ID   QCR10_NEUCR             Reviewed;          91 AA.
AC   V5IP95;
DT   26-FEB-2020, integrated into UniProtKB/Swiss-Prot.
DT   22-JAN-2014, sequence version 1.
DT   25-MAY-2022, entry version 32.
DE   RecName: Full=Cytochrome b-c1 complex subunit 10, mitochondrial {ECO:0000305};
DE   AltName: Full=Complex III subunit 10;
DE   AltName: Full=Ubiquinol-cytochrome c oxidoreductase subunit 10;
GN   ORFNames=NCU16844;
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   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   [3]
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   [4]
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   [5]
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 (Probable). The complex exists as an obligatory dimer
CC       and forms supercomplexes (SCs) in the inner mitochondrial membrane with
CC       NADH-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:19239619,
CC       ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000250|UniProtKB:P37299}; Single-pass membrane protein
CC       {ECO:0000250|UniProtKB:P37299}.
CC   -!- SIMILARITY: Belongs to the UQCR11/QCR10 family. {ECO:0000305}.
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DR   EMBL; CM002239; ESA42999.1; -; Genomic_DNA.
DR   RefSeq; XP_011394420.1; XM_011396118.1.
DR   AlphaFoldDB; V5IP95; -.
DR   STRING; 5141.EFNCRP00000007133; -.
DR   EnsemblFungi; ESA42999; ESA42999; NCU16844.
DR   GeneID; 23569684; -.
DR   KEGG; ncr:NCU16844; -.
DR   VEuPathDB; FungiDB:NCU16844; -.
DR   Proteomes; UP000001805; Chromosome 4, Linkage Group IV.
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   InterPro; IPR019182; Cytochrome_b-c1_su10_fun.
DR   PANTHER; PTHR28254; PTHR28254; 1.
DR   Pfam; PF09796; QCR10; 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..91
FT                   /note="Cytochrome b-c1 complex subunit 10, mitochondrial"
FT                   /id="PRO_0000449194"
FT   TOPO_DOM        1..34
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000250|UniProtKB:P37299"
FT   TRANSMEM        35..58
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P37299"
FT   TOPO_DOM        59..91
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000250|UniProtKB:P37299"
SQ   SEQUENCE   91 AA;  10338 MW;  8B05CCB379AFB434 CRC64;
     MFATSILRSA YPAYKSPYGP KYQYQPHIDG ITPKQLVRIL PTAAAWTGVA LFAVVYYASG
     IPRLRRDVLQ RIPYLGERYF VNEIPASDNP F