QCR8_KLULA
ID QCR8_KLULA Reviewed; 94 AA.
AC P49346;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 25-MAY-2022, entry version 115.
DE RecName: Full=Cytochrome b-c1 complex subunit 8;
DE AltName: Full=Complex III subunit 8;
DE AltName: Full=Complex III subunit VII;
DE AltName: Full=Ubiquinol-cytochrome c reductase complex 11 kDa protein;
DE AltName: Full=Ubiquinol-cytochrome c reductase complex ubiquinone-binding protein QP-C;
GN Name=QCR8; OrderedLocusNames=KLLA0A06754g;
OS Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=284590;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX PubMed=7948032; DOI=10.1016/0167-4781(94)90234-8;
RA Mulder W., Scholten I.H.J.M., Nagelkerken B., Grivell L.A.;
RT "Isolation and characterisation of the linked genes, FPS1 and QCR8, coding
RT for farnesyl-diphosphate synthase and the 11 kDa subunit VIII of the
RT mitochondrial bc1-complex in the yeast Kluyveromyces lactis.";
RL Biochim. Biophys. Acta 1219:713-718(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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:0000250|UniProtKB:P08525}.
CC -!- SUBUNIT: Component of the ubiquinol-cytochrome c oxidoreductase
CC (cytochrome b-c1 complex, complex III, CIII), a multisubunit enzyme
CC composed of 3 respiratory subunits cytochrome b, cytochrome c1 and
CC Rieske protein, 2 core protein subunits, and additional low-molecular
CC weight protein subunits. The complex exists as an obligatory dimer and
CC forms supercomplexes (SCs) in the inner mitochondrial membrane with
CC cytochrome c oxidase (complex IV, CIV). {ECO:0000250|UniProtKB:P08525}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:P08525}; Single-pass membrane protein
CC {ECO:0000250|UniProtKB:P08525}.
CC -!- SIMILARITY: Belongs to the UQCRQ/QCR8 family. {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; X76026; CAA53615.1; -; Genomic_DNA.
DR EMBL; CR382121; CAH02889.1; -; Genomic_DNA.
DR PIR; S50215; S50215.
DR RefSeq; XP_451301.1; XM_451301.1.
DR AlphaFoldDB; P49346; -.
DR SMR; P49346; -.
DR STRING; 28985.XP_451301.1; -.
DR EnsemblFungi; CAH02889; CAH02889; KLLA0_A06754g.
DR GeneID; 2896709; -.
DR KEGG; kla:KLLA0_A06754g; -.
DR eggNOG; KOG4116; Eukaryota.
DR HOGENOM; CLU_156007_0_1_1; -.
DR InParanoid; P49346; -.
DR OMA; KTTWHIG; -.
DR Proteomes; UP000000598; Chromosome A.
DR GO; GO:0005750; C:mitochondrial respiratory chain complex III; IEA:EnsemblFungi.
DR GO; GO:0006122; P:mitochondrial electron transport, ubiquinol to cytochrome c; IEA:EnsemblFungi.
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 3: Inferred from homology;
KW Electron transport; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW Reference proteome; Respiratory chain; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..94
FT /note="Cytochrome b-c1 complex subunit 8"
FT /id="PRO_0000193549"
FT TOPO_DOM 1..49
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000250|UniProtKB:P08525"
FT TRANSMEM 50..80
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P08525"
FT TOPO_DOM 81..94
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000250|UniProtKB:P08525"
SQ SEQUENCE 94 AA; 10821 MW; 1072F75FA85148CB CRC64;
MGGPHAKAYM GWWGSIGSPA QKGITTYTVS PYAQKPLNNI FHNAVFNTFR RVKSQILYMA
LPAALYWAWW VNCRDYNAYL YTKAGREELE RVNV