QCR8_BOVIN
ID QCR8_BOVIN Reviewed; 82 AA.
AC P13271; Q3ZBT9;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Cytochrome b-c1 complex subunit 8;
DE AltName: Full=Complex III subunit 8;
DE AltName: Full=Complex III subunit VIII;
DE AltName: Full=Ubiquinol-cytochrome c reductase complex 9.5 kDa protein;
DE AltName: Full=Ubiquinol-cytochrome c reductase complex ubiquinone-binding protein QP-C;
GN Name=UQCRQ;
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 NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Heart;
RX PubMed=7592738; DOI=10.1074/jbc.270.43.25634;
RA Yu L., Deng K.-P., Yu C.-A.;
RT "Cloning, gene sequencing, and expression of the small molecular mass
RT ubiquinone-binding protein of mitochondrial ubiquinol-cytochrome c
RT reductase.";
RL J. Biol. Chem. 270:25634-25638(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Heart ventricle;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 2-82.
RC TISSUE=Heart;
RX PubMed=3009231; DOI=10.1016/0014-5793(86)80515-4;
RA Borchart U., Machleidt W., Schaegger H., Link T.A., von Jagow G.;
RT "Isolation and amino acid sequence of the 9.5 kDa protein of beef heart
RT ubiquinol:cytochrome c reductase.";
RL FEBS Lett. 200:81-86(1986).
RN [4]
RP PROTEIN SEQUENCE OF 2-14 AND 50-58.
RX PubMed=2164842; DOI=10.1021/bi00471a017;
RA Usui S., Yu L., Yu C.A.;
RT "The small molecular mass ubiquinone-binding protein (QPc-9.5 kDa) in
RT mitochondrial ubiquinol-cytochrome c reductase: isolation, ubiquinone-
RT binding domain, and immunoinhibition.";
RL Biochemistry 29:4618-4626(1990).
RN [5]
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 [6]
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 [7]
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 [8]
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 [9]
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 [10]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
RX PubMed=16024040; DOI=10.1016/j.jmb.2005.05.053;
RA Huang L.S., Cobessi D., Tung E.Y., Berry E.A.;
RT "Binding of the respiratory chain inhibitor antimycin to the mitochondrial
RT bc1 complex: a new crystal structure reveals an altered intramolecular
RT hydrogen-bonding pattern.";
RL J. Mol. Biol. 351:573-597(2005).
RN [11]
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 [12]
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. {ECO:0000250|UniProtKB:P08525}.
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). Interacts with BRAWNIN (By
CC similarity). {ECO:0000250|UniProtKB:Q9CQ69,
CC ECO:0000269|PubMed:27830641, ECO:0000269|PubMed:9651245}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:P08525}; Single-pass membrane protein
CC {ECO:0000250|UniProtKB:P08525}.
CC -!- SIMILARITY: Belongs to the UQCRQ/QCR8 family. {ECO:0000305}.
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DR EMBL; L06665; AAB03845.1; -; mRNA.
DR EMBL; BC103110; AAI03111.1; -; mRNA.
DR PIR; A24864; A24864.
DR RefSeq; NP_777230.1; NM_174805.2.
DR PDB; 1BCC; X-ray; 3.16 A; G=2-82.
DR PDB; 1BE3; X-ray; 3.00 A; G=2-82.
DR PDB; 1BGY; X-ray; 3.00 A; G/S=2-82.
DR PDB; 1L0L; X-ray; 2.35 A; G=2-82.
DR PDB; 1L0N; X-ray; 2.60 A; G=2-82.
DR PDB; 1NTK; X-ray; 2.60 A; G=2-82.
DR PDB; 1NTM; X-ray; 2.40 A; G=2-82.
DR PDB; 1NTZ; X-ray; 2.60 A; G=2-82.
DR PDB; 1NU1; X-ray; 3.20 A; G=2-82.
DR PDB; 1PP9; X-ray; 2.10 A; G/T=2-82.
DR PDB; 1PPJ; X-ray; 2.10 A; G/T=2-82.
DR PDB; 1QCR; X-ray; 2.70 A; G=2-71.
DR PDB; 1SQB; X-ray; 2.69 A; G=2-82.
DR PDB; 1SQP; X-ray; 2.70 A; G=2-82.
DR PDB; 1SQQ; X-ray; 3.00 A; G=2-82.
DR PDB; 1SQV; X-ray; 2.85 A; G=2-82.
DR PDB; 1SQX; X-ray; 2.60 A; G=2-82.
DR PDB; 2A06; X-ray; 2.10 A; G/T=2-82.
DR PDB; 2BCC; X-ray; 3.50 A; G=2-82.
DR PDB; 2FYU; X-ray; 2.26 A; G=2-82.
DR PDB; 2YBB; EM; 19.00 A; G/g=2-82.
DR PDB; 3BCC; X-ray; 3.70 A; G=2-82.
DR PDB; 4D6T; X-ray; 3.57 A; G/T=1-82.
DR PDB; 4D6U; X-ray; 4.09 A; G/T=1-82.
DR PDB; 5GPN; EM; 5.40 A; G/S=2-82.
DR PDB; 5KLV; X-ray; 2.65 A; G=2-81.
DR PDB; 5LUF; EM; 9.10 A; g/s=2-82.
DR PDB; 5NMI; X-ray; 3.50 A; G/T=1-82.
DR PDB; 5OKD; X-ray; 3.10 A; G=1-82.
DR PDB; 6FO0; EM; 4.10 A; G/T=1-82.
DR PDB; 6FO2; EM; 4.40 A; G/T=1-82.
DR PDB; 6FO6; EM; 4.10 A; G/T=1-82.
DR PDB; 6HAW; X-ray; 3.45 A; G=3-76.
DR PDB; 6NHG; X-ray; 2.80 A; G=2-81.
DR PDB; 6XVF; X-ray; 3.50 A; G=3-76.
DR PDB; 6ZFS; X-ray; 3.50 A; G=2-76.
DR PDB; 6ZFT; X-ray; 3.30 A; G=3-76.
DR PDB; 6ZFU; X-ray; 3.50 A; G=3-76.
DR PDBsum; 1BCC; -.
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; 1PP9; -.
DR PDBsum; 1PPJ; -.
DR PDBsum; 1QCR; -.
DR PDBsum; 1SQB; -.
DR PDBsum; 1SQP; -.
DR PDBsum; 1SQQ; -.
DR PDBsum; 1SQV; -.
DR PDBsum; 1SQX; -.
DR PDBsum; 2A06; -.
DR PDBsum; 2BCC; -.
DR PDBsum; 2FYU; -.
DR PDBsum; 2YBB; -.
DR PDBsum; 3BCC; -.
DR PDBsum; 4D6T; -.
DR PDBsum; 4D6U; -.
DR PDBsum; 5GPN; -.
DR PDBsum; 5KLV; -.
DR PDBsum; 5LUF; -.
DR PDBsum; 5NMI; -.
DR PDBsum; 5OKD; -.
DR PDBsum; 6FO0; -.
DR PDBsum; 6FO2; -.
DR PDBsum; 6FO6; -.
DR PDBsum; 6HAW; -.
DR PDBsum; 6NHG; -.
DR PDBsum; 6XVF; -.
DR PDBsum; 6ZFS; -.
DR PDBsum; 6ZFT; -.
DR PDBsum; 6ZFU; -.
DR AlphaFoldDB; P13271; -.
DR SMR; P13271; -.
DR CORUM; P13271; -.
DR DIP; DIP-38971N; -.
DR IntAct; P13271; 2.
DR STRING; 9913.ENSBTAP00000040860; -.
DR PaxDb; P13271; -.
DR PRIDE; P13271; -.
DR GeneID; 286885; -.
DR KEGG; bta:286885; -.
DR CTD; 27089; -.
DR eggNOG; KOG4116; Eukaryota.
DR HOGENOM; CLU_156007_2_0_1; -.
DR InParanoid; P13271; -.
DR OrthoDB; 1523793at2759; -.
DR TreeFam; TF300281; -.
DR EvolutionaryTrace; P13271; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005750; C:mitochondrial respiratory chain complex III; IBA:GO_Central.
DR GO; GO:0006122; P:mitochondrial electron transport, ubiquinol to cytochrome c; IBA:GO_Central.
DR Gene3D; 1.20.5.210; -; 1.
DR InterPro; IPR004205; Cyt_bc1_su8.
DR InterPro; IPR036642; Cyt_bc1_su8_sf.
DR PANTHER; PTHR12119; PTHR12119; 1.
DR Pfam; PF02939; UcrQ; 1.
DR SUPFAM; SSF81508; SSF81508; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Direct protein sequencing; Electron transport;
KW Membrane; 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:2164842,
FT ECO:0000269|PubMed:3009231"
FT CHAIN 2..82
FT /note="Cytochrome b-c1 complex subunit 8"
FT /id="PRO_0000193543"
FT TOPO_DOM 2..39
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000269|PubMed:9651245"
FT TRANSMEM 40..68
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:9651245"
FT TOPO_DOM 69..82
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000269|PubMed:9651245"
FT MOD_RES 33
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9CQ69"
FT MOD_RES 33
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9CQ69"
FT CONFLICT 62
FT /note="W -> C (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 5..8
FT /evidence="ECO:0007829|PDB:1L0N"
FT STRAND 12..19
FT /evidence="ECO:0007829|PDB:1PP9"
FT TURN 21..23
FT /evidence="ECO:0007829|PDB:1PP9"
FT STRAND 26..29
FT /evidence="ECO:0007829|PDB:1SQB"
FT HELIX 30..69
FT /evidence="ECO:0007829|PDB:1PP9"
FT TURN 71..73
FT /evidence="ECO:0007829|PDB:1L0L"
FT TURN 74..76
FT /evidence="ECO:0007829|PDB:1BE3"
SQ SEQUENCE 82 AA; 9720 MW; 38D7E52051EB7FFA CRC64;
MGRQFGHLTR VRHVITYSLS PFEQRAFPHY FSKGIPNVLR RTRACILRVA PPFVAFYLVY
TWGTQEFEKS KRKNPAAYEN DR
