Cytochrome b-c1 complex subunit 2, mitochondrial precursor

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P23004 (QCR2_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 108. History...

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

Documents (3) |

Third-party data

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

Names and origin

Protein names

Recommended 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

Organism

Bos taurus (Bovine)

Taxonomic identifier

9913 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length	453 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	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.

Ontologies

Keywords
Biological process	Electron transport Respiratory chain Transport
Cellular component	Membrane Mitochondrion Mitochondrion inner membrane
Domain	Transit peptide
PTM	Acetylation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	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 inner membrane Inferred from electronic annotation. Source: UniProtKB-SubCell respiratory chain Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	metalloendopeptidase activity Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – 14

Mitochondrion Ref.4 Ref.5

Chain

15 – 453

439

Cytochrome b-c1 complex subunit 2, mitochondrial

PRO_0000026790

Amino acid modifications

Modified residue

250

N6-acetyllysine By similarity

Natural variations

Natural variant

T → R.

Secondary structure

453

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P23004 [UniParc].

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

FASTA

453

48,149

        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' referencesShow '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: 1712295] [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: 16305752] [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: 2841307] [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: 2848575] [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: 9204897] [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: 9651245] [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: 12269811] [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: 15312779] [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: 16024040] [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: 16924113] [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.

IPI

IPI00697827.

PIR

ZPBOC2. S16221.

RefSeq

NP_777055.1. NM_174630.2.

UniGene

Bt.27799.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1BCC	X-ray	3.16	B	32-453	[»]
1BE3	X-ray	3.00	B	15-453	[»]
1BGY	X-ray	3.00	B/N	15-453	[»]
1L0L	X-ray	2.35	B	15-453	[»]
1L0N	X-ray	2.60	B	15-453	[»]
1NTK	X-ray	2.60	B	15-453	[»]
1NTM	X-ray	2.40	B	15-453	[»]
1NTZ	X-ray	2.60	B	15-453	[»]
1NU1	X-ray	3.20	B	15-453	[»]
1PP9	X-ray	2.10	B/O	15-453	[»]
1PPJ	X-ray	2.10	B/O	15-453	[»]
1QCR	X-ray	2.70	B	31-453	[»]
1SQB	X-ray	2.69	B	1-453	[»]
1SQP	X-ray	2.70	B	1-453	[»]
1SQQ	X-ray	3.00	B	15-453	[»]
1SQV	X-ray	2.85	B	15-453	[»]
1SQX	X-ray	2.60	B	15-453	[»]
2A06	X-ray	2.10	B/O	15-453	[»]
2FYU	X-ray	2.26	B	15-453	[»]
2YBB	electron microscopy	19.00	B/b	15-453	[»]
3BCC	X-ray	3.70	B	32-453	[»]

ProteinModelPortal

P23004.

SMR

P23004. Positions 29-453.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-1106N.

IntAct

P23004. 2 interactions.

STRING

P23004.

Protein family/group databases

MEROPS

M16.974.

Proteomic databases

PRIDE

P23004.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSBTAT00000028853; ENSBTAP00000028853; ENSBTAG00000021651.

GeneID

282394.

KEGG

bta:282394.

Organism-specific databases

CTD

7385.

Phylogenomic databases

eggNOG

maNOG05645.

GeneTree

ENSGT00550000074666.

HOVERGEN

HBG055236.

InParanoid

P23004.

OrthoDB

EOG4QRH45.

PhylomeDB

P23004.

Family and domain databases

InterPro

IPR011249. Metalloenz_metal-bd.
IPR011237. Pept_M16_core.
IPR011765. Pept_M16_N.
IPR001431. Pept_M16_Zn_BS.
IPR007863. Peptidase_M16_C.
[Graphical view]

Gene3D

G3DSA:3.30.830.10. Pept_M16_core. 2 hits.

K00415.

Pfam

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

SUPFAM

SSF63411. Metalloenz_metal-bd. 2 hits.

PROSITE

PS00143. INSULINASE. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

QCR2_BOVIN

Accession

Primary (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:	December 14, 2011
This is version 108 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

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·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Amino acid modifications

Natural variations

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

Family and domain databases

Entry information

Relevant documents