Reviewed, UniProtKB/Swiss-Prot P07256 (QCR1_YEAST)

Names and origin

Protein names

Recommended name:
    Cytochrome b-c1 complex subunit 1, mitochondrial
Alternative name(s):
    Ubiquinol-cytochrome-c reductase complex core protein 1
      Short name=Core protein I
    Complex III subunit 1

Gene names

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

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [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.
Miscellaneous	Present with 19300 molecules/cell in log phase SD medium. Ref.6
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
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 Ref.1 Ref.8 Inferred from direct assay. 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
ECM4	P36156	1	EBI-19922,EBI-2042717
PCL9	Q12477	1	EBI-19922,EBI-38090
QCR2	P07257	2	EBI-19922,EBI-19929

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – 26

26

Mitochondrion

Chain

27 – 457

431

Cytochrome b-c1 complex subunit 1, mitochondrial

PRO_0000026788

Amino acid modifications

Modified residue

140

1

Phosphothreonine Ref.7

Secondary structure

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457

Helix Strand Turn

Details...

Beta strand

30 – 42

13

Beta strand

44 – 47

4

Beta strand

49 – 56

8

Helix

59 – 61

3

Turn

64 – 68

5

Helix

69 – 77

9

Helix

80 – 88

9

Beta strand

92 – 97

6

Beta strand

102 – 108

7

Helix

110 – 112

3

Helix

115 – 124

10

Turn

128 – 130

3

Helix

134 – 154

21

Helix

156 – 168

13

Turn

169 – 171

3

Helix

173 – 175

3

Helix

182 – 185

4

Helix

190 – 200

11

Beta strand

201 – 203

3

Beta strand

206 – 213

8

Helix

216 – 225

10

Beta strand

247 – 253

7

Beta strand

256 – 266

11

Helix

275 – 285

11

Beta strand

287 – 289

3

Helix

295 – 297

3

Helix

302 – 307

6

Turn

308 – 310

3

Beta strand

313 – 321

9

Beta strand

326 – 335

10

Helix

340 – 356

17

Helix

360 – 378

19

Helix

383 – 397

15

Helix

403 – 411

9

Helix

415 – 425

11

Turn

426 – 428

3

Beta strand

432 – 438

7

Helix

445 – 450

6

Sequences

	Sequence		Length	Mass (Da)
	P07256-1 [UniParc]. Last modified April 1, 1988. Version 1. Checksum: AE58739EFB695254	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

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. , 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: 7813418] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[4]	"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. , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J. Genome Res. 17:536-543(2007) [PubMed: 17322287] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[5]	"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.
[6]	"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].
[7]	"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.
[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: 10873857] [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: 11880631] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.97 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

J02636 Genomic DNA. Translation: AAA34508.1.
X78214 Genomic DNA. Translation: CAA55050.1.
Z35806 Genomic DNA. Translation: CAA84865.1.
AY693047 Genomic DNA. Translation: AAT93066.1.

PIR

A25351.

RefSeq

NP_009508.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1EZV	X-ray	2.30	A	27-457	[»]
1KB9	X-ray	2.30	A	27-454	[»]
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	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:2635N.

IntAct

P07256. 25 interactions.

STRING

P07256.

Protein family/group databases

MEROPS

M16.973.
M16.981.

Proteomic databases

PeptideAtlas

P07256.

PRIDE

P07256.

Genome annotation databases

Ensembl

YBL045C; YBL045C; YBL045C; Saccharomyces cerevisiae. [Genome view]

GeneID

852235.

KEGG

sce:YBL045C.

NMPDR

fig|4932.3.peg.198.

Organism-specific databases

CYGD

YBL045c.

SGD

S000000141. COR1.

Phylogenomic databases

HOGENOM

P07256.

OMA

ASIVQEY

OrthoDB

EOG9RR814

Enzyme and pathway databases

BRENDA

2.3.1.9. 341.

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.

Pfam

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

PROSITE

PS00143. INSULINASE. False negative.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

970775.

Entry information

Entry name

QCR1_YEAST

Accession

Primary (citable) accession number: P07256

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1988
Last sequence update:	April 1, 1988
Last modified:	November 24, 2009
This is version 113 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)