QCR9_YEAST
ID QCR9_YEAST Reviewed; 66 AA.
AC P22289; D6VUW6;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 190.
DE RecName: Full=Cytochrome b-c1 complex subunit 9, mitochondrial;
DE AltName: Full=Complex III subunit 9;
DE AltName: Full=Complex III subunit X;
DE AltName: Full=Cytochrome c1 non-heme 7.3 kDa protein;
DE AltName: Full=Ubiquinol-cytochrome c oxidoreductase subunit 9;
DE AltName: Full=Ubiquinol-cytochrome c reductase 7.3 kDa protein;
GN Name=QCR9; Synonyms=UCR9; OrderedLocusNames=YGR183C;
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], AND PROTEIN SEQUENCE OF 2-10.
RC STRAIN=ATCC 64665 / S288c / DC5;
RX PubMed=2174427; DOI=10.1016/s0021-9258(17)45288-4;
RA Phillips J.D., Schmitt M.E., Brown T.A., Beckmann J.D., Trumpower B.L.;
RT "Isolation and characterization of QCR9, a nuclear gene encoding the 7.3-
RT kDa subunit 9 of the Saccharomyces cerevisiae ubiquinol-cytochrome c
RT oxidoreductase complex. An intron-containing gene with a conserved sequence
RT occurring in the intron of COX4.";
RL J. Biol. Chem. 265:20813-20821(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9133739;
RX DOI=10.1002/(sici)1097-0061(19970330)13:4<357::aid-yea77>3.0.co;2-j;
RA Arroyo J., Garcia-Gonzalez M., Garcia-Saez M.I., Sanchez-Perez M.,
RA Nombela C.;
RT "DNA sequence analysis of a 23,002 bp DNA fragment of the right arm of
RT Saccharomyces cerevisiae chromosome VII.";
RL Yeast 13:357-363(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(1997).
RN [4]
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 [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 X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
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).
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 (1.90 ANGSTROMS).
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 [11]
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 [12]
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). Interacts with the
CC transmembrane segment of RIP1 (PubMed:30598556).
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}; Single-pass
CC membrane protein {ECO:0000269|PubMed:18390544,
CC ECO:0000269|PubMed:30598554}.
CC -!- MISCELLANEOUS: Present with 4550 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the UQCR10/QCR9 family. {ECO:0000305}.
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DR EMBL; M59797; AAA63575.1; -; Genomic_DNA.
DR EMBL; Z72968; CAA97209.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08277.1; -; Genomic_DNA.
DR PIR; A38325; A38325.
DR RefSeq; NP_011699.1; NM_001181312.1.
DR PDB; 1EZV; X-ray; 2.30 A; I=4-58.
DR PDB; 1KB9; X-ray; 2.30 A; I=4-58.
DR PDB; 1KYO; X-ray; 2.97 A; I/T=2-58.
DR PDB; 1P84; X-ray; 2.50 A; I=4-58.
DR PDB; 2IBZ; X-ray; 2.30 A; I=1-66.
DR PDB; 3CX5; X-ray; 1.90 A; I/T=2-66.
DR PDB; 3CXH; X-ray; 2.50 A; I/T=2-66.
DR PDB; 4PD4; X-ray; 3.04 A; I=2-58.
DR PDB; 6GIQ; EM; 3.23 A; I/T=1-66.
DR PDB; 6HU9; EM; 3.35 A; I/T=1-66.
DR PDB; 6T0B; EM; 2.80 A; I/T=1-66.
DR PDB; 6T15; EM; 3.29 A; I/T=1-66.
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; P22289; -.
DR SMR; P22289; -.
DR BioGRID; 33435; 318.
DR ComplexPortal; CPX-567; Mitochondrial respiratory chain complex III.
DR IntAct; P22289; 6.
DR MINT; P22289; -.
DR STRING; 4932.YGR183C; -.
DR MaxQB; P22289; -.
DR PaxDb; P22289; -.
DR PRIDE; P22289; -.
DR TopDownProteomics; P22289; -.
DR EnsemblFungi; YGR183C_mRNA; YGR183C; YGR183C.
DR GeneID; 853095; -.
DR KEGG; sce:YGR183C; -.
DR SGD; S000003415; QCR9.
DR VEuPathDB; FungiDB:YGR183C; -.
DR eggNOG; KOG3494; Eukaryota.
DR HOGENOM; CLU_171977_1_0_1; -.
DR InParanoid; P22289; -.
DR OMA; ANAGMQW; -.
DR BioCyc; MetaCyc:YGR183C-MON; -.
DR BioCyc; YEAST:YGR183C-MON; -.
DR Reactome; R-SCE-611105; Respiratory electron transport.
DR EvolutionaryTrace; P22289; -.
DR PRO; PR:P22289; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P22289; protein.
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; 1.20.5.260; -; 1.
DR InterPro; IPR008027; QCR9.
DR InterPro; IPR036656; QCR9_sf.
DR PANTHER; PTHR12980; PTHR12980; 1.
DR Pfam; PF05365; UCR_UQCRX_QCR9; 1.
DR SUPFAM; SSF81514; SSF81514; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Electron transport; Membrane;
KW Mitochondrion; Mitochondrion inner membrane; Reference proteome;
KW Respiratory chain; Transmembrane; Transmembrane helix; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:2174427"
FT CHAIN 2..66
FT /note="Cytochrome b-c1 complex subunit 9, mitochondrial"
FT /id="PRO_0000193558"
FT TOPO_DOM 2..17
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000269|PubMed:18390544,
FT ECO:0000269|PubMed:30598554"
FT TRANSMEM 18..43
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:18390544,
FT ECO:0000269|PubMed:30598554"
FT TOPO_DOM 44..66
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000269|PubMed:18390544,
FT ECO:0000269|PubMed:30598554"
FT HELIX 4..11
FT /evidence="ECO:0007829|PDB:3CX5"
FT HELIX 18..43
FT /evidence="ECO:0007829|PDB:3CX5"
FT TURN 44..47
FT /evidence="ECO:0007829|PDB:3CX5"
FT HELIX 49..55
FT /evidence="ECO:0007829|PDB:3CX5"
SQ SEQUENCE 66 AA; 7476 MW; 120106C00F3CCED0 CRC64;
MSFSSLYKTF FKRNAVFVGT IFAGAFVFQT VFDTAITSWY ENHNKGKLWK DVKARIAAGD
GDDDDE
