QCR9_NEUCR
ID QCR9_NEUCR Reviewed; 59 AA.
AC Q7SGT7;
DT 26-FEB-2020, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 2.
DT 25-MAY-2022, entry version 92.
DE RecName: Full=Cytochrome b-c1 complex subunit 9, mitochondrial;
DE AltName: Full=Complex III subunit 9;
DE AltName: Full=Complex III subunit IX {ECO:0000303|PubMed:6302289};
DE AltName: Full=Ubiquinol-cytochrome c oxidoreductase subunit 9;
DE AltName: Full=Ubiquinol-cytochrome c reductase complex 8 kDa protein;
GN Name=qcr9; ORFNames=NCU03233;
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 [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 [2]
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 [3]
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 [4]
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 [5]
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 [6]
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 [7]
RP SUBUNIT.
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 [8]
RP FUNCTION OF COMPLEX III, AND SUBUNIT.
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:6302289). The
CC complex exists as an obligatory dimer and forms supercomplexes (SCs) in
CC the inner mitochondrial membrane with NADH-ubiquinone oxidoreductase
CC (complex I, CI) and cytochrome c oxidase (complex IV, CIV), resulting
CC in different assemblies (supercomplexes SCI(1)III(2), SCIII(2)IV(1) and
CC SCIII(2)IV(2) as well as higher order I(x)III(y)IV(z) megacomplexes)
CC (PubMed:17873079, PubMed:19239619). {ECO:0000269|PubMed:17873079,
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:0000250|UniProtKB:P22289}; Single-pass membrane protein
CC {ECO:0000250|UniProtKB:P22289}.
CC -!- SIMILARITY: Belongs to the UQCR10/QCR9 family. {ECO:0000305}.
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DR EMBL; CM002236; EAA36097.2; -; Genomic_DNA.
DR RefSeq; XP_965333.2; XM_960240.3.
DR AlphaFoldDB; Q7SGT7; -.
DR SMR; Q7SGT7; -.
DR STRING; 5141.EFNCRP00000003023; -.
DR EnsemblFungi; EAA36097; EAA36097; NCU03233.
DR GeneID; 3881482; -.
DR KEGG; ncr:NCU03233; -.
DR VEuPathDB; FungiDB:NCU03233; -.
DR HOGENOM; CLU_171977_3_0_1; -.
DR InParanoid; Q7SGT7; -.
DR OMA; DIKHRYI; -.
DR Proteomes; UP000001805; Chromosome 1, Linkage Group I.
DR GO; GO:0005750; C:mitochondrial respiratory chain complex III; IBA:GO_Central.
DR GO; GO:0006122; P:mitochondrial electron transport, ubiquinol to cytochrome c; IBA:GO_Central.
DR Gene3D; 1.20.5.260; -; 1.
DR InterPro; IPR008027; QCR9.
DR InterPro; IPR036656; QCR9_sf.
DR PANTHER; PTHR12980; PTHR12980; 1.
DR Pfam; PF05365; UCR_UQCRX_QCR9; 1.
DR SUPFAM; SSF81514; SSF81514; 1.
PE 1: Evidence at protein level;
KW Electron transport; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW Reference proteome; Respiratory chain; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..59
FT /note="Cytochrome b-c1 complex subunit 9, mitochondrial"
FT /id="PRO_0000449193"
FT TOPO_DOM 1..15
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000250|UniProtKB:P22289"
FT TRANSMEM 16..41
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P22289"
FT TOPO_DOM 42..59
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000250|UniProtKB:P22289"
SQ SEQUENCE 59 AA; 6861 MW; C0A34A4F6A9F2D79 CRC64;
MSALYNLIFR NNTAFVGAVF AGAFAFELAY DNGMDKVWDK INKGRQWKDI RHKYVEAEE
