QCR7_YEAST
ID QCR7_YEAST Reviewed; 127 AA.
AC P00128; D6VTF0;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 193.
DE RecName: Full=Cytochrome b-c1 complex subunit 7, mitochondrial;
DE AltName: Full=Complex III subunit 7;
DE AltName: Full=Complex III subunit VII;
DE AltName: Full=Ubiquinol-cytochrome c oxidoreductase subunit 7;
DE AltName: Full=Ubiquinol-cytochrome c reductase 14 kDa protein;
GN Name=QCR7; Synonyms=CRO1, UCR7; OrderedLocusNames=YDR529C;
GN ORFNames=D9719.32;
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=6319130; DOI=10.1111/j.1432-1033.1984.tb07896.x;
RA de Haan M., van Loon A.P.G.M., Kreike J., Vaessen R.T.M.J., Grivell L.A.;
RT "The biosynthesis of the ubiquinol-cytochrome c reductase complex in yeast.
RT DNA sequence analysis of the nuclear gene coding for the 14-kDa subunit.";
RL Eur. J. Biochem. 138:169-177(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
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 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 [5]
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 [6]
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 [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 3-127.
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 [9]
RP X-RAY CRYSTALLOGRAPHY (2.97 ANGSTROMS) OF 2-127.
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 [10]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 3-127.
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 [11]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 2-127.
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 [12]
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 [13]
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).
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:30598554}; Peripheral
CC membrane protein {ECO:0000269|PubMed:18390544,
CC ECO:0000269|PubMed:30598554}; Matrix side {ECO:0000269|PubMed:18390544,
CC ECO:0000269|PubMed:30598554}.
CC -!- MISCELLANEOUS: Present with 10100 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the UQCRB/QCR7 family. {ECO:0000305}.
CC -!- CAUTION: Was originally thought to be the ubiquinone-binding protein
CC (QP-C). {ECO:0000305}.
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DR EMBL; X00256; CAA25064.1; -; Genomic_DNA.
DR EMBL; U33057; AAB64968.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12360.1; -; Genomic_DNA.
DR PIR; S69584; RDBYUN.
DR RefSeq; NP_010818.1; NM_001180837.1.
DR PDB; 1EZV; X-ray; 2.30 A; F=3-127.
DR PDB; 1KB9; X-ray; 2.30 A; G=3-127.
DR PDB; 1KYO; X-ray; 2.97 A; G/R=2-127.
DR PDB; 1P84; X-ray; 2.50 A; G=3-127.
DR PDB; 2IBZ; X-ray; 2.30 A; F=1-127.
DR PDB; 3CX5; X-ray; 1.90 A; G/R=2-127.
DR PDB; 3CXH; X-ray; 2.50 A; G/R=2-127.
DR PDB; 4PD4; X-ray; 3.04 A; G=2-127.
DR PDB; 6GIQ; EM; 3.23 A; G/R=1-127.
DR PDB; 6HU9; EM; 3.35 A; G/R=1-127.
DR PDB; 6T0B; EM; 2.80 A; G/R=1-127.
DR PDB; 6T15; EM; 3.29 A; G/R=1-127.
DR PDB; 6YMX; EM; 3.17 A; G/R=2-127.
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 PDBsum; 6YMX; -.
DR AlphaFoldDB; P00128; -.
DR SMR; P00128; -.
DR BioGRID; 32578; 145.
DR ComplexPortal; CPX-567; Mitochondrial respiratory chain complex III.
DR DIP; DIP-2061N; -.
DR IntAct; P00128; 8.
DR STRING; 4932.YDR529C; -.
DR MaxQB; P00128; -.
DR PaxDb; P00128; -.
DR PRIDE; P00128; -.
DR EnsemblFungi; YDR529C_mRNA; YDR529C; YDR529C.
DR GeneID; 852142; -.
DR KEGG; sce:YDR529C; -.
DR SGD; S000002937; QCR7.
DR VEuPathDB; FungiDB:YDR529C; -.
DR eggNOG; KOG3440; Eukaryota.
DR GeneTree; ENSGT00390000012916; -.
DR HOGENOM; CLU_115154_1_0_1; -.
DR InParanoid; P00128; -.
DR OMA; APYIMKR; -.
DR BioCyc; MetaCyc:YDR529C-MON; -.
DR BioCyc; YEAST:YDR529C-MON; -.
DR Reactome; R-SCE-611105; Respiratory electron transport.
DR EvolutionaryTrace; P00128; -.
DR PRO; PR:P00128; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; P00128; protein.
DR GO; GO:0099617; C:matrix side of mitochondrial inner membrane; IDA:UniProtKB.
DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:ComplexPortal.
DR GO; GO:0005750; C:mitochondrial respiratory chain complex III; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA: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:0034551; P:mitochondrial respiratory chain complex III assembly; IMP:SGD.
DR GO; GO:1902600; P:proton transmembrane transport; IEA:GOC.
DR Gene3D; 1.10.1090.10; -; 1.
DR InterPro; IPR003197; QCR7.
DR InterPro; IPR036544; QCR7_sf.
DR PANTHER; PTHR12022; PTHR12022; 1.
DR Pfam; PF02271; UCR_14kD; 1.
DR PIRSF; PIRSF000022; Bc1_14K; 1.
DR SUPFAM; SSF81524; SSF81524; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Electron transport; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Reference proteome; Respiratory chain;
KW Transport.
FT CHAIN 1..127
FT /note="Cytochrome b-c1 complex subunit 7, mitochondrial"
FT /id="PRO_0000193539"
FT CONFLICT 92
FT /note="E -> Q (in Ref. 1; CAA25064)"
FT /evidence="ECO:0000305"
FT HELIX 5..17
FT /evidence="ECO:0007829|PDB:3CX5"
FT HELIX 19..36
FT /evidence="ECO:0007829|PDB:3CX5"
FT HELIX 38..41
FT /evidence="ECO:0007829|PDB:3CX5"
FT HELIX 45..48
FT /evidence="ECO:0007829|PDB:3CX5"
FT HELIX 54..62
FT /evidence="ECO:0007829|PDB:3CX5"
FT HELIX 65..83
FT /evidence="ECO:0007829|PDB:3CX5"
FT HELIX 90..92
FT /evidence="ECO:0007829|PDB:3CX5"
FT HELIX 96..98
FT /evidence="ECO:0007829|PDB:3CX5"
FT HELIX 104..121
FT /evidence="ECO:0007829|PDB:3CX5"
FT STRAND 123..125
FT /evidence="ECO:0007829|PDB:6T15"
SQ SEQUENCE 127 AA; 14565 MW; 1F1BA3DB6C4067B4 CRC64;
MPQSFTSIAR IGDYILKSPV LSKLCVPVAN QFINLAGYKK LGLKFDDLIA EENPIMQTAL
RRLPEDESYA RAYRIIRAHQ TELTHHLLPR NEWIKAQEDV PYLLPYILEA EAAAKEKDEL
DNIEVSK
