QCR2_NEUCR
ID QCR2_NEUCR Reviewed; 454 AA.
AC O60044; Q7RWQ2; Q8WZH3;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2004, sequence version 2.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Cytochrome b-c1 complex subunit 2, mitochondrial;
DE AltName: Full=Complex III subunit II {ECO:0000303|PubMed:6302289};
DE AltName: Full=Core protein II;
DE AltName: Full=Ubiquinol-cytochrome c oxidoreductase complex core protein 2;
DE AltName: Full=Ubiquinol-cytochrome c reductase complex 45 kDa protein;
DE Flags: Precursor;
GN Name=ucr-1; ORFNames=B7N14.100, NCU03559;
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 [MRNA].
RA Brumme S., Schmitz U.K., Braun H.P.;
RT "The core II protein from Neurospora crassa.";
RL Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases.
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=12655011; DOI=10.1093/nar/gkg293;
RA Mannhaupt G., Montrone C., Haase D., Mewes H.-W., Aign V., Hoheisel J.D.,
RA Fartmann B., Nyakatura G., Kempken F., Maier J., Schulte U.;
RT "What's in the genome of a filamentous fungus? Analysis of the Neurospora
RT genome sequence.";
RL Nucleic Acids Res. 31:1944-1954(2003).
RN [3]
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 [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 OF COMPLEX III.
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 COMPOSITION OF THE RESPIRATORY COMPLEX III, AND IDENTIFICATION BY MASS
RP 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. {ECO:0000269|PubMed:3015618,
CC ECO:0000305|PubMed:1847681, ECO:0000305|PubMed:19239619}.
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}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P07257}; Matrix side
CC {ECO:0000250|UniProtKB:P07257}.
CC -!- DISRUPTION PHENOTYPE: Mutants display reduced growth, are female
CC sterile and lack active complex III. {ECO:0000269|PubMed:19239619}.
CC -!- SIMILARITY: Belongs to the peptidase M16 family. UQCRC2/QCR2 subfamily.
CC {ECO:0000305}.
CC -!- CAUTION: Does not seem to have a protease activity as it lack the zinc-
CC binding site. {ECO:0000305}.
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DR EMBL; Y08841; CAA70067.1; -; mRNA.
DR EMBL; AL669986; CAD21046.1; -; Genomic_DNA.
DR EMBL; CM002237; EAA26886.2; -; Genomic_DNA.
DR PIR; T47253; T47253.
DR RefSeq; XP_956122.2; XM_951029.3.
DR AlphaFoldDB; O60044; -.
DR SMR; O60044; -.
DR STRING; 5141.EFNCRP00000002612; -.
DR PRIDE; O60044; -.
DR EnsemblFungi; EAA26886; EAA26886; NCU03559.
DR GeneID; 3872277; -.
DR KEGG; ncr:NCU03559; -.
DR VEuPathDB; FungiDB:NCU03559; -.
DR HOGENOM; CLU_009902_0_1_1; -.
DR InParanoid; O60044; -.
DR OMA; WVGEFFT; -.
DR Proteomes; UP000001805; Chromosome 6, Linkage Group II.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0070469; C:respirasome; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR InterPro; IPR011249; Metalloenz_LuxS/M16.
DR InterPro; IPR011765; Pept_M16_N.
DR InterPro; IPR007863; Peptidase_M16_C.
DR Pfam; PF00675; Peptidase_M16; 1.
DR Pfam; PF05193; Peptidase_M16_C; 1.
DR SUPFAM; SSF63411; SSF63411; 2.
PE 1: Evidence at protein level;
KW Electron transport; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW Reference proteome; Respiratory chain; Transit peptide; Transport.
FT TRANSIT 1..35
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 36..454
FT /note="Cytochrome b-c1 complex subunit 2, mitochondrial"
FT /id="PRO_0000026798"
FT CONFLICT 8
FT /note="S -> L (in Ref. 1; CAA70067)"
FT /evidence="ECO:0000305"
FT CONFLICT 63
FT /note="V -> G (in Ref. 1; CAA70067)"
FT /evidence="ECO:0000305"
FT CONFLICT 75
FT /note="P -> A (in Ref. 1; CAA70067)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 454 AA; 46982 MW; 881C6D79ADC4D0C7 CRC64;
MISRSALSRG SQLALRRPAA AKTAQRGFAA AAASPAASYE PTTIAGVKVA SRDDSGPTTR
LAVVAKAGTR YEPLPGLTVG LEEFAFKNTN KRTALRITRE SELLGGQLQA YHTREAVVLQ
ASFLREDLPY FTELLAEVIS ETKYTTHEFH ELVENCIHEK QAKLDSAAIA LDAAHNVAFH
SGLGSPLYPT VDTPTSSYLN ENSVAAFANL AYNKANIAVV ADGASQAGLE KWVEPFFKGV
PATSSGNLNT AASKYFGGEQ RVAKNGKNAI VIAFPGASLG VPHPETSVLV GLLGGVSNIK
WSPGFSLLAK ATAANPGAEA FAHNYAYSDA GLLAIQITGK GAAVGKVAVE AVKGLKAIAA
GGVSKEDLTK AIAKAKFNLL SASEVSGTGL VHAGANLLAG GKPIQVAETL KALEGVTAEK
LQAAAKKLLE GKASVSAVGD LHVLPYAEDL GLKV
