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P13272

- UCRI_BOVIN

UniProt

P13272 - UCRI_BOVIN

Protein

Cytochrome b-c1 complex subunit Rieske, mitochondrial

Gene

UQCRFS1

Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 138 (01 Oct 2014)
      Sequence version 3 (01 Feb 1996)
      Previous versions | rss
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    Functioni

    Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is a respiratory chain that generates an electrochemical potential coupled to ATP synthesis.
    The transit peptide of the Rieske protein seems to form part of the bc1 complex and is considered to be the subunit 11/IX of that complex.

    Catalytic activityi

    Quinol + 2 ferricytochrome c = quinone + 2 ferrocytochrome c + 2 H+.

    Cofactori

    Binds 1 2Fe-2S cluster per subunit.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi217 – 2171Iron-sulfur (2Fe-2S)
    Metal bindingi219 – 2191Iron-sulfur (2Fe-2S); via pros nitrogen
    Metal bindingi236 – 2361Iron-sulfur (2Fe-2S)
    Metal bindingi239 – 2391Iron-sulfur (2Fe-2S); via pros nitrogen

    GO - Molecular functioni

    1. 2 iron, 2 sulfur cluster binding Source: UniProtKB-KW
    2. metal ion binding Source: UniProtKB-KW
    3. ubiquinol-cytochrome-c reductase activity Source: UniProtKB-EC

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Electron transport, Respiratory chain, Transport

    Keywords - Ligandi

    2Fe-2S, Iron, Iron-sulfur, Metal-binding

    Protein family/group databases

    TCDBi3.D.3.2.1. the proton-translocating quinol:cytochrome c reductase (qcr) superfamily.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Cytochrome b-c1 complex subunit Rieske, mitochondrial (EC:1.10.2.2)
    Alternative name(s):
    Complex III subunit 5
    Cytochrome b-c1 complex subunit 5
    Rieske iron-sulfur protein
    Short name:
    RISP
    Ubiquinol-cytochrome c reductase iron-sulfur subunit
    Cleaved into the following chain:
    Alternative name(s):
    Complex III subunit IX
    Ubiquinol-cytochrome c reductase 8 kDa protein
    Gene namesi
    Name:UQCRFS1
    OrganismiBos taurus (Bovine)
    Taxonomic identifieri9913 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
    ProteomesiUP000009136: Unplaced

    Subcellular locationi

    GO - Cellular componenti

    1. integral component of membrane Source: UniProtKB-KW
    2. mitochondrial inner membrane Source: AgBase
    3. mitochondrion Source: AgBase
    4. 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 – 7878Mitochondrion2 PublicationsAdd
    BLAST
    Chaini1 – 7878Cytochrome b-c1 complex subunit 11PRO_0000030659Add
    BLAST
    Chaini79 – 274196Cytochrome b-c1 complex subunit Rieske, mitochondrialPRO_0000030660Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi222 ↔ 2381 PublicationPROSITE-ProRule annotation

    Keywords - PTMi

    Disulfide bond

    Proteomic databases

    PRIDEiP13272.

    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

    IntActiP13272. 3 interactions.

    Structurei

    Secondary structure

    1
    274
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi5 – 73
    Beta strandi8 – 103
    Beta strandi12 – 198
    Beta strandi22 – 243
    Beta strandi27 – 293
    Helixi30 – 334
    Beta strandi34 – 363
    Beta strandi43 – 453
    Helixi52 – 554
    Beta strandi65 – 728
    Beta strandi75 – 773
    Helixi80 – 823
    Turni89 – 913
    Helixi94 – 963
    Beta strandi99 – 1013
    Helixi104 – 14037
    Helixi144 – 1474
    Beta strandi150 – 1556
    Helixi156 – 1583
    Beta strandi164 – 1696
    Beta strandi172 – 1787
    Helixi181 – 1888
    Helixi192 – 1943
    Beta strandi195 – 1973
    Helixi201 – 2033
    Beta strandi205 – 2073
    Beta strandi210 – 2145
    Turni218 – 2203
    Beta strandi225 – 2273
    Turni229 – 2313
    Beta strandi232 – 2365
    Turni237 – 2404
    Beta strandi241 – 2444
    Beta strandi245 – 2473
    Beta strandi249 – 2535
    Beta strandi263 – 27311

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1BCCX-ray3.16A192-195[»]
    E79-274[»]
    1BE3X-ray3.00E79-274[»]
    I1-78[»]
    1BGYX-ray3.00E/Q79-274[»]
    I/U1-78[»]
    1L0LX-ray2.35E79-274[»]
    I1-78[»]
    1L0NX-ray2.60E79-274[»]
    I1-78[»]
    1NTKX-ray2.60E79-274[»]
    I1-57[»]
    1NTMX-ray2.40E79-274[»]
    I1-57[»]
    1NTZX-ray2.60E79-274[»]
    I1-57[»]
    1NU1X-ray3.20E79-274[»]
    I1-57[»]
    1PP9X-ray2.10E/R79-274[»]
    I/V1-78[»]
    1PPJX-ray2.10E/R79-274[»]
    I/V1-78[»]
    1QCRX-ray2.70E79-274[»]
    I21-48[»]
    1RIEX-ray1.50A146-274[»]
    1SQBX-ray2.69E79-274[»]
    I1-78[»]
    1SQPX-ray2.70E79-274[»]
    I1-78[»]
    1SQQX-ray3.00E79-274[»]
    I1-78[»]
    1SQVX-ray2.85E79-274[»]
    I1-78[»]
    1SQXX-ray2.60E79-274[»]
    I1-78[»]
    2A06X-ray2.10E/R79-274[»]
    I/V1-78[»]
    2FYUX-ray2.26E79-274[»]
    I1-78[»]
    2YBBelectron microscopy19.00E/e79-274[»]
    I/i14-78[»]
    ProteinModelPortaliP13272.
    SMRiP13272. Positions 1-57, 79-274.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP13272.

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei103 – 14038HelicalAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini187 – 27286RieskePROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 Rieske domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Transit peptide, Transmembrane, Transmembrane helix

    Phylogenomic databases

    HOVERGENiHBG001040.
    KOiK00411.

    Family and domain databases

    Gene3Di1.20.5.270. 1 hit.
    2.102.10.10. 1 hit.
    InterProiIPR011070. Globular_prot_asu/bsu.
    IPR017941. Rieske_2Fe-2S.
    IPR014349. Rieske_Fe-S_prot.
    IPR005805. Rieske_Fe-S_prot_C.
    IPR015248. Ubiqinol_cyt_c_Rdtase_N.
    IPR006317. Ubiquinol_cyt_c_Rdtase_Fe-S-su.
    IPR004192. Ubiquinol_cyt_Rdtase_TM.
    [Graphical view]
    PANTHERiPTHR10134. PTHR10134. 1 hit.
    PfamiPF00355. Rieske. 1 hit.
    PF09165. Ubiq-Cytc-red_N. 1 hit.
    PF02921. UCR_TM. 1 hit.
    [Graphical view]
    PRINTSiPR00162. RIESKE.
    SUPFAMiSSF50022. SSF50022. 1 hit.
    SSF56568. SSF56568. 1 hit.
    TIGRFAMsiTIGR01416. Rieske_proteo. 1 hit.
    PROSITEiPS51296. RIESKE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P13272-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLSVAARSGP FAPVLSATSR GVAGALRPLV QAAVPATSES PVLDLKRSVL    50
    CRESLRGQAA GRPLVASVSL NVPASVRYSH TDIKVPDFSD YRRPEVLDST 100
    KSSKESSEAR KGFSYLVTAT TTVGVAYAAK NVVSQFVSSM SASADVLAMS 150
    KIEIKLSDIP EGKNMAFKWR GKPLFVRHRT KKEIDQEAAV EVSQLRDPQH 200
    DLERVKKPEW VILIGVCTHL GCVPIANAGD FGGYYCPCHG SHYDASGRIR 250
    KGPAPLNLEV PSYEFTSDDM VIVG 274
    Length:274
    Mass (Da):29,547
    Last modified:February 1, 1996 - v3
    Checksum:i7C5FC17D2A0DD1C9
    GO

    Sequence cautioni

    The sequence AAA30515.1 differs from that shown. Reason: Frameshift at several positions.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti150 – 1501S → A AA sequence (PubMed:3036596)Curated
    Sequence conflicti269 – 2691D → G AA sequence (PubMed:3036596)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M34336 mRNA. Translation: AAA30515.1. Sequence problems.
    S58789 mRNA. Translation: AAB26197.1.
    BC115994 mRNA. Translation: AAI15995.1.
    BC133620 mRNA. Translation: AAI33621.1.
    BC133632 mRNA. Translation: AAI33633.1.
    PIRiA46063. A34660.
    RefSeqiNP_777238.1. NM_174813.2.
    UniGeneiBt.265.

    Genome annotation databases

    GeneIDi287020.
    KEGGibta:287020.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M34336 mRNA. Translation: AAA30515.1 . Sequence problems.
    S58789 mRNA. Translation: AAB26197.1 .
    BC115994 mRNA. Translation: AAI15995.1 .
    BC133620 mRNA. Translation: AAI33621.1 .
    BC133632 mRNA. Translation: AAI33633.1 .
    PIRi A46063. A34660.
    RefSeqi NP_777238.1. NM_174813.2.
    UniGenei Bt.265.

    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 192-195 [» ]
    E 79-274 [» ]
    1BE3 X-ray 3.00 E 79-274 [» ]
    I 1-78 [» ]
    1BGY X-ray 3.00 E/Q 79-274 [» ]
    I/U 1-78 [» ]
    1L0L X-ray 2.35 E 79-274 [» ]
    I 1-78 [» ]
    1L0N X-ray 2.60 E 79-274 [» ]
    I 1-78 [» ]
    1NTK X-ray 2.60 E 79-274 [» ]
    I 1-57 [» ]
    1NTM X-ray 2.40 E 79-274 [» ]
    I 1-57 [» ]
    1NTZ X-ray 2.60 E 79-274 [» ]
    I 1-57 [» ]
    1NU1 X-ray 3.20 E 79-274 [» ]
    I 1-57 [» ]
    1PP9 X-ray 2.10 E/R 79-274 [» ]
    I/V 1-78 [» ]
    1PPJ X-ray 2.10 E/R 79-274 [» ]
    I/V 1-78 [» ]
    1QCR X-ray 2.70 E 79-274 [» ]
    I 21-48 [» ]
    1RIE X-ray 1.50 A 146-274 [» ]
    1SQB X-ray 2.69 E 79-274 [» ]
    I 1-78 [» ]
    1SQP X-ray 2.70 E 79-274 [» ]
    I 1-78 [» ]
    1SQQ X-ray 3.00 E 79-274 [» ]
    I 1-78 [» ]
    1SQV X-ray 2.85 E 79-274 [» ]
    I 1-78 [» ]
    1SQX X-ray 2.60 E 79-274 [» ]
    I 1-78 [» ]
    2A06 X-ray 2.10 E/R 79-274 [» ]
    I/V 1-78 [» ]
    2FYU X-ray 2.26 E 79-274 [» ]
    I 1-78 [» ]
    2YBB electron microscopy 19.00 E/e 79-274 [» ]
    I/i 14-78 [» ]
    ProteinModelPortali P13272.
    SMRi P13272. Positions 1-57, 79-274.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P13272. 3 interactions.

    Protein family/group databases

    TCDBi 3.D.3.2.1. the proton-translocating quinol:cytochrome c reductase (qcr) superfamily.

    Proteomic databases

    PRIDEi P13272.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 287020.
    KEGGi bta:287020.

    Organism-specific databases

    CTDi 7386.

    Phylogenomic databases

    HOVERGENi HBG001040.
    KOi K00411.

    Miscellaneous databases

    EvolutionaryTracei P13272.
    NextBioi 20806543.

    Family and domain databases

    Gene3Di 1.20.5.270. 1 hit.
    2.102.10.10. 1 hit.
    InterProi IPR011070. Globular_prot_asu/bsu.
    IPR017941. Rieske_2Fe-2S.
    IPR014349. Rieske_Fe-S_prot.
    IPR005805. Rieske_Fe-S_prot_C.
    IPR015248. Ubiqinol_cyt_c_Rdtase_N.
    IPR006317. Ubiquinol_cyt_c_Rdtase_Fe-S-su.
    IPR004192. Ubiquinol_cyt_Rdtase_TM.
    [Graphical view ]
    PANTHERi PTHR10134. PTHR10134. 1 hit.
    Pfami PF00355. Rieske. 1 hit.
    PF09165. Ubiq-Cytc-red_N. 1 hit.
    PF02921. UCR_TM. 1 hit.
    [Graphical view ]
    PRINTSi PR00162. RIESKE.
    SUPFAMi SSF50022. SSF50022. 1 hit.
    SSF56568. SSF56568. 1 hit.
    TIGRFAMsi TIGR01416. Rieske_proteo. 1 hit.
    PROSITEi PS51296. RIESKE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and sequencing of a cDNA encoding the Rieske iron-sulfur protein of bovine heart mitochondrial ubiquinol-cytochrome c reductase."
      Usui S., Yu L., Yu C.-A.
      Biochem. Biophys. Res. Commun. 167:575-579(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Heart.
    2. "The mitochondrial targeting presequence of the Rieske iron-sulfur protein is processed in a single step after insertion into the cytochrome bc1 complex in mammals and retained as a subunit in the complex."
      Brandt U., Yu L., Yu C.-A., Trumpower B.L.
      J. Biol. Chem. 268:8387-8390(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], SEQUENCE REVISION.
      Tissue: Heart.
    3. NIH - Mammalian Gene Collection (MGC) project
      Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: Crossbred X Angus and Hereford.
      Tissue: Fetal brain, Fetal cerebellum and Liver.
    4. "Isolation and amino acid sequence of the 8 kDa DCCD-binding protein of beef heart ubiquinol:cytochrome c reductase."
      Borchart U., Machleidt W., Schagger H., Link T.A., von Jagow G.
      FEBS Lett. 191:125-130(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 1-78.
      Tissue: Heart.
    5. "Isolation and amino acid sequence of the 'Rieske' iron sulfur protein of beef heart ubiquinol:cytochrome c reductase."
      Schaegger H., Borchart U., Machleidt W., Link T.A., von Jagow G.
      FEBS Lett. 219:161-168(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 79-274.
    6. "Structure of a water soluble fragment of the 'Rieske' iron-sulfur protein of the bovine heart mitochondrial cytochrome bc1 complex determined by MAD phasing at 1.5-A resolution."
      Iwata S., Saynovits M., Link T.A., Michel H.
      Structure 4:567-579(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 148-274.
    7. "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).
    8. 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)
    9. "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).
    10. "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).
    11. "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).
    12. "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).
    13. "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 nameiUCRI_BOVIN
    AccessioniPrimary (citable) accession number: P13272
    Secondary accession number(s): A3KN53, P07588, Q1LZH6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1988
    Last sequence update: February 1, 1996
    Last modified: October 1, 2014
    This is version 138 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    The Rieske protein is a high potential 2Fe-2S protein.

    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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3