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QCR8_NEUCR
ID   QCR8_NEUCR              Reviewed;         107 AA.
AC   P48503; Q7S7F4;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   25-MAY-2022, entry version 135.
DE   RecName: Full=Cytochrome b-c1 complex subunit 8;
DE   AltName: Full=Complex III subunit 8;
DE   AltName: Full=Complex III subunit VIII {ECO:0000303|PubMed:6302289};
DE   AltName: Full=Ubiquinol-cytochrome c reductase complex 11 kDa protein;
DE   AltName: Full=Ubiquinol-cytochrome c reductase complex ubiquinone-binding protein QP-C;
DE   Flags: Precursor;
GN   Name=qcr8; ORFNames=20H10.240, NCU08947;
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], AND PROTEIN SEQUENCE OF 9-26.
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=9003361; DOI=10.1042/bj3200769;
RA   Lobo-Hajdu G., Braun H.P., Romp N., Grivell L.A., Berden J.A.,
RA   Schmitz U.K.;
RT   "Subunit VII of ubiquinol:cytochrome-c oxidoreductase from Neurospora
RT   crassa is functional in yeast and has an N-terminal extension that is not
RT   essential for mitochondrial targeting.";
RL   Biochem. J. 320:769-775(1996).
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, 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: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:P08525}.
CC   -!- SIMILARITY: Belongs to the UQCRQ/QCR8 family. {ECO:0000305}.
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DR   EMBL; U20790; AAC49654.1; -; mRNA.
DR   EMBL; BX294024; CAD71007.1; -; Genomic_DNA.
DR   EMBL; CM002240; EAA31578.1; -; Genomic_DNA.
DR   PIR; T46746; T46746.
DR   RefSeq; XP_960814.1; XM_955721.3.
DR   AlphaFoldDB; P48503; -.
DR   SMR; P48503; -.
DR   STRING; 5141.EFNCRP00000008104; -.
DR   EnsemblFungi; EAA31578; EAA31578; NCU08947.
DR   GeneID; 3876952; -.
DR   KEGG; ncr:NCU08947; -.
DR   VEuPathDB; FungiDB:NCU08947; -.
DR   HOGENOM; CLU_156007_0_1_1; -.
DR   InParanoid; P48503; -.
DR   OMA; AAIFNTW; -.
DR   Proteomes; UP000001805; Chromosome 2, Linkage Group V.
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; 1.20.5.210; -; 1.
DR   InterPro; IPR004205; Cyt_bc1_su8.
DR   InterPro; IPR036642; Cyt_bc1_su8_sf.
DR   PANTHER; PTHR12119; PTHR12119; 1.
DR   Pfam; PF02939; UcrQ; 1.
DR   SUPFAM; SSF81508; SSF81508; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Electron transport; Membrane; Mitochondrion;
KW   Mitochondrion inner membrane; Reference proteome; Respiratory chain;
KW   Transmembrane; Transmembrane helix; Transport.
FT   PROPEP          1..8
FT                   /note="Plays a role in role in intramitochondrial sorting"
FT                   /evidence="ECO:0000269|PubMed:9003361"
FT                   /id="PRO_0000035994"
FT   CHAIN           9..107
FT                   /note="Cytochrome b-c1 complex subunit 8"
FT                   /id="PRO_0000035995"
FT   TOPO_DOM        1..62
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000250|UniProtKB:P08525"
FT   TRANSMEM        63..93
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P08525"
FT   TOPO_DOM        94..107
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000250|UniProtKB:P08525"
SQ   SEQUENCE   107 AA;  11776 MW;  2C496C14044B67A1 CRC64;
     MRPTQTMLGG GGGAPIGKHN HYLGGWGNFG GMKQRGIISY GISPNRQNPL AGTAHDAVFN
     TFRRVSSQFL YWAPSLVAGY YIMNWAIERN HYLNSKAGRA EFAGQEE
 
 
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