UCRI_NEUCR
ID UCRI_NEUCR Reviewed; 231 AA.
AC P07056; Q7S9Q9;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1988, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Cytochrome b-c1 complex subunit Rieske, mitochondrial;
DE EC=7.1.1.8 {ECO:0000269|PubMed:1847681, ECO:0000269|PubMed:19239619, ECO:0000269|PubMed:3015618};
DE AltName: Full=Complex III subunit 5;
DE AltName: Full=Complex III subunit V {ECO:0000303|PubMed:6302289};
DE AltName: Full=Rieske iron-sulfur protein;
DE Short=RISP;
DE AltName: Full=Ubiquinol-cytochrome c oxidoreductase iron-sulfur subunit;
DE AltName: Full=Ubiquinol-cytochrome c reductase complex 25 kDa protein;
DE Flags: Precursor;
GN Name=fes-1; ORFNames=NCU06606;
OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS FGSC 987).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=367110;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 33-56.
RX PubMed=2986972; DOI=10.1111/j.1432-1033.1985.tb08898.x;
RA Harnisch U., Weiss H., Sebald W.;
RT "The primary structure of the iron-sulfur subunit of ubiquinol-cytochrome c
RT reductase from Neurospora, determined by cDNA and gene sequencing.";
RL Eur. J. Biochem. 149:95-99(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12712197; DOI=10.1038/nature01554;
RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT "The genome sequence of the filamentous fungus Neurospora crassa.";
RL Nature 422:859-868(2003).
RN [3]
RP PROTEIN SEQUENCE OF 25-57.
RX PubMed=3022944; DOI=10.1016/0092-8674(86)90809-3;
RA Hartl F.U., Schmidt B., Wachter E., Weiss H., Neupert W.;
RT "Transport into mitochondria and intramitochondrial sorting of the Fe/S
RT protein of ubiquinol-cytochrome c reductase.";
RL Cell 47:939-951(1986).
RN [4]
RP SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=226365; DOI=10.1111/j.1432-1033.1979.tb13240.x;
RA Weiss H., Kolb H.J.;
RT "Isolation of mitochondrial succinate: ubiquinone reductase, cytochrome c
RT reductase and cytochrome c oxidase from Neurospora crassa using nonionic
RT detergent.";
RL Eur. J. Biochem. 99:139-149(1979).
RN [5]
RP SUBUNIT.
RX PubMed=6273583; DOI=10.1016/0022-2836(81)90301-6;
RA Leonard K., Wingfield P., Arad T., Weiss H.;
RT "Three-dimensional structure of ubiquinol:cytochrome c reductase from
RT Neurospora mitochondria determined by electron microscopy of membrane
RT crystals.";
RL J. Mol. Biol. 149:259-274(1981).
RN [6]
RP SUBUNIT.
RX PubMed=18251112; DOI=10.1007/bf00744526;
RA Mendel-Hartvig I., Nelson B.D.;
RT "Comparative study of the peptide composition of Complex III (quinol-
RT cytochrome c reductase).";
RL J. Bioenerg. Biomembr. 15:289-299(1983).
RN [7]
RP SUBUNIT.
RX PubMed=6302289; DOI=10.1016/s0022-2836(83)80258-7;
RA Karlsson B., Hovmoeller S., Weiss H., Leonard K.;
RT "Structural studies of cytochrome reductase. Subunit topography determined
RT by electron microscopy of membrane crystals of a subcomplex.";
RL J. Mol. Biol. 165:287-302(1983).
RN [8]
RP FUNCTION.
RX PubMed=3015618; DOI=10.1111/j.1432-1033.1986.tb09799.x;
RA Linke P., Bechmann G., Gothe A., Weiss H.;
RT "Dimeric ubiquinol:cytochrome c reductase of Neurospora mitochondria
RT contains one cooperative ubiquinone-reduction centre.";
RL Eur. J. Biochem. 158:615-621(1986).
RN [9]
RP FUNCTION OF COMPLEX III.
RX PubMed=1847681; DOI=10.1111/j.1432-1033.1991.tb15722.x;
RA Bechmann G., Weiss H.;
RT "Regulation of the proton/electron stoichiometry of mitochondrial
RT ubiquinol:cytochrome c reductase by the membrane potential.";
RL Eur. J. Biochem. 195:431-438(1991).
RN [10]
RP SUBUNIT, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=17873079; DOI=10.1128/ec.00149-07;
RA Marques I., Dencher N.A., Videira A., Krause F.;
RT "Supramolecular organization of the respiratory chain in Neurospora crassa
RT mitochondria.";
RL Eukaryot. Cell 6:2391-2405(2007).
RN [11]
RP FUNCTION OF COMPLEX III, SUBUNIT, AND DISRUPTION PHENOTYPE.
RX PubMed=19239619; DOI=10.1111/j.1365-2958.2009.06643.x;
RA Duarte M., Videira A.;
RT "Effects of mitochondrial complex III disruption in the respiratory chain
RT of Neurospora crassa.";
RL Mol. Microbiol. 72:246-258(2009).
CC -!- FUNCTION: Component of the ubiquinol-cytochrome c oxidoreductase, a
CC multisubunit transmembrane complex that is part of the mitochondrial
CC electron transport chain which drives oxidative phosphorylation. The
CC respiratory chain contains 3 multisubunit complexes succinate
CC dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase
CC (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase
CC (complex IV, CIV), that cooperate to transfer electrons derived from
CC NADH and succinate to molecular oxygen, creating an electrochemical
CC gradient over the inner membrane that drives transmembrane transport
CC and the ATP synthase. The cytochrome b-c1 complex catalyzes electron
CC transfer from ubiquinol to cytochrome c, linking this redox reaction to
CC translocation of protons across the mitochondrial inner membrane, with
CC protons being carried across the membrane as hydrogens on the quinol.
CC In the process called Q cycle, 2 protons are consumed from the matrix,
CC 4 protons are released into the intermembrane space and 2 electrons are
CC passed to cytochrome c (PubMed:3015618) (Probable). The Rieske protein
CC is a catalytic core subunit containing a [2Fe-2S] iron-sulfur cluster.
CC It cycles between 2 conformational states during catalysis to transfer
CC electrons from the quinol bound in the Q(0) site in cytochrome b to
CC cytochrome c1 (By similarity). {ECO:0000250|UniProtKB:P08067,
CC ECO:0000269|PubMed:3015618, ECO:0000305|PubMed:1847681,
CC ECO:0000305|PubMed:19239619}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a quinol + 2 Fe(III)-[cytochrome c](out) = a quinone + 2
CC Fe(II)-[cytochrome c](out) + 2 H(+)(out); Xref=Rhea:RHEA:11484,
CC Rhea:RHEA-COMP:10350, Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:24646, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034,
CC ChEBI:CHEBI:132124; EC=7.1.1.8; Evidence={ECO:0000269|PubMed:1847681,
CC ECO:0000269|PubMed:19239619, ECO:0000269|PubMed:3015618};
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00628};
CC Note=Binds 1 [2Fe-2S] cluster per subunit. {ECO:0000255|PROSITE-
CC ProRule:PRU00628};
CC -!- SUBUNIT: Component of the ubiquinol-cytochrome c oxidoreductase
CC (cytochrome b-c1 complex, complex III, CIII), a multisubunit enzyme
CC composed of 10 subunits. The complex is composed of 3 respiratory
CC subunits cytochrome b (cob), cytochrome c1 (cyt-1) and Rieske protein
CC (fes-1), 2 core protein subunits pep and ucr-1, and 5 low-molecular
CC weight protein subunits qcr6, qcr7, qcr8, qcr9 and probably
CC NCU16844/qcr10 (PubMed:226365, PubMed:6273583, PubMed:18251112,
CC PubMed:6302289). The complex exists as an obligatory dimer and forms
CC supercomplexes (SCs) in the inner mitochondrial membrane with NADH-
CC ubiquinone oxidoreductase (complex I, CI) and cytochrome c oxidase
CC (complex IV, CIV), resulting in different assemblies (supercomplexes
CC SCI(1)III(2), SCIII(2)IV(1) and SCIII(2)IV(2) as well as higher order
CC I(x)III(y)IV(z) megacomplexes) (PubMed:17873079, PubMed:19239619).
CC {ECO:0000269|PubMed:17873079, ECO:0000269|PubMed:18251112,
CC ECO:0000269|PubMed:19239619, ECO:0000269|PubMed:226365,
CC ECO:0000269|PubMed:6273583, ECO:0000269|PubMed:6302289}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:226365}; Single-pass membrane protein
CC {ECO:0000250|UniProtKB:P08067}.
CC -!- PTM: Processed by both the mitochondrial processing peptidase (MPP) and
CC the mitochondrial intermediate protease (MIP). Initially, MPP removes
CC 25 amino acids from the newly imported precursor in the mitochondrial
CC matrix. This proteolytic processing is then followed by a second
CC proteolytic cleavage by MIP, which removes an octapeptide to generate
CC mature-sized Rieske protein. {ECO:0000269|PubMed:3022944}.
CC -!- DISRUPTION PHENOTYPE: Mutants display reduced growth, are female
CC sterile and lack active complex III. {ECO:0000269|PubMed:19239619}.
CC -!- MISCELLANEOUS: The Rieske protein is a high potential 2Fe-2S protein.
CC -!- SIMILARITY: Belongs to the Rieske iron-sulfur protein family.
CC {ECO:0000305}.
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DR EMBL; X02472; CAA26308.1; -; Genomic_DNA.
DR EMBL; CM002239; EAA33112.1; -; Genomic_DNA.
DR PIR; A24612; RDNCUF.
DR RefSeq; XP_962348.1; XM_957255.3.
DR AlphaFoldDB; P07056; -.
DR SMR; P07056; -.
DR STRING; 5141.EFNCRP00000006347; -.
DR EnsemblFungi; EAA33112; EAA33112; NCU06606.
DR GeneID; 3878496; -.
DR KEGG; ncr:NCU06606; -.
DR VEuPathDB; FungiDB:NCU06606; -.
DR HOGENOM; CLU_055690_0_0_1; -.
DR InParanoid; P07056; -.
DR OMA; KRTWLIA; -.
DR Proteomes; UP000001805; Chromosome 4, Linkage Group IV.
DR GO; GO:0005750; C:mitochondrial respiratory chain complex III; IBA:GO_Central.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0008121; F:ubiquinol-cytochrome-c reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0006122; P:mitochondrial electron transport, ubiquinol to cytochrome c; IBA:GO_Central.
DR Gene3D; 1.20.5.270; -; 1.
DR Gene3D; 2.102.10.10; -; 1.
DR InterPro; IPR037008; bc1_Rieske_TM_sf.
DR InterPro; IPR017941; Rieske_2Fe-2S.
DR InterPro; IPR036922; Rieske_2Fe-2S_sf.
DR InterPro; IPR014349; Rieske_Fe-S_prot.
DR InterPro; IPR005805; Rieske_Fe-S_prot_C.
DR InterPro; IPR004192; Rieske_TM.
DR InterPro; IPR006317; Ubiquinol_cyt_c_Rdtase_Fe-S-su.
DR PANTHER; PTHR10134; PTHR10134; 1.
DR Pfam; PF00355; Rieske; 1.
DR Pfam; PF02921; UCR_TM; 1.
DR PRINTS; PR00162; RIESKE.
DR SUPFAM; SSF50022; SSF50022; 1.
DR TIGRFAMs; TIGR01416; Rieske_proteo; 1.
DR PROSITE; PS51296; RIESKE; 1.
PE 1: Evidence at protein level;
KW 2Fe-2S; Direct protein sequencing; Disulfide bond; Electron transport;
KW Iron; Iron-sulfur; Membrane; Metal-binding; Mitochondrion;
KW Mitochondrion inner membrane; Reference proteome; Respiratory chain;
KW Transit peptide; Translocase; Transmembrane; Transmembrane helix;
KW Transport.
FT TRANSIT 1..24
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:2986972"
FT PROPEP 25..32
FT /note="Removed in mature form"
FT /evidence="ECO:0000269|PubMed:3022944"
FT /id="PRO_0000449191"
FT CHAIN 33..231
FT /note="Cytochrome b-c1 complex subunit Rieske,
FT mitochondrial"
FT /id="PRO_0000030681"
FT TOPO_DOM 33..65
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000250|UniProtKB:P08067"
FT TRANSMEM 66..95
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P08067"
FT TOPO_DOM 96..231
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000250|UniProtKB:P08067"
FT DOMAIN 134..229
FT /note="Rieske"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 174
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 176
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 193
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 196
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT DISULFID 179..195
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
SQ SEQUENCE 231 AA; 24771 MW; 66B780FE78227351 CRC64;
MAPVSIVSRA AMRAAAAPAR AVRALTTSTA LQGSSSSTFE SPFKGESKAA KVPDFGKYMS
KAPPSTNMLF SYFMVGTMGA ITAAGAKSTI QEFLKNMSAS ADVLAMAKVE VDLNAIPEGK
NVIIKWRGKP VFIRHRTPAE IEEANKVNVA TLRDPETDAD RVKKPEWLVM LGVCTHLGCV
PIGEAGDYGG WFCPCHGSHY DISGRIRKGP APLNLEIPLY EFPEEGKLVI G
