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P23004

- QCR2_BOVIN

UniProt

P23004 - QCR2_BOVIN

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Protein

Cytochrome b-c1 complex subunit 2, mitochondrial

Gene

UQCRC2

Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

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.

GO - Molecular functioni

  1. metal ion binding Source: InterPro
  2. metalloendopeptidase activity Source: InterPro

GO - Biological processi

  1. oxidation-reduction process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Electron transport, Respiratory chain, Transport

Protein family/group databases

MEROPSiM16.974.

Names & Taxonomyi

Protein namesi
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 namesi
Name:UQCRC2
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
ProteomesiUP000009136: Chromosome 25

Subcellular locationi

GO - Cellular componenti

  1. extracellular vesicular exosome Source: Ensembl
  2. mitochondrial respiratory chain complex III Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion inner membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 1414Mitochondrion2 PublicationsAdd
BLAST
Chaini15 – 453439Cytochrome b-c1 complex subunit 2, mitochondrialPRO_0000026790Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei66 – 661N6-acetyllysineBy similarity
Modified residuei199 – 1991N6-acetyllysineBy similarity
Modified residuei250 – 2501N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP23004.
PRIDEiP23004.

Interactioni

Subunit structurei

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).

Protein-protein interaction databases

DIPiDIP-1106N.
IntActiP23004. 2 interactions.
MINTiMINT-149969.

Structurei

Secondary structure

1
453
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi39 – 424
Beta strandi44 – 463
Beta strandi48 – 525
Beta strandi57 – 6610
Helixi69 – 713
Turni74 – 785
Helixi79 – 857
Turni86 – 883
Beta strandi91 – 944
Helixi96 – 10510
Beta strandi109 – 1146
Beta strandi119 – 1268
Helixi127 – 1293
Helixi130 – 14213
Helixi148 – 16518
Helixi169 – 18113
Beta strandi182 – 1843
Helixi185 – 1873
Helixi194 – 1963
Turni197 – 1993
Helixi202 – 21211
Helixi215 – 2173
Beta strandi218 – 2258
Helixi227 – 23711
Beta strandi246 – 2494
Beta strandi256 – 2616
Beta strandi265 – 27410
Beta strandi278 – 2803
Helixi281 – 29313
Beta strandi298 – 3014
Helixi308 – 3169
Beta strandi321 – 33010
Beta strandi333 – 34311
Helixi344 – 3463
Helixi347 – 36216
Helixi368 – 38518
Helixi389 – 40315
Helixi409 – 4179
Helixi421 – 43313
Beta strandi436 – 4427
Helixi444 – 4463
Helixi450 – 4523

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliP23004.
SMRiP23004. Positions 29-453.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP23004.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0612.
GeneTreeiENSGT00550000074666.
HOGENOMiHOG000046923.
HOVERGENiHBG055236.
InParanoidiP23004.
KOiK00415.
OMAiQFVQNNF.
OrthoDBiEOG79CXZF.
TreeFamiTF105033.

Family and domain databases

Gene3Di3.30.830.10. 2 hits.
InterProiIPR011249. Metalloenz_LuxS/M16.
IPR011237. Pept_M16_dom.
IPR011765. Pept_M16_N.
IPR001431. Pept_M16_Zn_BS.
IPR007863. Peptidase_M16_C.
[Graphical view]
PfamiPF00675. Peptidase_M16. 1 hit.
PF05193. Peptidase_M16_C. 1 hit.
[Graphical view]
SUPFAMiSSF63411. SSF63411. 3 hits.
PROSITEiPS00143. INSULINASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P23004-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKLLTRAGSL SRFYSLKVAP KVKATEAPAG VPPHPQDLEF TRLPNGLVIA
60 70 80 90 100
SLENYAPASR IGLFIKAGSR YENSNNLGTS HLLRLASSLT TKGASSFKIT
110 120 130 140 150
RGIEAVGGKL SVTSTRENMA YTVECLRDDV DILMEFLLNV TTAPEFRRWE
160 170 180 190 200
VAALQPQLRI DKAVALQNPQ AHVIENLHAA AYRNALANSL YCPDYRIGKV
210 220 230 240 250
TPVELHDYVQ NHFTSARMAL IGLGVSHPVL KQVAEQFLNI RGGLGLSGAK
260 270 280 290 300
AKYHGGEIRE QNGDSLVHAA LVAESAAIGS AEANAFSVLQ HVLGAGPHVK
310 320 330 340 350
RGSNATSSLY QAVAKGVHQP FDVSAFNASY SDSGLFGFYT ISQAASAGDV
360 370 380 390 400
IKAAYNQVKT IAQGNLSNPD VQAAKNKLKA GYLMSVESSE GFLDEVGSQA
410 420 430 440 450
LAAGSYTPPS TVLQQIDAVA DADVINAAKK FVSGRKSMAA SGNLGHTPFI

DEL
Length:453
Mass (Da):48,149
Last modified:July 1, 1993 - v2
Checksum:iB7C600DA71CD34CF
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti41 – 411T → R.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X59693 mRNA. Translation: CAA42214.1.
BT020993 mRNA. Translation: AAX09010.1.
BC102337 mRNA. Translation: AAI02338.1.
PIRiS16221. ZPBOC2.
RefSeqiNP_777055.1. NM_174630.2.
UniGeneiBt.27799.

Genome annotation databases

EnsembliENSBTAT00000028853; ENSBTAP00000028853; ENSBTAG00000021651.
GeneIDi282394.
KEGGibta:282394.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X59693 mRNA. Translation: CAA42214.1 .
BT020993 mRNA. Translation: AAX09010.1 .
BC102337 mRNA. Translation: AAI02338.1 .
PIRi S16221. ZPBOC2.
RefSeqi NP_777055.1. NM_174630.2.
UniGenei Bt.27799.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
2BCC X-ray 3.50 B 32-453 [» ]
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 [» ]
ProteinModelPortali P23004.
SMRi P23004. Positions 29-453.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-1106N.
IntActi P23004. 2 interactions.
MINTi MINT-149969.

Protein family/group databases

MEROPSi M16.974.

Proteomic databases

PaxDbi P23004.
PRIDEi P23004.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSBTAT00000028853 ; ENSBTAP00000028853 ; ENSBTAG00000021651 .
GeneIDi 282394.
KEGGi bta:282394.

Organism-specific databases

CTDi 7385.

Phylogenomic databases

eggNOGi COG0612.
GeneTreei ENSGT00550000074666.
HOGENOMi HOG000046923.
HOVERGENi HBG055236.
InParanoidi P23004.
KOi K00415.
OMAi QFVQNNF.
OrthoDBi EOG79CXZF.
TreeFami TF105033.

Miscellaneous databases

EvolutionaryTracei P23004.
NextBioi 20806181.

Family and domain databases

Gene3Di 3.30.830.10. 2 hits.
InterProi IPR011249. Metalloenz_LuxS/M16.
IPR011237. Pept_M16_dom.
IPR011765. Pept_M16_N.
IPR001431. Pept_M16_Zn_BS.
IPR007863. Peptidase_M16_C.
[Graphical view ]
Pfami PF00675. Peptidase_M16. 1 hit.
PF05193. Peptidase_M16_C. 1 hit.
[Graphical view ]
SUPFAMi SSF63411. SSF63411. 3 hits.
PROSITEi PS00143. INSULINASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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. 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).

Entry informationi

Entry nameiQCR2_BOVIN
AccessioniPrimary (citable) accession number: P23004
Secondary accession number(s): Q3ZCG7, Q5E9C7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: July 1, 1993
Last modified: October 29, 2014
This is version 125 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Caution

Does not seem to have a protease activity as it lack the zinc-binding site.Curated

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3