QCR10_BOVIN
ID QCR10_BOVIN Reviewed; 56 AA.
AC P07552; A1A4P1; O18996; Q3T176;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 2.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Cytochrome b-c1 complex subunit 10;
DE AltName: Full=Complex III subunit 10;
DE AltName: Full=Complex III subunit XI;
DE AltName: Full=Ubiquinol-cytochrome c reductase complex 6.4 kDa protein;
GN Name=UQCR11; Synonyms=UQCR;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP PROTEIN SEQUENCE.
RC TISSUE=Heart;
RX PubMed=2995132; DOI=10.1016/0014-5793(85)80434-8;
RA Schaegger H., Borchart U., Aquila H., Link T.A., von Jagow G.;
RT "Isolation and amino acid sequence of the smallest subunit of beef heart
RT bc1 complex.";
RL FEBS Lett. 190:89-94(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Heart muscle;
RX PubMed=9161705; DOI=10.1080/15216549700202191;
RA Islam M.M., Suzuki H., Yoneda M., Tanaka M.;
RT "Primary structure of the smallest (6.4-kDa) subunit of human and bovine
RT ubiquinol-cytochrome c reductase deduced from cDNA sequences.";
RL Biochem. Mol. Biol. Int. 41:1109-1116(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus, and Hereford; TISSUE=Fetal pons, and Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
RX PubMed=9204897; DOI=10.1126/science.277.5322.60;
RA Xia D., Yu C.A., Kim H., Xia J.Z., Kachurin A.M., Zhang L., Yu L.,
RA Deisenhofer J.;
RT "Crystal structure of the cytochrome bc1 complex from bovine heart
RT mitochondria.";
RL Science 277:60-66(1997).
RN [5]
RP ERRATUM OF PUBMED:9204897.
RA Xia D., Yu C.A., Kim H., Xia J.Z., Kachurin A.M., Zhang L., Yu L.,
RA Deisenhofer J.;
RL Science 278:2037-2037(1997).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
RX PubMed=9651245; DOI=10.1126/science.281.5373.64;
RA Iwata S., Lee J.W., Okada K., Lee J.K., Iwata M., Rasmussen B., Link T.A.,
RA Ramaswamy S., Jap B.K.;
RT "Complete structure of the 11-subunit bovine mitochondrial cytochrome bc1
RT complex.";
RL Science 281:64-71(1998).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS).
RX PubMed=12269811; DOI=10.1021/bi026252p;
RA Gao X., Wen X., Yu C., Esser L., Tsao S., Quinn B., Zhang L., Yu L.,
RA Xia D.;
RT "The crystal structure of mitochondrial cytochrome bc1 in complex with
RT famoxadone: the role of aromatic-aromatic interaction in inhibition.";
RL Biochemistry 41:11692-11702(2002).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.69 ANGSTROMS).
RX PubMed=15312779; DOI=10.1016/j.jmb.2004.05.065;
RA Esser L., Quinn B., Li Y.F., Zhang M., Elberry M., Yu L., Yu C.A., Xia D.;
RT "Crystallographic studies of quinol oxidation site inhibitors: a modified
RT classification of inhibitors for the cytochrome bc(1) complex.";
RL J. Mol. Biol. 341:281-302(2004).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.26 ANGSTROMS).
RX PubMed=16924113; DOI=10.1073/pnas.0601149103;
RA Esser L., Gong X., Yang S., Yu L., Yu C.A., Xia D.;
RT "Surface-modulated motion switch: capture and release of iron-sulfur
RT protein in the cytochrome bc1 complex.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:13045-13050(2006).
RN [10]
RP STRUCTURE BY ELECTRON MICROSCOPY (9.10 ANGSTROMS), AND SUBUNIT.
RX PubMed=27830641; DOI=10.7554/elife.21290;
RA Sousa J.S., Mills D.J., Vonck J., Kuehlbrandt W.;
RT "Functional asymmetry and electron flow in the bovine respirasome.";
RL Elife 5:0-0(2016).
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. QCR10 has a role in CIII assembly and RIP1
CC stability. {ECO:0000250|UniProtKB:P37299}.
CC -!- SUBUNIT: Component of the ubiquinol-cytochrome c oxidoreductase
CC (cytochrome b-c1 complex, complex III, CIII), a multisubunit enzyme
CC composed of 11 subunits. The complex is composed of 3 respiratory
CC subunits cytochrome b, cytochrome c1 and Rieske protein UQCRFS1, 2 core
CC protein subunits UQCRC1/QCR1 and UQCRC2/QCR2, and 6 low-molecular
CC weight protein subunits UQCRH/QCR6, UQCRB/QCR7, UQCRQ/QCR8,
CC UQCR10/QCR9, UQCR11/QCR10 and subunit 9, the cleavage product of Rieske
CC protein UQCRFS1 (PubMed:9651245). The complex exists as an obligatory
CC dimer and forms supercomplexes (SCs) in the inner mitochondrial
CC membrane with NADH-ubiquinone oxidoreductase (complex I, CI) and
CC cytochrome c oxidase (complex IV, CIV), resulting in different
CC assemblies (supercomplex SCI(1)III(2)IV(1) and megacomplex
CC MCI(2)III(2)IV(2)) (PubMed:27830641). {ECO:0000269|PubMed:27830641,
CC ECO:0000269|PubMed:9651245}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:P37299}; Single-pass membrane protein
CC {ECO:0000250|UniProtKB:P37299}.
CC -!- SIMILARITY: Belongs to the UQCR11/QCR10 family. {ECO:0000305}.
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DR EMBL; D55637; BAA21747.1; -; mRNA.
DR EMBL; BC102080; AAI02081.1; -; mRNA.
DR EMBL; BC126774; AAI26775.1; -; mRNA.
DR PIR; A24096; CBBOC6.
DR RefSeq; NP_776640.1; NM_174215.2.
DR PDB; 1BE3; X-ray; 3.00 A; K=1-56.
DR PDB; 1BGY; X-ray; 3.00 A; K/W=1-56.
DR PDB; 1L0L; X-ray; 2.35 A; K=1-56.
DR PDB; 1L0N; X-ray; 2.60 A; K=1-56.
DR PDB; 1NTK; X-ray; 2.60 A; K=1-56.
DR PDB; 1NTM; X-ray; 2.40 A; K=1-56.
DR PDB; 1NTZ; X-ray; 2.60 A; K=1-56.
DR PDB; 1NU1; X-ray; 3.20 A; K=1-56.
DR PDB; 1QCR; X-ray; 2.70 A; K=1-45.
DR PDB; 1SQB; X-ray; 2.69 A; K=1-56.
DR PDB; 1SQP; X-ray; 2.70 A; K=1-56.
DR PDB; 1SQQ; X-ray; 3.00 A; K=1-56.
DR PDB; 1SQV; X-ray; 2.85 A; K=1-56.
DR PDB; 1SQX; X-ray; 2.60 A; K=1-56.
DR PDB; 2FYU; X-ray; 2.26 A; K=1-56.
DR PDB; 2YBB; EM; 19.00 A; K/k=1-56.
DR PDB; 5GPN; EM; 5.40 A; K/V=1-56.
DR PDB; 5KLV; X-ray; 2.65 A; K=2-56.
DR PDB; 5LUF; EM; 9.10 A; k/w=1-56.
DR PDB; 5NMI; X-ray; 3.50 A; K/X=15-36.
DR PDB; 6NHG; X-ray; 2.80 A; K=2-56.
DR PDBsum; 1BE3; -.
DR PDBsum; 1BGY; -.
DR PDBsum; 1L0L; -.
DR PDBsum; 1L0N; -.
DR PDBsum; 1NTK; -.
DR PDBsum; 1NTM; -.
DR PDBsum; 1NTZ; -.
DR PDBsum; 1NU1; -.
DR PDBsum; 1QCR; -.
DR PDBsum; 1SQB; -.
DR PDBsum; 1SQP; -.
DR PDBsum; 1SQQ; -.
DR PDBsum; 1SQV; -.
DR PDBsum; 1SQX; -.
DR PDBsum; 2FYU; -.
DR PDBsum; 2YBB; -.
DR PDBsum; 5GPN; -.
DR PDBsum; 5KLV; -.
DR PDBsum; 5LUF; -.
DR PDBsum; 5NMI; -.
DR PDBsum; 6NHG; -.
DR AlphaFoldDB; P07552; -.
DR SMR; P07552; -.
DR CORUM; P07552; -.
DR DIP; DIP-61255N; -.
DR IntAct; P07552; 1.
DR STRING; 9913.ENSBTAP00000011458; -.
DR PaxDb; P07552; -.
DR PRIDE; P07552; -.
DR Ensembl; ENSBTAT00000011458; ENSBTAP00000011458; ENSBTAG00000008692.
DR GeneID; 281570; -.
DR KEGG; bta:281570; -.
DR CTD; 10975; -.
DR VEuPathDB; HostDB:ENSBTAG00000008692; -.
DR eggNOG; ENOG502S9FZ; Eukaryota.
DR GeneTree; ENSGT00390000018299; -.
DR HOGENOM; CLU_211742_0_0_1; -.
DR InParanoid; P07552; -.
DR OMA; ASMWGAV; -.
DR OrthoDB; 1621371at2759; -.
DR TreeFam; TF105034; -.
DR EvolutionaryTrace; P07552; -.
DR Proteomes; UP000009136; Chromosome 7.
DR Bgee; ENSBTAG00000008692; Expressed in cardiac ventricle and 109 other tissues.
DR GO; GO:0005743; C:mitochondrial inner membrane; IBA:GO_Central.
DR GO; GO:0005750; C:mitochondrial respiratory chain complex III; IEA:Ensembl.
DR GO; GO:0006122; P:mitochondrial electron transport, ubiquinol to cytochrome c; IEA:InterPro.
DR InterPro; IPR029027; Single_a-helix_sf.
DR InterPro; IPR015089; UQCR.
DR PANTHER; PTHR15420; PTHR15420; 1.
DR Pfam; PF08997; UCR_6-4kD; 1.
DR SUPFAM; SSF81518; SSF81518; 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 CHAIN 1..56
FT /note="Cytochrome b-c1 complex subunit 10"
FT /id="PRO_0000193559"
FT TOPO_DOM 1..12
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000269|PubMed:9651245"
FT TRANSMEM 13..35
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:9651245"
FT TOPO_DOM 36..56
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000269|PubMed:9651245"
FT CONFLICT 22
FT /note="S -> Q (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 34
FT /note="W -> S (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 38
FT /note="W -> S (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 2..5
FT /evidence="ECO:0007829|PDB:2FYU"
FT HELIX 8..36
FT /evidence="ECO:0007829|PDB:2FYU"
FT HELIX 39..42
FT /evidence="ECO:0007829|PDB:2FYU"
FT STRAND 44..47
FT /evidence="ECO:0007829|PDB:2FYU"
FT HELIX 48..51
FT /evidence="ECO:0007829|PDB:1SQQ"
SQ SEQUENCE 56 AA; 6520 MW; A412EA7EB58F45FE CRC64;
MLTRFLGPRY RQLARNWVPT ASLWGAVGAV GLVWATDWRL ILDWVPYING KFKKDD
