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P23004 (QCR2_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 122. 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 2, mitochondrial
Alternative name(s):
Complex III subunit 2
Core protein II
Ubiquinol-cytochrome-c reductase complex core protein 2
Gene names
Name:UQCRC2
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length453 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. The core protein 2 is required for the assembly of the complex.

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. UQCRC2/QCR2 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 – 1414Mitochondrion Ref.4 Ref.5
Chain15 – 453439Cytochrome b-c1 complex subunit 2, mitochondrial
PRO_0000026790

Amino acid modifications

Modified residue661N6-acetyllysine By similarity
Modified residue1991N6-acetyllysine By similarity
Modified residue2501N6-acetyllysine By similarity

Natural variations

Natural variant411T → R.

Secondary structure

.......................................................................... 453
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P23004 [UniParc].

Last modified July 1, 1993. Version 2.
Checksum: B7C600DA71CD34CF

FASTA45348,149
        10         20         30         40         50         60 
MKLLTRAGSL SRFYSLKVAP KVKATEAPAG VPPHPQDLEF TRLPNGLVIA SLENYAPASR 

        70         80         90        100        110        120 
IGLFIKAGSR YENSNNLGTS HLLRLASSLT TKGASSFKIT RGIEAVGGKL SVTSTRENMA 

       130        140        150        160        170        180 
YTVECLRDDV DILMEFLLNV TTAPEFRRWE VAALQPQLRI DKAVALQNPQ AHVIENLHAA 

       190        200        210        220        230        240 
AYRNALANSL YCPDYRIGKV TPVELHDYVQ NHFTSARMAL IGLGVSHPVL KQVAEQFLNI 

       250        260        270        280        290        300 
RGGLGLSGAK AKYHGGEIRE QNGDSLVHAA LVAESAAIGS AEANAFSVLQ HVLGAGPHVK 

       310        320        330        340        350        360 
RGSNATSSLY QAVAKGVHQP FDVSAFNASY SDSGLFGFYT ISQAASAGDV IKAAYNQVKT 

       370        380        390        400        410        420 
IAQGNLSNPD VQAAKNKLKA GYLMSVESSE GFLDEVGSQA LAAGSYTPPS TVLQQIDAVA 

       430        440        450 
DADVINAAKK FVSGRKSMAA SGNLGHTPFI DEL 

« Hide

References

« Hide 'large scale' 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]"Characterization of 954 bovine full-CDS cDNA sequences."
Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L., Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.
BMC Genomics 6:166-166(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]NIH - Mammalian Gene Collection (MGC) project
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Crossbred X Angus.
Tissue: Ileum.
[4]"Complexity and tissue specificity of the mitochondrial respiratory chain."
Capaldi R.A., Gonzalez-Halphen D., Zhang Y.-Z., Yanamura W.
J. Bioenerg. Biomembr. 20:291-311(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 15-46.
[5]"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 15-43.
[6]"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).
[7]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)
[8]"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).
[9]"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).
[10]"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).
[11]"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).
[12]"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
X59693 mRNA. Translation: CAA42214.1.
BT020993 mRNA. Translation: AAX09010.1.
BC102337 mRNA. Translation: AAI02338.1.
PIRZPBOC2. S16221.
RefSeqNP_777055.1. NM_174630.2.
UniGeneBt.27799.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1BCCX-ray3.16B32-453[»]
1BE3X-ray3.00B15-453[»]
1BGYX-ray3.00B/N15-453[»]
1L0LX-ray2.35B15-453[»]
1L0NX-ray2.60B15-453[»]
1NTKX-ray2.60B15-453[»]
1NTMX-ray2.40B15-453[»]
1NTZX-ray2.60B15-453[»]
1NU1X-ray3.20B15-453[»]
1PP9X-ray2.10B/O15-453[»]
1PPJX-ray2.10B/O15-453[»]
1QCRX-ray2.70B31-453[»]
1SQBX-ray2.69B1-453[»]
1SQPX-ray2.70B1-453[»]
1SQQX-ray3.00B15-453[»]
1SQVX-ray2.85B15-453[»]
1SQXX-ray2.60B15-453[»]
2A06X-ray2.10B/O15-453[»]
2BCCX-ray3.50B32-453[»]
2FYUX-ray2.26B15-453[»]
2YBBelectron microscopy19.00B/b15-453[»]
3BCCX-ray3.70B32-453[»]
ProteinModelPortalP23004.
SMRP23004. Positions 29-453.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-1106N.
IntActP23004. 2 interactions.
MINTMINT-149969.

Protein family/group databases

MEROPSM16.974.

Proteomic databases

PaxDbP23004.
PRIDEP23004.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSBTAT00000028853; ENSBTAP00000028853; ENSBTAG00000021651.
GeneID282394.
KEGGbta:282394.

Organism-specific databases

CTD7385.

Phylogenomic databases

eggNOGCOG0612.
GeneTreeENSGT00550000074666.
HOGENOMHOG000046923.
HOVERGENHBG055236.
InParanoidP23004.
KOK00415.
OMAQFVQNNF.
OrthoDBEOG79CXZF.
TreeFamTF105033.

Family and domain databases

Gene3D3.30.830.10. 2 hits.
InterProIPR011249. Metalloenz_LuxS/M16.
IPR011237. Pept_M16_dom.
IPR011765. Pept_M16_N.
IPR001431. Pept_M16_Zn_BS.
IPR007863. Peptidase_M16_C.
[Graphical view]
PfamPF00675. Peptidase_M16. 1 hit.
PF05193. Peptidase_M16_C. 1 hit.
[Graphical view]
SUPFAMSSF63411. SSF63411. 3 hits.
PROSITEPS00143. INSULINASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP23004.
NextBio20806181.

Entry information

Entry nameQCR2_BOVIN
AccessionPrimary (citable) accession number: P23004
Secondary accession number(s): Q3ZCG7, Q5E9C7
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: July 1, 1993
Last modified: February 19, 2014
This is version 122 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