QCR7_BOVIN
ID QCR7_BOVIN Reviewed; 111 AA.
AC P00129; Q3SZ83;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Cytochrome b-c1 complex subunit 7;
DE AltName: Full=Complex III subunit 7;
DE AltName: Full=Complex III subunit VII;
DE AltName: Full=QP-C;
DE AltName: Full=Ubiquinol-cytochrome c reductase complex 14 kDa protein;
GN Name=UQCRB;
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 [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 [2]
RP PROTEIN SEQUENCE OF 2-111, AND ACETYLATION AT ALA-2.
RX PubMed=2981208; DOI=10.1016/s0021-9258(18)89737-x;
RA Wakabayashi S., Takao T., Shimonishi Y., Kuramitsu S., Matsubara H.,
RA Wang T., Zhang Z., King T.E.;
RT "Complete amino acid sequence of the ubiquinone binding protein (QP-C), a
RT protein similar to the 14,000-dalton subunit of the yeast ubiquinol-
RT cytochrome c reductase complex.";
RL J. Biol. Chem. 260:337-343(1985).
RN [3]
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 [4]
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 [5]
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 [6]
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 [7]
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 [8]
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 [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. {ECO:0000250|UniProtKB:P00128}.
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:P00128}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P00128}; Matrix side
CC {ECO:0000250|UniProtKB:P00128}.
CC -!- SIMILARITY: Belongs to the UQCRB/QCR7 family. {ECO:0000305}.
CC -!- CAUTION: Was originally thought to be the ubiquinone-binding protein
CC (QP-C). {ECO:0000305|PubMed:2981208}.
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DR EMBL; BC103057; AAI03058.1; -; mRNA.
DR PIR; A00122; UYBO.
DR RefSeq; NP_001029969.1; NM_001034797.2.
DR PDB; 1BCC; X-ray; 3.16 A; F=2-108.
DR PDB; 1BE3; X-ray; 3.00 A; F=2-111.
DR PDB; 1BGY; X-ray; 3.00 A; F/R=2-111.
DR PDB; 1L0L; X-ray; 2.35 A; F=2-111.
DR PDB; 1L0N; X-ray; 2.60 A; F=2-111.
DR PDB; 1NTK; X-ray; 2.60 A; F=2-111.
DR PDB; 1NTM; X-ray; 2.40 A; F=2-111.
DR PDB; 1NTZ; X-ray; 2.60 A; F=2-111.
DR PDB; 1NU1; X-ray; 3.20 A; F=2-111.
DR PDB; 1PP9; X-ray; 2.10 A; F/S=2-111.
DR PDB; 1PPJ; X-ray; 2.10 A; F/S=2-111.
DR PDB; 1QCR; X-ray; 2.70 A; F=9-111.
DR PDB; 1SQB; X-ray; 2.69 A; F=2-111.
DR PDB; 1SQP; X-ray; 2.70 A; F=2-111.
DR PDB; 1SQQ; X-ray; 3.00 A; F=2-111.
DR PDB; 1SQV; X-ray; 2.85 A; F=2-111.
DR PDB; 1SQX; X-ray; 2.60 A; F=2-111.
DR PDB; 2A06; X-ray; 2.10 A; F/S=2-111.
DR PDB; 2BCC; X-ray; 3.50 A; F=2-108.
DR PDB; 2FYU; X-ray; 2.26 A; F=2-111.
DR PDB; 2YBB; EM; 19.00 A; F/f=2-111.
DR PDB; 3BCC; X-ray; 3.70 A; F=2-108.
DR PDB; 4D6T; X-ray; 3.57 A; F/S=1-111.
DR PDB; 4D6U; X-ray; 4.09 A; F/S=1-111.
DR PDB; 5KLV; X-ray; 2.65 A; F=2-111.
DR PDB; 5LUF; EM; 9.10 A; f/r=2-111.
DR PDB; 5NMI; X-ray; 3.50 A; F/S=1-111.
DR PDB; 5OKD; X-ray; 3.10 A; F=1-111.
DR PDB; 6FO0; EM; 4.10 A; F/S=1-111.
DR PDB; 6FO2; EM; 4.40 A; F/S=1-111.
DR PDB; 6FO6; EM; 4.10 A; F/S=1-111.
DR PDB; 6HAW; X-ray; 3.45 A; F=12-110.
DR PDB; 6NHG; X-ray; 2.80 A; F=2-111.
DR PDB; 6XVF; X-ray; 3.50 A; F=12-111.
DR PDB; 6ZFS; X-ray; 3.50 A; F=12-110.
DR PDB; 6ZFT; X-ray; 3.30 A; F=12-110.
DR PDB; 6ZFU; X-ray; 3.50 A; F=12-110.
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; 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; P00129; -.
DR SMR; P00129; -.
DR CORUM; P00129; -.
DR DIP; DIP-1082N; -.
DR IntAct; P00129; 3.
DR STRING; 9913.ENSBTAP00000001993; -.
DR iPTMnet; P00129; -.
DR PaxDb; P00129; -.
DR PRIDE; P00129; -.
DR Ensembl; ENSBTAT00000001993; ENSBTAP00000001993; ENSBTAG00000001521.
DR GeneID; 616871; -.
DR KEGG; bta:616871; -.
DR CTD; 7381; -.
DR VEuPathDB; HostDB:ENSBTAG00000001521; -.
DR VGNC; VGNC:36694; UQCRB.
DR eggNOG; KOG3440; Eukaryota.
DR GeneTree; ENSGT00390000012916; -.
DR HOGENOM; CLU_115154_2_0_1; -.
DR InParanoid; P00129; -.
DR OMA; WTIYEED; -.
DR OrthoDB; 1606436at2759; -.
DR TreeFam; TF105035; -.
DR EvolutionaryTrace; P00129; -.
DR Proteomes; UP000009136; Chromosome 14.
DR Bgee; ENSBTAG00000001521; Expressed in cardiac ventricle and 105 other tissues.
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; 1.10.1090.10; -; 1.
DR InterPro; IPR003197; QCR7.
DR InterPro; IPR036544; QCR7_sf.
DR PANTHER; PTHR12022; PTHR12022; 1.
DR Pfam; PF02271; UCR_14kD; 1.
DR PIRSF; PIRSF000022; Bc1_14K; 1.
DR SUPFAM; SSF81524; SSF81524; 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; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:2981208"
FT CHAIN 2..111
FT /note="Cytochrome b-c1 complex subunit 7"
FT /id="PRO_0000193523"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|PubMed:2981208"
FT MOD_RES 19
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9D855"
FT MOD_RES 78
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9D855"
FT MOD_RES 78
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9D855"
FT MOD_RES 83
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9D855"
FT MOD_RES 88
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9D855"
FT MOD_RES 88
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9D855"
FT MOD_RES 96
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9D855"
FT CONFLICT 57
FT /note="N -> D (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT TURN 9..13
FT /evidence="ECO:0007829|PDB:1SQP"
FT HELIX 14..25
FT /evidence="ECO:0007829|PDB:1PP9"
FT HELIX 27..30
FT /evidence="ECO:0007829|PDB:1PP9"
FT HELIX 34..37
FT /evidence="ECO:0007829|PDB:1PP9"
FT HELIX 42..49
FT /evidence="ECO:0007829|PDB:1PP9"
FT HELIX 53..71
FT /evidence="ECO:0007829|PDB:1PP9"
FT HELIX 78..80
FT /evidence="ECO:0007829|PDB:1PP9"
FT HELIX 84..86
FT /evidence="ECO:0007829|PDB:1PP9"
FT HELIX 92..110
FT /evidence="ECO:0007829|PDB:1PP9"
SQ SEQUENCE 111 AA; 13476 MW; 2D89B44D53DA494B CRC64;
MAGRPAVSAS SRWLEGIRKW YYNAAGFNKL GLMRDDTIHE NDDVKEAIRR LPENLYNDRV
FRIKRALDLS MRQQILPKEQ WTKYEEDKSY LEPYLKEVIR ERKEREEWAK K
