QCR6_BOVIN
ID QCR6_BOVIN Reviewed; 91 AA.
AC P00126; Q3SZS4;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 27-JUN-2006, sequence version 2.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Cytochrome b-c1 complex subunit 6, mitochondrial;
DE AltName: Full=Complex III subunit 6;
DE AltName: Full=Complex III subunit VIII;
DE AltName: Full=Cytochrome c1 non-heme 11 kDa protein;
DE AltName: Full=Mitochondrial hinge protein;
DE AltName: Full=Ubiquinol-cytochrome c reductase complex 11 kDa protein;
DE Flags: Precursor;
GN Name=UQCRH;
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=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE OF 14-91.
RX PubMed=6126477; DOI=10.1093/oxfordjournals.jbchem.a133901;
RA Wakabayashi S., Takeda H., Matsubara H., Kim C.H., King T.E.;
RT "Identity of the heme-not-containing protein in bovine heart cytochrome c1
RT preparation with the protein mediating c1-c complex formation -- a protein
RT with high glutamic acid content.";
RL J. Biochem. 91:2077-2085(1982).
RN [3]
RP DISULFIDE BONDS.
RX PubMed=3003044; DOI=10.1093/oxfordjournals.jbchem.a135409;
RA Mukai K., Miyazaki T., Wakabayashi S., Kuramitsu S., Matsubara H.;
RT "Dissociation of bovine cytochrome c1 subcomplex and the status of cysteine
RT residues in the subunits.";
RL J. Biochem. 98:1417-1425(1985).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 14-91.
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) OF 14-91.
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 (2.1 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 [10]
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 [11]
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:P00127}.
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:P00127}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P00127}; Intermembrane side
CC {ECO:0000250|UniProtKB:P00127}.
CC -!- SIMILARITY: Belongs to the UQCRH/QCR6 family. {ECO:0000305}.
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DR EMBL; BC102729; AAI02730.1; -; mRNA.
DR PIR; A00119; CCBO11.
DR RefSeq; NP_001029917.1; NM_001034745.2.
DR PDB; 1BCC; X-ray; 3.16 A; H=14-91.
DR PDB; 1BE3; X-ray; 3.00 A; H=14-91.
DR PDB; 1BGY; X-ray; 3.00 A; H/T=14-91.
DR PDB; 1L0L; X-ray; 2.35 A; H=14-91.
DR PDB; 1L0N; X-ray; 2.60 A; H=14-91.
DR PDB; 1NTK; X-ray; 2.60 A; H=14-91.
DR PDB; 1NTM; X-ray; 2.40 A; H=14-91.
DR PDB; 1NTZ; X-ray; 2.60 A; H=14-91.
DR PDB; 1NU1; X-ray; 3.20 A; H=14-91.
DR PDB; 1PP9; X-ray; 2.10 A; H/U=14-91.
DR PDB; 1PPJ; X-ray; 2.10 A; H/U=14-91.
DR PDB; 1QCR; X-ray; 2.70 A; H=31-90.
DR PDB; 1SQB; X-ray; 2.69 A; H=14-91.
DR PDB; 1SQP; X-ray; 2.70 A; H=14-91.
DR PDB; 1SQQ; X-ray; 3.00 A; H=14-91.
DR PDB; 1SQV; X-ray; 2.85 A; H=14-91.
DR PDB; 1SQX; X-ray; 2.60 A; H=14-91.
DR PDB; 2A06; X-ray; 2.10 A; H/U=14-91.
DR PDB; 2BCC; X-ray; 3.50 A; H=14-91.
DR PDB; 2FYU; X-ray; 2.26 A; H=14-91.
DR PDB; 2YBB; EM; 19.00 A; H/h=14-91.
DR PDB; 3BCC; X-ray; 3.70 A; H=14-91.
DR PDB; 4D6T; X-ray; 3.57 A; H/U=1-91.
DR PDB; 4D6U; X-ray; 4.09 A; H/U=1-91.
DR PDB; 5GPN; EM; 5.40 A; H/T=14-91.
DR PDB; 5KLV; X-ray; 2.65 A; H=14-91.
DR PDB; 5LUF; EM; 9.10 A; h/t=14-91.
DR PDB; 5NMI; X-ray; 3.50 A; H/U=1-91.
DR PDB; 5OKD; X-ray; 3.10 A; H=1-91.
DR PDB; 6FO0; EM; 4.10 A; H/U=1-91.
DR PDB; 6FO2; EM; 4.40 A; H/U=1-91.
DR PDB; 6FO6; EM; 4.10 A; H/U=1-91.
DR PDB; 6HAW; X-ray; 3.45 A; H=27-90.
DR PDB; 6NHG; X-ray; 2.80 A; H=14-91.
DR PDB; 6XVF; X-ray; 3.50 A; H=27-90.
DR PDB; 6ZFS; X-ray; 3.50 A; H=27-90.
DR PDB; 6ZFT; X-ray; 3.30 A; H=26-90.
DR PDB; 6ZFU; X-ray; 3.50 A; H=26-90.
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; P00126; -.
DR SMR; P00126; -.
DR CORUM; P00126; -.
DR DIP; DIP-38973N; -.
DR IntAct; P00126; 2.
DR STRING; 9913.ENSBTAP00000012635; -.
DR PaxDb; P00126; -.
DR PeptideAtlas; P00126; -.
DR PRIDE; P00126; -.
DR Ensembl; ENSBTAT00000075187; ENSBTAP00000067387; ENSBTAG00000009603.
DR GeneID; 613899; -.
DR KEGG; bta:613899; -.
DR CTD; 7388; -.
DR VEuPathDB; HostDB:ENSBTAG00000009603; -.
DR eggNOG; KOG4763; Eukaryota.
DR GeneTree; ENSGT00390000003860; -.
DR HOGENOM; CLU_115913_3_0_1; -.
DR InParanoid; P00126; -.
DR OMA; CQSKGHI; -.
DR OrthoDB; 1621720at2759; -.
DR TreeFam; TF105036; -.
DR EvolutionaryTrace; P00126; -.
DR Proteomes; UP000009136; Chromosome 3.
DR Bgee; ENSBTAG00000009603; Expressed in cardiac ventricle and 107 other tissues.
DR ExpressionAtlas; P00126; baseline and differential.
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; 1.10.287.20; -; 1.
DR InterPro; IPR003422; Cyt_b-c1_6.
DR InterPro; IPR023184; Ubol_cytC_Rdtase_hinge_dom.
DR InterPro; IPR036811; Ubol_cytC_Rdtase_hinge_dom_sf.
DR PANTHER; PTHR15336; PTHR15336; 1.
DR Pfam; PF02320; UCR_hinge; 1.
DR PIRSF; PIRSF000019; Bc1_11K; 1.
DR SUPFAM; SSF81531; SSF81531; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Direct protein sequencing; Disulfide bond;
KW Electron transport; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW Reference proteome; Respiratory chain; Transit peptide; Transport.
FT TRANSIT 1..13
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:6126477"
FT CHAIN 14..91
FT /note="Cytochrome b-c1 complex subunit 6, mitochondrial"
FT /id="PRO_0000193540"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 42
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P99028"
FT MOD_RES 85
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P99028"
FT DISULFID 37..81
FT /evidence="ECO:0000269|PubMed:3003044"
FT DISULFID 53..67
FT /evidence="ECO:0000269|PubMed:3003044"
FT HELIX 17..24
FT /evidence="ECO:0007829|PDB:1L0L"
FT HELIX 29..37
FT /evidence="ECO:0007829|PDB:1PP9"
FT STRAND 38..40
FT /evidence="ECO:0007829|PDB:1SQV"
FT HELIX 41..58
FT /evidence="ECO:0007829|PDB:1PP9"
FT STRAND 61..63
FT /evidence="ECO:0007829|PDB:1L0L"
FT HELIX 68..85
FT /evidence="ECO:0007829|PDB:1PP9"
FT HELIX 86..89
FT /evidence="ECO:0007829|PDB:1PP9"
SQ SEQUENCE 91 AA; 10624 MW; F444A2E7B6A147D4 CRC64;
MGLEDEQRML TGSGDPKEEE EEEEELVDPL TTVREQCEQL EKCVKARERL ELCDERVSSR
SQTEEDCTEE LLDFLHARDH CVAHKLFNSL K
