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 02-SEP-2026, entry version 171. 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 (Probable) (PubMed:3015618). 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:18251112, PubMed:226365, PubMed:6273583, 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 FunCoup; P07056; 773. DR STRING; 367110.P07056; -. DR PaxDb; 367110-P07056; -. 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 OrthoDB; 1637982at2759; -. DR Proteomes; UP000001805; Chromosome 4, Linkage Group IV. DR GO; GO:0005743; C:mitochondrial inner membrane; EXP:UniProtKB. DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:InterPro. DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central. DR GO; GO:0008121; F:quinol-cytochrome-c reductase activity; EXP:UniProtKB. DR GO; GO:0006122; P:mitochondrial electron transport, ubiquinol to cytochrome c; IBA:GO_Central. DR CDD; cd03470; Rieske_cytochrome_bc1; 1. DR FunFam; 1.20.5.270:FF:000002; Cytochrome b-c1 complex subunit Rieske, mitochondrial; 1. DR FunFam; 2.102.10.10:FF:000001; Cytochrome b-c1 complex subunit Rieske, mitochondrial; 1. DR Gene3D; 2.102.10.10; Rieske [2Fe-2S] iron-sulphur domain; 1. DR Gene3D; 1.20.5.270; Ubiquinol cytochrome reductase, transmembrane domain; 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 NCBIfam; TIGR01416; Rieske_proteo; 1. DR PANTHER; PTHR10134; CYTOCHROME B-C1 COMPLEX SUBUNIT RIESKE, MITOCHONDRIAL; 1. DR Pfam; PF00355; Rieske; 1. DR Pfam; PF02921; UCR_TM; 1. DR PRINTS; PR00162; RIESKE. DR SUPFAM; SSF50022; ISP domain; 1. DR SUPFAM; SSF81502; ISP transmembrane anchor; 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 //