QCR2_YEAST
ID QCR2_YEAST Reviewed; 368 AA.
AC P07257; D6W4J1;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1988, sequence version 1.
DT 03-AUG-2022, entry version 216.
DE RecName: Full=Cytochrome b-c1 complex subunit 2, mitochondrial;
DE AltName: Full=Complex III subunit 2;
DE AltName: Full=Core protein II;
DE AltName: Full=Ubiquinol-cytochrome c oxidoreductase core protein 2;
DE Flags: Precursor;
GN Name=QCR2; Synonyms=COR2, UCR2; OrderedLocusNames=YPR191W;
GN ORFNames=P9677.6;
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 17-22.
RX PubMed=3028797; DOI=10.1111/j.1432-1033.1987.tb10741.x;
RA Oudshoorn P., van Steeg H., Swinkels B.W., Schoppink P., Grivell L.A.;
RT "Subunit II of yeast QH2:cytochrome-c oxidoreductase. Nucleotide sequence
RT of the gene and features of the protein.";
RL Eur. J. Biochem. 163:97-103(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(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 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
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 SUBCELLULAR LOCATION.
RX PubMed=11502169; DOI=10.1021/bi010277r;
RA Grandier-Vazeille X., Bathany K., Chaignepain S., Camougrand N., Manon S.,
RA Schmitter J.-M.;
RT "Yeast mitochondrial dehydrogenases are associated in a supramolecular
RT complex.";
RL Biochemistry 40:9758-9769(2001).
RN [8]
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-141, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 76625 / YPH499;
RX PubMed=17761666; DOI=10.1074/mcp.m700098-mcp200;
RA Reinders J., Wagner K., Zahedi R.P., Stojanovski D., Eyrich B.,
RA van der Laan M., Rehling P., Sickmann A., Pfanner N., Meisinger C.;
RT "Profiling phosphoproteins of yeast mitochondria reveals a role of
RT phosphorylation in assembly of the ATP synthase.";
RL Mol. Cell. Proteomics 6:1896-1906(2007).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-168, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [11]
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 [12]
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 [13]
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 [14]
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 [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).
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 -!- INTERACTION:
CC P07257; P07256: COR1; NbExp=3; IntAct=EBI-19929, EBI-19922;
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:11502169, ECO:0000269|PubMed:18390544,
CC ECO:0000269|PubMed:22984289, 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 35700 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the peptidase M16 family. UQCRC2/QCR2 subfamily.
CC {ECO:0000305}.
CC -!- CAUTION: Does not seem to have a protease activity as it lack the zinc-
CC binding site. {ECO:0000305}.
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DR EMBL; X05120; CAA28768.1; -; Genomic_DNA.
DR EMBL; U25841; AAB64620.1; -; Genomic_DNA.
DR EMBL; AY558068; AAS56394.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11607.1; -; Genomic_DNA.
DR PIR; A27535; A27535.
DR RefSeq; NP_015517.1; NM_001184288.1.
DR PDB; 1EZV; X-ray; 2.30 A; B=17-368.
DR PDB; 1KB9; X-ray; 2.30 A; B=17-368.
DR PDB; 1KYO; X-ray; 2.97 A; B/M=17-368.
DR PDB; 1P84; X-ray; 2.50 A; B=17-368.
DR PDB; 2IBZ; X-ray; 2.30 A; B=17-368.
DR PDB; 3CX5; X-ray; 1.90 A; B/M=17-368.
DR PDB; 3CXH; X-ray; 2.50 A; B/M=17-368.
DR PDB; 4PD4; X-ray; 3.04 A; B=17-368.
DR PDB; 6GIQ; EM; 3.23 A; B/M=1-368.
DR PDB; 6HU9; EM; 3.35 A; B/M=17-368.
DR PDB; 6T0B; EM; 2.80 A; B/M=17-368.
DR PDB; 6T15; EM; 3.29 A; B/M=17-368.
DR PDB; 6YMX; EM; 3.17 A; B/M=17-368.
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; P07257; -.
DR SMR; P07257; -.
DR BioGRID; 36363; 434.
DR ComplexPortal; CPX-567; Mitochondrial respiratory chain complex III.
DR DIP; DIP-3820N; -.
DR IntAct; P07257; 30.
DR MINT; P07257; -.
DR STRING; 4932.YPR191W; -.
DR iPTMnet; P07257; -.
DR MaxQB; P07257; -.
DR PaxDb; P07257; -.
DR PRIDE; P07257; -.
DR EnsemblFungi; YPR191W_mRNA; YPR191W; YPR191W.
DR GeneID; 856321; -.
DR KEGG; sce:YPR191W; -.
DR SGD; S000006395; QCR2.
DR VEuPathDB; FungiDB:YPR191W; -.
DR eggNOG; KOG2583; Eukaryota.
DR GeneTree; ENSGT00940000173495; -.
DR HOGENOM; CLU_009902_0_1_1; -.
DR InParanoid; P07257; -.
DR OMA; YKYQDAG; -.
DR BioCyc; MetaCyc:YPR191W-MON; -.
DR BioCyc; YEAST:YPR191W-MON; -.
DR EvolutionaryTrace; P07257; -.
DR PRO; PR:P07257; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; P07257; protein.
DR GO; GO:0030061; C:mitochondrial crista; IDA:SGD.
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; IDA:SGD.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
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:SGD.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR GO; GO:1902600; P:proton transmembrane transport; IEA:GOC.
DR InterPro; IPR011249; Metalloenz_LuxS/M16.
DR InterPro; IPR011765; Pept_M16_N.
DR InterPro; IPR001431; Pept_M16_Zn_BS.
DR Pfam; PF00675; Peptidase_M16; 1.
DR SUPFAM; SSF63411; SSF63411; 2.
DR PROSITE; PS00143; INSULINASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Electron transport; Membrane;
KW Mitochondrion; Mitochondrion inner membrane; Phosphoprotein;
KW Reference proteome; Respiratory chain; Transit peptide; Transport.
FT TRANSIT 1..16
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:3028797"
FT CHAIN 17..368
FT /note="Cytochrome b-c1 complex subunit 2, mitochondrial"
FT /id="PRO_0000026801"
FT MOD_RES 141
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17761666"
FT MOD_RES 168
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT STRAND 18..22
FT /evidence="ECO:0007829|PDB:3CX5"
FT STRAND 27..36
FT /evidence="ECO:0007829|PDB:3CX5"
FT HELIX 39..41
FT /evidence="ECO:0007829|PDB:3CX5"
FT HELIX 47..54
FT /evidence="ECO:0007829|PDB:3CX5"
FT STRAND 59..62
FT /evidence="ECO:0007829|PDB:3CX5"
FT HELIX 64..74
FT /evidence="ECO:0007829|PDB:3CX5"
FT STRAND 77..82
FT /evidence="ECO:0007829|PDB:3CX5"
FT STRAND 87..94
FT /evidence="ECO:0007829|PDB:3CX5"
FT HELIX 95..97
FT /evidence="ECO:0007829|PDB:3CX5"
FT HELIX 98..111
FT /evidence="ECO:0007829|PDB:3CX5"
FT HELIX 116..121
FT /evidence="ECO:0007829|PDB:3CX5"
FT HELIX 123..135
FT /evidence="ECO:0007829|PDB:3CX5"
FT HELIX 138..151
FT /evidence="ECO:0007829|PDB:3CX5"
FT TURN 152..156
FT /evidence="ECO:0007829|PDB:3CX5"
FT STRAND 163..165
FT /evidence="ECO:0007829|PDB:3CX5"
FT HELIX 169..179
FT /evidence="ECO:0007829|PDB:3CX5"
FT HELIX 182..184
FT /evidence="ECO:0007829|PDB:3CX5"
FT STRAND 185..192
FT /evidence="ECO:0007829|PDB:3CX5"
FT HELIX 194..203
FT /evidence="ECO:0007829|PDB:3CX5"
FT TURN 205..208
FT /evidence="ECO:0007829|PDB:3CX5"
FT STRAND 228..232
FT /evidence="ECO:0007829|PDB:3CX5"
FT STRAND 234..245
FT /evidence="ECO:0007829|PDB:3CX5"
FT TURN 247..249
FT /evidence="ECO:0007829|PDB:3CX5"
FT HELIX 250..261
FT /evidence="ECO:0007829|PDB:3CX5"
FT STRAND 262..265
FT /evidence="ECO:0007829|PDB:1P84"
FT HELIX 268..270
FT /evidence="ECO:0007829|PDB:3CX5"
FT STRAND 272..279
FT /evidence="ECO:0007829|PDB:3CX5"
FT STRAND 282..292
FT /evidence="ECO:0007829|PDB:3CX5"
FT HELIX 294..309
FT /evidence="ECO:0007829|PDB:3CX5"
FT STRAND 310..313
FT /evidence="ECO:0007829|PDB:6T15"
FT HELIX 315..317
FT /evidence="ECO:0007829|PDB:3CX5"
FT HELIX 318..328
FT /evidence="ECO:0007829|PDB:3CX5"
FT HELIX 329..331
FT /evidence="ECO:0007829|PDB:1KB9"
FT STRAND 332..334
FT /evidence="ECO:0007829|PDB:6T15"
FT HELIX 340..342
FT /evidence="ECO:0007829|PDB:3CX5"
FT STRAND 345..347
FT /evidence="ECO:0007829|PDB:6T15"
FT STRAND 352..358
FT /evidence="ECO:0007829|PDB:3CX5"
FT HELIX 359..361
FT /evidence="ECO:0007829|PDB:3CX5"
FT HELIX 365..367
FT /evidence="ECO:0007829|PDB:3CX5"
SQ SEQUENCE 368 AA; 40478 MW; 51FDE1C5DA4420D0 CRC64;
MLSAARLQFA QGSVRRLTVS ARDAPTKIST LAVKVHGGSR YATKDGVAHL LNRFNFQNTN
TRSALKLVRE SELLGGTFKS TLDREYITLK ATFLKDDLPY YVNALADVLY KTAFKPHELT
ESVLPAARYD YAVAEQCPVK SAEDQLYAIT FRKGLGNPLL YDGVERVSLQ DIKDFADKVY
TKENLEVSGE NVVEADLKRF VDESLLSTLP AGKSLVSKSE PKFFLGEENR VRFIGDSVAA
IGIPVNKASL AQYEVLANYL TSALSELSGL ISSAKLDKFT DGGLFTLFVR DQDSAVVSSN
IKKIVADLKK GKDLSPAINY TKLKNAVQNE SVSSPIELNF DAVKDFKLGK FNYVAVGDVS
NLPYLDEL
