QCR6_YEAST
ID QCR6_YEAST Reviewed; 147 AA.
AC P00127; D6VTR6;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 2.
DT 03-AUG-2022, entry version 195.
DE RecName: Full=Cytochrome b-c1 complex subunit 6, mitochondrial;
DE AltName: Full=Complex III subunit 6;
DE AltName: Full=Complex III subunit VI;
DE AltName: Full=Cytochrome c1 non-heme 17 kDa protein;
DE AltName: Full=Mitochondrial hinge protein;
DE AltName: Full=Ubiquinol-cytochrome c oxidoreductase subunit 6;
DE AltName: Full=Ubiquinol-cytochrome c reductase 17 kDa protein;
GN Name=QCR6; Synonyms=UCR6; OrderedLocusNames=YFR033C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 28383 / FL100 / VTT C-80102;
RX PubMed=6329732;
RA van Loon A.P.G.M., de Groot R.J., de Haan M., Dekker A., Grivell L.A.;
RT "The DNA sequence of the nuclear gene coding for the 17-kd subunit VI of
RT the yeast ubiquinol-cytochrome c reductase: a protein with an extremely
RT high content of acidic amino acids.";
RL EMBO J. 3:1039-1043(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7670463; DOI=10.1038/ng0795-261;
RA Murakami Y., Naitou M., Hagiwara H., Shibata T., Ozawa M., Sasanuma S.,
RA Sasanuma M., Tsuchiya Y., Soeda E., Yokoyama K., Yamazaki M., Tashiro H.,
RA Eki T.;
RT "Analysis of the nucleotide sequence of chromosome VI from Saccharomyces
RT cerevisiae.";
RL Nat. Genet. 10:261-268(1995).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204511 / S288c / AB972;
RX PubMed=8686381;
RX DOI=10.1002/(sici)1097-0061(199602)12:2<177::aid-yea896>3.0.co;2-a;
RA Eki T., Naitou M., Hagiwara H., Abe M., Ozawa M., Sasanuma S., Sasanuma M.,
RA Tsuchiya Y., Shibata T., Watanabe K., Ono A., Yamazaki M., Tashiro H.,
RA Hanaoka F., Murakami Y.;
RT "Fifteen open reading frames in a 30.8 kb region of the right arm of
RT chromosome VI from Saccharomyces cerevisiae.";
RL Yeast 12:177-190(1996).
RN [5]
RP FORMATION OF CYTOCHROME BC1-CYTOCHROME C OXIDASE SUPERCOMPLEX.
RX PubMed=10775262; DOI=10.1093/emboj/19.8.1777;
RA Schaegger H., Pfeiffer K.;
RT "Supercomplexes in the respiratory chains of yeast and mammalian
RT mitochondria.";
RL EMBO J. 19:1777-1783(2000).
RN [6]
RP FORMATION OF CYTOCHROME BC1-CYTOCHROME C OXIDASE SUPERCOMPLEX.
RX PubMed=10764779; DOI=10.1074/jbc.m001901200;
RA Cruciat C.M., Brunner S., Baumann F., Neupert W., Stuart R.A.;
RT "The cytochrome bc1 and cytochrome c oxidase complexes associate to form a
RT single supracomplex in yeast mitochondria.";
RL J. Biol. Chem. 275:18093-18098(2000).
RN [7]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RX PubMed=22984289; DOI=10.1074/mcp.m112.021105;
RA Voegtle F.N., Burkhart J.M., Rao S., Gerbeth C., Hinrichs J.,
RA Martinou J.C., Chacinska A., Sickmann A., Zahedi R.P., Meisinger C.;
RT "Intermembrane space proteome of yeast mitochondria.";
RL Mol. Cell. Proteomics 11:1840-1852(2012).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 74-147, AND DISULFIDE BOND.
RX PubMed=10873857; DOI=10.1016/s0969-2126(00)00152-0;
RA Hunte C., Koepke J., Lange C., Rossmanith T., Michel H.;
RT "Structure at 2.3 A resolution of the cytochrome bc1 complex from the yeast
RT Saccharomyces cerevisiae co-crystallized with an antibody Fv fragment.";
RL Structure 8:669-684(2000).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 74-147, AND DISULFIDE BOND.
RX PubMed=11726495; DOI=10.1093/emboj/20.23.6591;
RA Lange C., Nett J.H., Trumpower B.L., Hunte C.;
RT "Specific roles of protein-phospholipid interactions in the yeast
RT cytochrome bc1 complex structure.";
RL EMBO J. 20:6591-6600(2001).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.97 ANGSTROMS) OF 75-147, AND DISULFIDE BOND.
RX PubMed=11880631; DOI=10.1073/pnas.052704699;
RA Lange C., Hunte C.;
RT "Crystal structure of the yeast cytochrome bc1 complex with its bound
RT substrate cytochrome c.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:2800-2805(2002).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 74-147, AND DISULFIDE BOND.
RX PubMed=12782631; DOI=10.1074/jbc.m302195200;
RA Palsdottir H., Lojero C.G., Trumpower B.L., Hunte C.;
RT "Structure of the yeast cytochrome bc1 complex with a hydroxyquinone anion
RT Qo site inhibitor bound.";
RL J. Biol. Chem. 278:31303-31311(2003).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 74-147, AND DISULFIDE BOND.
RX PubMed=17337272; DOI=10.1016/j.jmb.2007.02.013;
RA Lancaster C.R., Hunte C., Kelley J., Trumpower B.L., Ditchfield R.;
RT "A comparison of stigmatellin conformations, free and bound to the
RT photosynthetic reaction center and the cytochrome bc1 complex.";
RL J. Mol. Biol. 368:197-208(2007).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 2-147, AND DISULFIDE BOND.
RX PubMed=18390544; DOI=10.1074/jbc.m710126200;
RA Solmaz S.R., Hunte C.;
RT "Structure of complex III with bound cytochrome c in reduced state and
RT definition of a minimal core interface for electron transfer.";
RL J. Biol. Chem. 283:17542-17549(2008).
RN [15]
RP STRUCTURE BY ELECTRON MICROSCOPY (3.23 ANGSTROMS).
RX PubMed=30598556; DOI=10.1038/s41594-018-0169-7;
RA Rathore S., Berndtsson J., Marin-Buera L., Conrad J., Carroni M.,
RA Brzezinski P., Ott M.;
RT "Cryo-EM structure of the yeast respiratory supercomplex.";
RL Nat. Struct. Mol. Biol. 26:50-57(2019).
RN [16]
RP STRUCTURE BY ELECTRON MICROSCOPY (3.35 ANGSTROMS).
RX PubMed=30598554; DOI=10.1038/s41594-018-0172-z;
RA Hartley A.M., Lukoyanova N., Zhang Y., Cabrera-Orefice A., Arnold S.,
RA Meunier B., Pinotsis N., Marechal A.;
RT "Structure of yeast cytochrome c oxidase in a supercomplex with cytochrome
RT bc1.";
RL Nat. Struct. Mol. Biol. 26:78-83(2019).
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:0000305|PubMed:11880631}.
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 (CYT1) and Rieske protein
CC (RIP1), 2 core protein subunits COR1 and QCR2, and 5 low-molecular
CC weight protein subunits QCR6, QCR7, QCR8, QCR9 and QCR10
CC (PubMed:10873857, PubMed:11880631, PubMed:18390544, PubMed:30598554).
CC The complex exists as an obligatory dimer and forms supercomplexes
CC (SCs) in the inner mitochondrial membrane with a monomer or a dimer of
CC cytochrome c oxidase (complex IV, CIV), resulting in 2 different
CC assemblies (supercomplexes III(2)IV and III(2)IV(2)) (PubMed:10775262,
CC PubMed:10764779, PubMed:30598556, PubMed:30598554). QCR6 interacts with
CC COX5A at the CIII-CIV interface (PubMed:30598554).
CC {ECO:0000269|PubMed:10764779, ECO:0000269|PubMed:10775262,
CC ECO:0000269|PubMed:10873857, ECO:0000269|PubMed:11880631,
CC ECO:0000269|PubMed:18390544, ECO:0000269|PubMed:30598554,
CC ECO:0000269|PubMed:30598556}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:18390544, ECO:0000269|PubMed:22984289,
CC ECO:0000269|PubMed:30598554}; Peripheral membrane protein
CC {ECO:0000269|PubMed:18390544, ECO:0000269|PubMed:30598554};
CC Intermembrane side {ECO:0000269|PubMed:18390544,
CC ECO:0000269|PubMed:30598554}.
CC -!- MISCELLANEOUS: Present with 4490 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the UQCRH/QCR6 family. {ECO:0000305}.
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DR EMBL; X00551; CAA25220.1; -; Genomic_DNA.
DR EMBL; D50617; BAA09272.1; -; Genomic_DNA.
DR EMBL; BK006940; DAA12476.1; -; Genomic_DNA.
DR PIR; S56288; RDBYUC.
DR RefSeq; NP_116691.3; NM_001179998.3.
DR PDB; 1EZV; X-ray; 2.30 A; H=74-147.
DR PDB; 1KB9; X-ray; 2.30 A; F=74-147.
DR PDB; 1KYO; X-ray; 2.97 A; F/Q=75-147.
DR PDB; 1P84; X-ray; 2.50 A; F=74-147.
DR PDB; 2IBZ; X-ray; 2.30 A; H=74-147.
DR PDB; 3CX5; X-ray; 1.90 A; F/Q=2-147.
DR PDB; 3CXH; X-ray; 2.50 A; F/Q=2-147.
DR PDB; 4PD4; X-ray; 3.04 A; F=74-147.
DR PDB; 6GIQ; EM; 3.23 A; F/Q=1-147.
DR PDB; 6HU9; EM; 3.35 A; F/Q=1-147.
DR PDB; 6T0B; EM; 2.80 A; F/Q=1-147.
DR PDB; 6T15; EM; 3.29 A; F/Q=1-147.
DR PDBsum; 1EZV; -.
DR PDBsum; 1KB9; -.
DR PDBsum; 1KYO; -.
DR PDBsum; 1P84; -.
DR PDBsum; 2IBZ; -.
DR PDBsum; 3CX5; -.
DR PDBsum; 3CXH; -.
DR PDBsum; 4PD4; -.
DR PDBsum; 6GIQ; -.
DR PDBsum; 6HU9; -.
DR PDBsum; 6T0B; -.
DR PDBsum; 6T15; -.
DR AlphaFoldDB; P00127; -.
DR SMR; P00127; -.
DR BioGRID; 31190; 112.
DR ComplexPortal; CPX-567; Mitochondrial respiratory chain complex III.
DR DIP; DIP-1621N; -.
DR IntAct; P00127; 5.
DR MINT; P00127; -.
DR STRING; 4932.YFR033C; -.
DR CarbonylDB; P00127; -.
DR MaxQB; P00127; -.
DR PaxDb; P00127; -.
DR PRIDE; P00127; -.
DR EnsemblFungi; YFR033C_mRNA; YFR033C; YFR033C.
DR GeneID; 850593; -.
DR KEGG; sce:YFR033C; -.
DR SGD; S000001929; QCR6.
DR VEuPathDB; FungiDB:YFR033C; -.
DR eggNOG; KOG4763; Eukaryota.
DR GeneTree; ENSGT00390000003860; -.
DR HOGENOM; CLU_115913_0_1_1; -.
DR InParanoid; P00127; -.
DR OMA; CKNSPQC; -.
DR BioCyc; MetaCyc:YFR033C-MON; -.
DR BioCyc; YEAST:YFR033C-MON; -.
DR Reactome; R-SCE-611105; Respiratory electron transport.
DR EvolutionaryTrace; P00127; -.
DR PRO; PR:P00127; -.
DR Proteomes; UP000002311; Chromosome VI.
DR RNAct; P00127; protein.
DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:ComplexPortal.
DR GO; GO:0005758; C:mitochondrial intermembrane space; IDA:SGD.
DR GO; GO:0005750; C:mitochondrial respiratory chain complex III; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0034399; C:nuclear periphery; IDA:SGD.
DR GO; GO:0009060; P:aerobic respiration; IMP:SGD.
DR GO; GO:0045333; P:cellular respiration; IDA:ComplexPortal.
DR GO; GO:0006122; P:mitochondrial electron transport, ubiquinol to cytochrome c; IDA:ComplexPortal.
DR GO; GO:1902600; P:proton transmembrane transport; IEA:GOC.
DR DisProt; DP00853; -.
DR Gene3D; 1.10.287.20; -; 1.
DR InterPro; IPR023184; Ubol_cytC_Rdtase_hinge_dom.
DR InterPro; IPR036811; Ubol_cytC_Rdtase_hinge_dom_sf.
DR Pfam; PF02320; UCR_hinge; 1.
DR SUPFAM; SSF81531; SSF81531; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Disulfide bond; Electron transport; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Reference proteome; Respiratory chain;
KW Transport.
FT CHAIN 1..147
FT /note="Cytochrome b-c1 complex subunit 6, mitochondrial"
FT /id="PRO_0000193542"
FT REGION 25..89
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 26..40
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 41..77
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 101..123
FT /evidence="ECO:0000269|PubMed:10873857,
FT ECO:0000269|PubMed:11726495, ECO:0000269|PubMed:11880631,
FT ECO:0000269|PubMed:12782631, ECO:0000269|PubMed:17337272,
FT ECO:0000269|PubMed:18390544"
FT CONFLICT 2
FT /note="G -> D (in Ref. 1; CAA25220)"
FT /evidence="ECO:0000305"
FT HELIX 77..86
FT /evidence="ECO:0007829|PDB:3CX5"
FT HELIX 89..110
FT /evidence="ECO:0007829|PDB:3CX5"
FT STRAND 111..113
FT /evidence="ECO:0007829|PDB:6T0B"
FT HELIX 114..116
FT /evidence="ECO:0007829|PDB:3CX5"
FT STRAND 117..119
FT /evidence="ECO:0007829|PDB:6T0B"
FT HELIX 124..142
FT /evidence="ECO:0007829|PDB:3CX5"
FT HELIX 143..145
FT /evidence="ECO:0007829|PDB:3CX5"
SQ SEQUENCE 147 AA; 17257 MW; 1488B9C0EB57BE8F CRC64;
MGMLELVGEY WEQLKITVVP VVAAAEDDDN EQHEEKAAEG EEKEEENGDE DEDEDEDEDD
DDDDDEDEEE EEEVTDQLED LREHFKNTEE GKALVHHYEE CAERVKIQQQ QPGYADLEHK
EDCVEEFFHL QHYLDTATAP RLFDKLK
