ID   QCR10_YEAST             Reviewed;          77 AA.
AC   P37299; D3DKR8; O13538; Q9T2W2;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   27-MAR-2024, entry version 158.
DE   RecName: Full=Cytochrome b-c1 complex subunit 10, mitochondrial;
DE   AltName: Full=Complex III subunit 10;
DE   AltName: Full=Complex III subunit XI;
DE   AltName: Full=Ubiquinol-cytochrome c oxidoreductase subunit 10;
DE   AltName: Full=Ubiquinol-cytochrome c reductase 8.5 kDa protein;
GN   Name=QCR10; OrderedLocusNames=YHR001W-A; ORFNames=YHR001BW;
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 FUNCTION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=8175712; DOI=10.1016/s0021-9258(18)99967-9;
RA   Brandt U., Uribe S., Schaegger H., Trumpower B.L.;
RT   "Isolation and characterization of QCR10, the nuclear gene encoding the
RT   8.5-kDa subunit 10 of the Saccharomyces cerevisiae cytochrome bc1
RT   complex.";
RL   J. Biol. Chem. 269:12947-12953(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=8091229; DOI=10.1126/science.8091229;
RA   Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z.,
RA   Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T.,
RA   Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P., Louis E.J.,
RA   Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L.,
RA   St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P.,
RA   Waterston R., Wilson R., Vaudin M.;
RT   "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
RT   VIII.";
RL   Science 265:2077-2082(1994).
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   PROTEIN SEQUENCE OF 2-29 AND 38-59.
RC   STRAIN=GM50-3C;
RX   PubMed=1325905; DOI=10.1111/j.1432-1033.1992.tb17197.x;
RA   Geier B.M., Schaegger H., Brandt U., Colson A.-M., von Jagow G.;
RT   "Point mutation in cytochrome b of yeast ubihydroquinone:cytochrome-c
RT   oxidoreductase causing myxothiazol resistance and facilitated dissociation
RT   of the iron-sulfur subunit.";
RL   Eur. J. Biochem. 208:375-380(1992).
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   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   [9]
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 (Probable). QCR10 has a role in CIII assembly
CC       and RIP1 stability (PubMed:8175712, PubMed:30598556, PubMed:30598554).
CC       {ECO:0000269|PubMed:30598554, ECO:0000269|PubMed:30598556,
CC       ECO:0000269|PubMed:8175712, ECO:0000305|PubMed:30598554}.
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:30598554). The complex exists as an obligatory dimer and forms
CC       supercomplexes (SCs) in the inner mitochondrial membrane with a monomer
CC       or a dimer of cytochrome c oxidase (complex IV, CIV), resulting in 2
CC       different assemblies (supercomplexes III(2)IV and III(2)IV(2))
CC       (PubMed:10775262, PubMed:10764779, PubMed:30598556, PubMed:30598554).
CC       QCR10 interacts with CYT1, QCR9 and RIP1 on the intermembrane space
CC       (IMS) and with COR2 and QCR7 on the matrix side (PubMed:30598556,
CC       PubMed:30598554). {ECO:0000269|PubMed:10764779,
CC       ECO:0000269|PubMed:10775262, ECO:0000269|PubMed:30598554,
CC       ECO:0000269|PubMed:30598556}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000269|PubMed:30598554}; Single-pass membrane protein
CC       {ECO:0000269|PubMed:30598554}.
CC   -!- MISCELLANEOUS: Present with 5590 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the UQCR11/QCR10 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB68434.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; U07275; AAA19322.1; -; Unassigned_DNA.
DR   EMBL; U10555; AAB68434.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; BK006934; DAA06688.1; -; Genomic_DNA.
DR   PIR; A53768; A53768.
DR   RefSeq; NP_011864.1; NM_001181426.1.
DR   PDB; 6GIQ; EM; 3.23 A; U/V=1-77.
DR   PDB; 6HU9; EM; 3.35 A; J/U=1-77.
DR   PDB; 6T0B; EM; 2.80 A; J/U=1-77.
DR   PDB; 6T15; EM; 3.29 A; J/U=1-77.
DR   PDB; 8E7S; EM; 3.20 A; D/d=1-77.
DR   PDBsum; 6GIQ; -.
DR   PDBsum; 6HU9; -.
DR   PDBsum; 6T0B; -.
DR   PDBsum; 6T15; -.
DR   PDBsum; 8E7S; -.
DR   AlphaFoldDB; P37299; -.
DR   EMDB; EMD-0004; -.
DR   EMDB; EMD-0262; -.
DR   EMDB; EMD-10317; -.
DR   EMDB; EMD-10340; -.
DR   SMR; P37299; -.
DR   BioGRID; 36426; 99.
DR   ComplexPortal; CPX-567; Mitochondrial respiratory chain complex III.
DR   DIP; DIP-7141N; -.
DR   IntAct; P37299; 3.
DR   STRING; 4932.YHR001W-A; -.
DR   MaxQB; P37299; -.
DR   PaxDb; 4932-YHR001W-A; -.
DR   PeptideAtlas; P37299; -.
DR   TopDownProteomics; P37299; -.
DR   EnsemblFungi; YHR001W-A_mRNA; YHR001W-A; YHR001W-A.
DR   GeneID; 856390; -.
DR   KEGG; sce:YHR001W-A; -.
DR   AGR; SGD:S000003529; -.
DR   SGD; S000003529; QCR10.
DR   VEuPathDB; FungiDB:YHR001W-A; -.
DR   eggNOG; ENOG502S83P; Eukaryota.
DR   HOGENOM; CLU_152072_2_0_1; -.
DR   InParanoid; P37299; -.
DR   OMA; VFTEGWP; -.
DR   OrthoDB; 2052076at2759; -.
DR   BioCyc; MetaCyc:G3O-31243-MONOMER; -.
DR   BioCyc; YEAST:G3O-31243-MONOMER; -.
DR   BioGRID-ORCS; 856390; 0 hits in 10 CRISPR screens.
DR   PRO; PR:P37299; -.
DR   Proteomes; UP000002311; Chromosome VIII.
DR   RNAct; P37299; 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; IGI: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   InterPro; IPR019182; Cytochrome_b-c1_su10_fun.
DR   PANTHER; PTHR28254; CYTOCHROME B-C1 COMPLEX SUBUNIT 10; 1.
DR   PANTHER; PTHR28254:SF1; CYTOCHROME B-C1 COMPLEX SUBUNIT 10, MITOCHONDRIAL; 1.
DR   Pfam; PF09796; QCR10; 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:1325905"
FT   CHAIN           2..77
FT                   /note="Cytochrome b-c1 complex subunit 10, mitochondrial"
FT                   /id="PRO_0000193563"
FT   TOPO_DOM        2..21
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000269|PubMed:30598554"
FT   TRANSMEM        22..45
FT                   /note="Helical"
FT                   /evidence="ECO:0000269|PubMed:30598554"
FT   TOPO_DOM        46..77
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000269|PubMed:30598554"
FT   STRAND          9..11
FT                   /evidence="ECO:0007829|PDB:6T15"
FT   STRAND          14..17
FT                   /evidence="ECO:0007829|PDB:6T0B"
FT   HELIX           20..44
FT                   /evidence="ECO:0007829|PDB:6T0B"
FT   TURN            45..47
FT                   /evidence="ECO:0007829|PDB:6T0B"
FT   HELIX           49..54
FT                   /evidence="ECO:0007829|PDB:6T0B"
FT   TURN            55..57
FT                   /evidence="ECO:0007829|PDB:6T0B"
FT   STRAND          60..63
FT                   /evidence="ECO:0007829|PDB:6T0B"
SQ   SEQUENCE   77 AA;  8593 MW;  B9212B4FD194BB3E CRC64;
     MAYTSHLSSK TGLHFGRLSL RSLTAYAPNL MLWGGASMLG LFVFTEGWPK FQDTLYKKIP
     LLGPTLEDHT PPEDKPN
//