRV LEHLHSTAFQ NTPLSLPTRG 

       190        200        210        220        230        240 
TLESLENLVV ADLESFANNH FLNSNAVVVG TGNIKHEDLV NSIESKNLSL QTGTKPVLKK 

       250        260        270        280        290        300 
KAAFLGSEVR LRDDTLPKAW ISLAVEGEPV NSPNYFVAKL AAQIFGSYNA FEPASRLQGI 

       310        320        330        340        350        360 
KLLDNIQEYQ LCDNFNHFSL SYKDSGLWGF STATRNVTMI DDLIHFTLKQ WNRLTISVTD 

       370        380        390        400        410        420 
TEVERAKSLL KLQLGQLYES GNPVNDANLL GAEVLIKGSK LSLGEAFKKI DAITVKDVKA 

       430        440        450 
WAGKRLWDQD IAIAGTGQIE GLLDYMRIRS DMSMMRW

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 3023384] [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: 7871888] [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. Kleine K. EMBO J. 13:5795-5809(1994) [PubMed: 7813418] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[4]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[5]	"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae." Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. LaBaer J. Genome Res. 17:536-543(2007) [PubMed: 17322287] [Abstract] 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: 11502169] [Abstract] Cited for: SUBCELLULAR LOCATION.
[7]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[8]	"A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-140, MASS SPECTROMETRY.
[9]	"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: 10873857] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
[10]	"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: 11880631] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.97 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

PIR

A25351.

RefSeq

NP_009508.1. NM_001178285.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1EZV	X-ray	2.30	A	27-457	[»]
1KB9	X-ray	2.30	A	27-457	[»]
1KYO	X-ray	2.97	A/L	27-457	[»]
1P84	X-ray	2.50	A	27-457	[»]
2IBZ	X-ray	2.30	A	27-457	[»]
3CX5	X-ray	1.90	A/L	27-457	[»]
3CXH	X-ray	2.50	A/L	27-457	[»]

ProteinModelPortal

P07256.

SMR

P07256. Positions 27-457.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-2635N.

IntAct

P07256. 24 interactions.

MINT

MINT-424492.

STRING

P07256.

Protein family/group databases

MEROPS

M16.973.

Proteomic databases

PeptideAtlas

P07256.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YBL045C; YBL045C; YBL045C.

GeneID

852235.

KEGG

sce:YBL045C.

NMPDR

fig|4932.3.peg.198.

Organism-specific databases

CYGD

YBL045c.

SGD

S000000141. COR1.

Phylogenomic databases

eggNOG

fuNOG07954.

GeneTree

EFGT00050000004568.

HOGENOM

HBG476859.

OMA

TAFQNTP.

OrthoDB

EOG4VMJQ9.

Enzyme and pathway databases

BRENDA

2.3.1.9. 6758.

Gene expression databases

ArrayExpress

P07256.

Genevestigator

P07256.

GermOnline

YBL045C. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR011249. Metalloenz_metal-bd.
IPR011237. Pept_M16_core.
IPR011765. Pept_M16_N.
IPR007863. Peptidase_M16_C.
[Graphical view]

Gene3D

G3DSA:3.30.830.10. Pept_M16_core. 2 hits.

K00414.

Pfam

PF00675. Peptidase_M16. 1 hit.
PF05193. Peptidase_M16_C. 1 hit.
[Graphical view]

SUPFAM

SSF63411. Metalloenz_metal-bd. 2 hits.

PROSITE

PS00143. INSULINASE. False negative.
[Graphical view]

ProtoNet

Search...

Other

NextBio

970775.

Entry information

Entry name

QCR1_YEAST

Accession

Primary (citable) accession number: P07256
Secondary accession number(s): D6VPV3

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1988
Last sequence update:	April 1, 1988
Last modified:	December 14, 2011
This is version 131 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

Yeast chromosome II

Yeast (Saccharomyces cerevisiae) chromosome II: entries and gene names

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Amino acid modifications

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents