QCR1_YEAST
ID QCR1_YEAST Reviewed; 457 AA.
AC P07256; D6VPV3;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1988, sequence version 1.
DT 03-AUG-2022, entry version 211.
DE RecName: Full=Cytochrome b-c1 complex subunit 1, mitochondrial;
DE AltName: Full=Complex III subunit 1;
DE AltName: Full=Core protein I;
DE AltName: Full=Ubiquinol-cytochrome c oxidoreductase core protein 1;
DE AltName: Full=Ubiquinol-cytochrome c reductase 44 kDa protein;
DE Flags: Precursor;
GN Name=COR1; Synonyms=QCR1; OrderedLocusNames=YBL045C; ORFNames=YBL0403;
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].
RX PubMed=3023384; DOI=10.1016/s0021-9258(19)76013-x;
RA Tzagoloff A., Wu M., Crivellone M.;
RT "Assembly of the mitochondrial membrane system. Characterization of COR1,
RT the structural gene for the 44-kilodalton core protein of yeast coenzyme
RT QH2-cytochrome c reductase.";
RL J. Biol. Chem. 261:17163-17169(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7871888; DOI=10.1002/yea.320101113;
RA de Wergifosse P., Jacques B., Jonniaux J.-L., Purnelle B., Skala J.,
RA Goffeau A.;
RT "The sequence of a 22.4 kb DNA fragment from the left arm of yeast
RT chromosome II reveals homologues to bacterial proline synthetase and murine
RT alpha-adaptin, as well as a new permease and a DNA-binding protein.";
RL Yeast 10:1489-1496(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA Mewes H.-W., Kleine K.;
RT "Complete DNA sequence of yeast chromosome II.";
RL EMBO J. 13:5795-5809(1994).
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 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 [6]
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 [7]
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 [8]
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 [9]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=14690591; DOI=10.1016/s1097-2765(03)00476-3;
RA Hazbun T.R., Malmstroem L., Anderson S., Graczyk B.J., Fox B., Riffle M.,
RA Sundin B.A., Aranda J.D., McDonald W.H., Chiu C.-H., Snydsman B.E.,
RA Bradley P., Muller E.G.D., Fields S., Baker D., Yates J.R. III, Davis T.N.;
RT "Assigning function to yeast proteins by integration of technologies.";
RL Mol. Cell 12:1353-1365(2003).
RN [10]
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 [11]
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 [12]
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 [13]
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 [14]
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 [15]
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). COR1 interacts with
CC COX5A at the CIII-CIV interface (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 P07256; P07257: QCR2; NbExp=3; IntAct=EBI-19922, EBI-19929;
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:11502169, ECO:0000269|PubMed:18390544,
CC ECO:0000269|PubMed:30598554}; Peripheral membrane protein
CC {ECO:0000269|PubMed:18390544, ECO:0000269|PubMed:30598554}; Matrix side
CC {ECO:0000269|PubMed:18390544, ECO:0000269|PubMed:30598554}.
CC -!- MISCELLANEOUS: Present with 19300 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the peptidase M16 family. UQCRC1/QCR1 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; J02636; AAA34508.1; -; Genomic_DNA.
DR EMBL; X78214; CAA55050.1; -; Genomic_DNA.
DR EMBL; Z35806; CAA84865.1; -; Genomic_DNA.
DR EMBL; AY693047; AAT93066.1; -; Genomic_DNA.
DR EMBL; BK006936; DAA07073.1; -; Genomic_DNA.
DR PIR; A25351; A25351.
DR RefSeq; NP_009508.1; NM_001178285.1.
DR PDB; 1EZV; X-ray; 2.30 A; A=27-457.
DR PDB; 1KB9; X-ray; 2.30 A; A=27-457.
DR PDB; 1KYO; X-ray; 2.97 A; A/L=27-457.
DR PDB; 1P84; X-ray; 2.50 A; A=27-457.
DR PDB; 2IBZ; X-ray; 2.30 A; A=27-457.
DR PDB; 3CX5; X-ray; 1.90 A; A/L=27-457.
DR PDB; 3CXH; X-ray; 2.50 A; A/L=27-457.
DR PDB; 4PD4; X-ray; 3.04 A; A=27-457.
DR PDB; 6GIQ; EM; 3.23 A; A/L=1-457.
DR PDB; 6HU9; EM; 3.35 A; A/L=27-457.
DR PDB; 6T0B; EM; 2.80 A; A/L=27-457.
DR PDB; 6T15; EM; 3.29 A; A/L=27-457.
DR PDB; 6YMX; EM; 3.17 A; A/L=27-457.
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; P07256; -.
DR SMR; P07256; -.
DR BioGRID; 32652; 153.
DR ComplexPortal; CPX-567; Mitochondrial respiratory chain complex III.
DR DIP; DIP-2635N; -.
DR IntAct; P07256; 33.
DR MINT; P07256; -.
DR STRING; 4932.YBL045C; -.
DR iPTMnet; P07256; -.
DR MaxQB; P07256; -.
DR PaxDb; P07256; -.
DR PRIDE; P07256; -.
DR EnsemblFungi; YBL045C_mRNA; YBL045C; YBL045C.
DR GeneID; 852235; -.
DR KEGG; sce:YBL045C; -.
DR SGD; S000000141; COR1.
DR VEuPathDB; FungiDB:YBL045C; -.
DR eggNOG; KOG0960; Eukaryota.
DR HOGENOM; CLU_009902_4_2_1; -.
DR InParanoid; P07256; -.
DR OMA; PYNNGVS; -.
DR BioCyc; MetaCyc:YBL045C-MON; -.
DR BioCyc; YEAST:YBL045C-MON; -.
DR BRENDA; 2.3.1.9; 6758.
DR Reactome; R-SCE-611105; Respiratory electron transport.
DR EvolutionaryTrace; P07256; -.
DR PRO; PR:P07256; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P07256; 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; IDA:SGD.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0004222; F:metalloendopeptidase activity; IBA:GO_Central.
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:0006627; P:protein processing involved in protein targeting to mitochondrion; IBA:GO_Central.
DR GO; GO:1902600; P:proton transmembrane transport; IEA:GOC.
DR InterPro; IPR011249; Metalloenz_LuxS/M16.
DR InterPro; IPR011765; Pept_M16_N.
DR InterPro; IPR007863; Peptidase_M16_C.
DR Pfam; PF00675; Peptidase_M16; 1.
DR Pfam; PF05193; Peptidase_M16_C; 1.
DR SUPFAM; SSF63411; SSF63411; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Electron transport; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Reference proteome; Respiratory chain;
KW Transit peptide; Transport.
FT TRANSIT 1..26
FT /note="Mitochondrion"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:3023384"
FT CHAIN 27..457
FT /note="Cytochrome b-c1 complex subunit 1, mitochondrial"
FT /id="PRO_0000026788"
FT STRAND 30..42
FT /evidence="ECO:0007829|PDB:3CX5"
FT STRAND 47..56
FT /evidence="ECO:0007829|PDB:3CX5"
FT HELIX 59..61
FT /evidence="ECO:0007829|PDB:3CX5"
FT TURN 64..68
FT /evidence="ECO:0007829|PDB:3CX5"
FT HELIX 69..77
FT /evidence="ECO:0007829|PDB:3CX5"
FT HELIX 80..88
FT /evidence="ECO:0007829|PDB:3CX5"
FT STRAND 92..97
FT /evidence="ECO:0007829|PDB:3CX5"
FT STRAND 102..108
FT /evidence="ECO:0007829|PDB:3CX5"
FT HELIX 110..112
FT /evidence="ECO:0007829|PDB:1EZV"
FT HELIX 113..124
FT /evidence="ECO:0007829|PDB:3CX5"
FT TURN 129..132
FT /evidence="ECO:0007829|PDB:3CX5"
FT HELIX 134..154
FT /evidence="ECO:0007829|PDB:3CX5"
FT HELIX 156..168
FT /evidence="ECO:0007829|PDB:3CX5"
FT TURN 169..171
FT /evidence="ECO:0007829|PDB:3CX5"
FT HELIX 173..175
FT /evidence="ECO:0007829|PDB:3CX5"
FT HELIX 182..186
FT /evidence="ECO:0007829|PDB:3CX5"
FT HELIX 190..200
FT /evidence="ECO:0007829|PDB:3CX5"
FT HELIX 203..205
FT /evidence="ECO:0007829|PDB:3CX5"
FT STRAND 206..213
FT /evidence="ECO:0007829|PDB:3CX5"
FT HELIX 216..223
FT /evidence="ECO:0007829|PDB:3CX5"
FT STRAND 247..252
FT /evidence="ECO:0007829|PDB:3CX5"
FT STRAND 256..266
FT /evidence="ECO:0007829|PDB:3CX5"
FT HELIX 275..285
FT /evidence="ECO:0007829|PDB:3CX5"
FT STRAND 287..289
FT /evidence="ECO:0007829|PDB:3CX5"
FT HELIX 295..297
FT /evidence="ECO:0007829|PDB:3CX5"
FT HELIX 302..307
FT /evidence="ECO:0007829|PDB:3CX5"
FT TURN 308..310
FT /evidence="ECO:0007829|PDB:3CX5"
FT STRAND 313..321
FT /evidence="ECO:0007829|PDB:3CX5"
FT STRAND 326..335
FT /evidence="ECO:0007829|PDB:3CX5"
FT HELIX 340..356
FT /evidence="ECO:0007829|PDB:3CX5"
FT HELIX 360..378
FT /evidence="ECO:0007829|PDB:3CX5"
FT HELIX 383..397
FT /evidence="ECO:0007829|PDB:3CX5"
FT HELIX 403..412
FT /evidence="ECO:0007829|PDB:3CX5"
FT HELIX 415..425
FT /evidence="ECO:0007829|PDB:3CX5"
FT TURN 426..428
FT /evidence="ECO:0007829|PDB:3CX5"
FT STRAND 432..438
FT /evidence="ECO:0007829|PDB:3CX5"
FT STRAND 440..442
FT /evidence="ECO:0007829|PDB:4PD4"
FT HELIX 445..450
FT /evidence="ECO:0007829|PDB:3CX5"
SQ SEQUENCE 457 AA; 50228 MW; AE58739EFB695254 CRC64;
MLRTVTSKTV SNQFKRSLAT AVATPKAEVT QLSNGIVVAT EHNPSAHTAS VGVVFGSGAA
NENPYNNGVS NLWKNIFLSK ENSAVAAKEG LALSSNISRD FQSYIVSSLP GSTDKSLDFL
NQSFIQQKAN LLSSSNFEAT KKSVLKQVQD FEENDHPNRV LEHLHSTAFQ NTPLSLPTRG
TLESLENLVV ADLESFANNH FLNSNAVVVG TGNIKHEDLV NSIESKNLSL QTGTKPVLKK
KAAFLGSEVR LRDDTLPKAW ISLAVEGEPV NSPNYFVAKL AAQIFGSYNA FEPASRLQGI
KLLDNIQEYQ LCDNFNHFSL SYKDSGLWGF STATRNVTMI DDLIHFTLKQ WNRLTISVTD
TEVERAKSLL KLQLGQLYES GNPVNDANLL GAEVLIKGSK LSLGEAFKKI DAITVKDVKA
WAGKRLWDQD IAIAGTGQIE GLLDYMRIRS DMSMMRW
