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P23004

- QCR2_BOVIN

UniProt

P23004 - QCR2_BOVIN

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
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    • History
      Entry version 124 (01 Oct 2014)
      Sequence version 2 (01 Jul 1993)
      Previous versions | rss
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    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

    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. mitochondrial inner membrane Source: UniProtKB-SubCell
    2. respiratory chain Source: UniProtKB-KW

    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

    MKLLTRAGSL SRFYSLKVAP KVKATEAPAG VPPHPQDLEF TRLPNGLVIA    50
    SLENYAPASR IGLFIKAGSR YENSNNLGTS HLLRLASSLT TKGASSFKIT 100
    RGIEAVGGKL SVTSTRENMA YTVECLRDDV DILMEFLLNV TTAPEFRRWE 150
    VAALQPQLRI DKAVALQNPQ AHVIENLHAA AYRNALANSL YCPDYRIGKV 200
    TPVELHDYVQ NHFTSARMAL IGLGVSHPVL KQVAEQFLNI RGGLGLSGAK 250
    AKYHGGEIRE QNGDSLVHAA LVAESAAIGS AEANAFSVLQ HVLGAGPHVK 300
    RGSNATSSLY QAVAKGVHQP FDVSAFNASY SDSGLFGFYT ISQAASAGDV 350
    IKAAYNQVKT IAQGNLSNPD VQAAKNKLKA GYLMSVESSE GFLDEVGSQA 400
    LAAGSYTPPS TVLQQIDAVA DADVINAAKK FVSGRKSMAA SGNLGHTPFI 450
    DEL 453
    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

    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 1, 2014
    This is version 124 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