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P31800

- QCR1_BOVIN

UniProt

P31800 - QCR1_BOVIN

Protein

Cytochrome b-c1 complex subunit 1, mitochondrial

Gene

UQCRC1

Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 126 (01 Oct 2014)
      Sequence version 2 (01 Dec 2000)
      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. This protein may mediate formation of the complex between cytochromes c and c1.

    GO - Molecular functioni

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

    GO - Biological processi

    1. oxidation-reduction process Source: UniProtKB-KW

    Keywords - Biological processi

    Electron transport, Respiratory chain, Transport

    Protein family/group databases

    MEROPSiM16.973.

    Names & Taxonomyi

    Protein namesi
    Recommended 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 namesi
    Name:UQCRC1
    OrganismiBos taurus (Bovine)
    Taxonomic identifieri9913 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
    ProteomesiUP000009136: Unplaced

    Subcellular locationi

    GO - Cellular componenti

    1. mitochondrial inner membrane Source: AgBase
    2. mitochondrion Source: AgBase
    3. 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 – 3434Mitochondrion1 PublicationAdd
    BLAST
    Chaini35 – 480446Cytochrome b-c1 complex subunit 1, mitochondrialPRO_0000026785Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei111 – 1111N6-acetyllysineBy similarity
    Modified residuei138 – 1381N6-acetyllysineBy similarity
    Modified residuei163 – 1631N6-acetyllysine; alternateBy similarity
    Modified residuei163 – 1631N6-succinyllysine; alternateBy similarity
    Modified residuei248 – 2481N6-acetyllysineBy similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    PaxDbiP31800.
    PRIDEiP31800.

    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-1105N.
    IntActiP31800. 3 interactions.
    MINTiMINT-149960.
    STRINGi9913.ENSBTAP00000025422.

    Structurei

    Secondary structure

    1
    480
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi38 – 425
    Beta strandi49 – 524
    Beta strandi54 – 563
    Beta strandi58 – 636
    Beta strandi67 – 7610
    Helixi79 – 813
    Turni84 – 885
    Helixi89 – 968
    Beta strandi97 – 993
    Beta strandi101 – 1044
    Turni105 – 1073
    Helixi108 – 1158
    Beta strandi119 – 1246
    Beta strandi129 – 1368
    Helixi137 – 1393
    Helixi140 – 15314
    Helixi158 – 17518
    Helixi179 – 19113
    Turni192 – 1943
    Helixi196 – 1983
    Helixi205 – 2106
    Helixi213 – 22311
    Helixi226 – 2283
    Beta strandi229 – 2368
    Helixi239 – 25012
    Beta strandi252 – 2565
    Beta strandi259 – 2613
    Beta strandi273 – 2797
    Beta strandi282 – 29312
    Helixi301 – 31111
    Beta strandi313 – 3153
    Helixi321 – 3233
    Helixi327 – 3359
    Beta strandi339 – 3479
    Beta strandi352 – 3609
    Helixi362 – 3643
    Helixi365 – 38218
    Helixi385 – 40218
    Helixi406 – 41914
    Helixi426 – 4349
    Helixi438 – 44811
    Turni449 – 4513
    Beta strandi455 – 4617
    Helixi462 – 4643
    Helixi468 – 4736

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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[»]
    ProteinModelPortaliP31800.
    SMRiP31800. Positions 35-480.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP31800.

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG0612.
    HOGENOMiHOG000242450.
    HOVERGENiHBG006393.
    InParanoidiP31800.
    KOiK00414.

    Family and domain databases

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

    Sequencei

    Sequence statusi: Complete.

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

    P31800-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAASAVCRAA GAGTRVLLRT RRSPALLRSS DLRGTATYAQ ALQSVPETQV    50
    SQLDNGLRVA SEQSSQPTCT VGVWIDAGSR YESEKNNGAG YFVEHLAFKG 100
    TKNRPGNALE KEVESMGAHL NAYSTREHTA YYIKALSKDL PKAVELLADI 150
    VQNCSLEDSQ IEKERDVILQ ELQENDTSMR DVVFNYLHAT AFQGTPLAQS 200
    VEGPSENVRK LSRADLTEYL SRHYKAPRMV LAAAGGLEHR QLLDLAQKHF 250
    SGLSGTYDED AVPTLSPCRF TGSQICHRED GLPLAHVAIA VEGPGWAHPD 300
    NVALQVANAI IGHYDCTYGG GAHLSSPLAS IAATNKLCQS FQTFNICYAD 350
    TGLLGAHFVC DHMSIDDMMF VLQGQWMRLC TSATESEVLR GKNLLRNALV 400
    SHLDGTTPVC EDIGRSLLTY GRRIPLAEWE SRIAEVDARV VREVCSKYFY 450
    DQCPAVAGFG PIEQLPDYNR IRSGMFWLRF 480
    Length:480
    Mass (Da):52,736
    Last modified:December 1, 2000 - v2
    Checksum:i4E54DD28C1905392
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X59692 mRNA. Translation: CAA42213.1.
    PIRiS16220. ZPBOC1.
    RefSeqiNP_777054.1. NM_174629.2.
    UniGeneiBt.23164.

    Genome annotation databases

    GeneIDi282393.
    KEGGibta:282393.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X59692 mRNA. Translation: CAA42213.1 .
    PIRi S16220. ZPBOC1.
    RefSeqi NP_777054.1. NM_174629.2.
    UniGenei Bt.23164.

    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 A 35-480 [» ]
    1BE3 X-ray 3.00 A 35-480 [» ]
    1BGY X-ray 3.00 A/M 35-480 [» ]
    1L0L X-ray 2.35 A 35-480 [» ]
    1L0N X-ray 2.60 A 35-480 [» ]
    1NTK X-ray 2.60 A 35-480 [» ]
    1NTM X-ray 2.40 A 35-480 [» ]
    1NTZ X-ray 2.60 A 35-480 [» ]
    1NU1 X-ray 3.20 A 35-480 [» ]
    1PP9 X-ray 2.10 A/N 35-480 [» ]
    1PPJ X-ray 2.10 A/N 35-480 [» ]
    1QCR X-ray 2.70 A 35-480 [» ]
    1SQB X-ray 2.69 A 1-480 [» ]
    1SQP X-ray 2.70 A 1-480 [» ]
    1SQQ X-ray 3.00 A 35-480 [» ]
    1SQV X-ray 2.85 A 35-480 [» ]
    1SQX X-ray 2.60 A 35-480 [» ]
    2A06 X-ray 2.10 A/N 35-480 [» ]
    2BCC X-ray 3.50 A 35-480 [» ]
    2FYU X-ray 2.26 A 35-480 [» ]
    2YBB electron microscopy 19.00 A/a 35-480 [» ]
    3BCC X-ray 3.70 A 35-480 [» ]
    ProteinModelPortali P31800.
    SMRi P31800. Positions 35-480.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-1105N.
    IntActi P31800. 3 interactions.
    MINTi MINT-149960.
    STRINGi 9913.ENSBTAP00000025422.

    Protein family/group databases

    MEROPSi M16.973.

    Proteomic databases

    PaxDbi P31800.
    PRIDEi P31800.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 282393.
    KEGGi bta:282393.

    Organism-specific databases

    CTDi 7384.

    Phylogenomic databases

    eggNOGi COG0612.
    HOGENOMi HOG000242450.
    HOVERGENi HBG006393.
    InParanoidi P31800.
    KOi K00414.

    Miscellaneous databases

    EvolutionaryTracei P31800.
    NextBioi 20806180.

    Family and domain databases

    Gene3Di 3.30.830.10. 2 hits.
    InterProi IPR011249. Metalloenz_LuxS/M16.
    IPR011237. Pept_M16_dom.
    IPR011765. Pept_M16_N.
    IPR007863. Peptidase_M16_C.
    [Graphical view ]
    Pfami PF00675. Peptidase_M16. 1 hit.
    PF05193. Peptidase_M16_C. 1 hit.
    [Graphical view ]
    SUPFAMi SSF63411. SSF63411. 2 hits.
    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. "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. 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).

    Entry informationi

    Entry nameiQCR1_BOVIN
    AccessioniPrimary (citable) accession number: P31800
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1993
    Last sequence update: December 1, 2000
    Last modified: October 1, 2014
    This is version 126 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