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P31800 (QCR1_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 125. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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:UQCRC1
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length480 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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 protein may mediate formation of the complex between cytochromes c and c1.

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; Peripheral membrane protein; Matrix side.

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 3434Mitochondrion Ref.3
Chain35 – 480446Cytochrome b-c1 complex subunit 1, mitochondrial
PRO_0000026785

Amino acid modifications

Modified residue1111N6-acetyllysine By similarity
Modified residue1381N6-acetyllysine By similarity
Modified residue1631N6-acetyllysine; alternate By similarity
Modified residue1631N6-succinyllysine; alternate By similarity
Modified residue2481N6-acetyllysine By similarity

Secondary structure

................................................................................ 480
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P31800 [UniParc].

Last modified December 1, 2000. Version 2.
Checksum: 4E54DD28C1905392

FASTA48052,736
        10         20         30         40         50         60 
MAASAVCRAA GAGTRVLLRT RRSPALLRSS DLRGTATYAQ ALQSVPETQV SQLDNGLRVA 

        70         80         90        100        110        120 
SEQSSQPTCT VGVWIDAGSR YESEKNNGAG YFVEHLAFKG TKNRPGNALE KEVESMGAHL 

       130        140        150        160        170        180 
NAYSTREHTA YYIKALSKDL PKAVELLADI VQNCSLEDSQ IEKERDVILQ ELQENDTSMR 

       190        200        210        220        230        240 
DVVFNYLHAT AFQGTPLAQS VEGPSENVRK LSRADLTEYL SRHYKAPRMV LAAAGGLEHR 

       250        260        270        280        290        300 
QLLDLAQKHF SGLSGTYDED AVPTLSPCRF TGSQICHRED GLPLAHVAIA VEGPGWAHPD 

       310        320        330        340        350        360 
NVALQVANAI IGHYDCTYGG GAHLSSPLAS IAATNKLCQS FQTFNICYAD TGLLGAHFVC 

       370        380        390        400        410        420 
DHMSIDDMMF VLQGQWMRLC TSATESEVLR GKNLLRNALV SHLDGTTPVC EDIGRSLLTY 

       430        440        450        460        470        480 
GRRIPLAEWE SRIAEVDARV VREVCSKYFY DQCPAVAGFG PIEQLPDYNR IRSGMFWLRF 

« Hide

References

[1]"Core I protein of bovine ubiquinol-cytochrome-c reductase; an additional member of the mitochondrial-protein-processing family. Cloning of bovine core I and core II cDNAs and primary structure of the proteins."
Gencic S., Schaegger H., von Jagow G.
Eur. J. Biochem. 199:123-131(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Heart.
[2]"Ubiquinol-cytochrome-c reductase from human and bovine mitochondria."
Schaegger H., Brandt U., Gencic S., von Jagow G.
Methods Enzymol. 260:82-96(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: SEQUENCE REVISION TO C-TERMINUS.
[3]"Subunit arrangement in beef heart complex III."
Gonzalez-Halphen D., Lindorfer M.A., Capaldi R.M.
Biochemistry 27:7021-7031(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 35-52.
[4]"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).
[5]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)
[6]"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).
[7]"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).
[8]"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).
[9]"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).
[10]"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
X59692 mRNA. Translation: CAA42213.1.
PIRZPBOC1. S16220.
RefSeqNP_777054.1. NM_174629.2.
UniGeneBt.23164.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1BCCX-ray3.16A35-480[»]
1BE3X-ray3.00A35-480[»]
1BGYX-ray3.00A/M35-480[»]
1L0LX-ray2.35A35-480[»]
1L0NX-ray2.60A35-480[»]
1NTKX-ray2.60A35-480[»]
1NTMX-ray2.40A35-480[»]
1NTZX-ray2.60A35-480[»]
1NU1X-ray3.20A35-480[»]
1PP9X-ray2.10A/N35-480[»]
1PPJX-ray2.10A/N35-480[»]
1QCRX-ray2.70A35-480[»]
1SQBX-ray2.69A1-480[»]
1SQPX-ray2.70A1-480[»]
1SQQX-ray3.00A35-480[»]
1SQVX-ray2.85A35-480[»]
1SQXX-ray2.60A35-480[»]
2A06X-ray2.10A/N35-480[»]
2BCCX-ray3.50A35-480[»]
2FYUX-ray2.26A35-480[»]
2YBBelectron microscopy19.00A/a35-480[»]
3BCCX-ray3.70A35-480[»]
ProteinModelPortalP31800.
SMRP31800. Positions 35-480.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-1105N.
IntActP31800. 3 interactions.
MINTMINT-149960.
STRING9913.ENSBTAP00000025422.

Protein family/group databases

MEROPSM16.973.

Proteomic databases

PaxDbP31800.
PRIDEP31800.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID282393.
KEGGbta:282393.

Organism-specific databases

CTD7384.

Phylogenomic databases

eggNOGCOG0612.
HOGENOMHOG000242450.
HOVERGENHBG006393.
InParanoidP31800.
KOK00414.

Family and domain databases

Gene3D3.30.830.10. 2 hits.
InterProIPR011249. Metalloenz_LuxS/M16.
IPR011237. Pept_M16_dom.
IPR011765. Pept_M16_N.
IPR007863. Peptidase_M16_C.
[Graphical view]
PfamPF00675. Peptidase_M16. 1 hit.
PF05193. Peptidase_M16_C. 1 hit.
[Graphical view]
SUPFAMSSF63411. SSF63411. 2 hits.
ProtoNetSearch...

Other

EvolutionaryTraceP31800.
NextBio20806180.

Entry information

Entry nameQCR1_BOVIN
AccessionPrimary (citable) accession number: P31800
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: December 1, 2000
Last modified: April 16, 2014
This is version 125 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references