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   24-JAN-2024, entry version 173.
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 UQCC6 (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   PDB; 7DGQ; EM; 5.00 A; A3/r=1-82.
DR   PDB; 7DGR; EM; 4.60 A; A2/r=1-82.
DR   PDB; 7DGS; EM; 7.80 A; A2/r=1-82.
DR   PDB; 7DKF; EM; 8.30 A; G1/S1=1-82.
DR   PDB; 7R3V; X-ray; 3.20 A; G=3-76.
DR   PDB; 7TAY; X-ray; 2.95 A; G=2-81.
DR   PDB; 7TZ6; EM; 2.88 A; G/T=2-81.
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   PDBsum; 7DGQ; -.
DR   PDBsum; 7DGR; -.
DR   PDBsum; 7DGS; -.
DR   PDBsum; 7DKF; -.
DR   PDBsum; 7R3V; -.
DR   PDBsum; 7TAY; -.
DR   PDBsum; 7TZ6; -.
DR   AlphaFoldDB; P13271; -.
DR   EMDB; EMD-26203; -.
DR   SMR; P13271; -.
DR   CORUM; P13271; -.
DR   DIP; DIP-38971N; -.
DR   IntAct; P13271; 2.
DR   STRING; 9913.ENSBTAP00000040860; -.
DR   PaxDb; 9913-ENSBTAP00000040860; -.
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; 1347677at2759; -.
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; Cytochrome b-c1 complex subunit 8; 1.
DR   InterPro; IPR004205; Cyt_bc1_su8.
DR   InterPro; IPR036642; Cyt_bc1_su8_sf.
DR   PANTHER; PTHR12119:SF2; CYTOCHROME B-C1 COMPLEX SUBUNIT 8; 1.
DR   PANTHER; PTHR12119; UBIQUINOL-CYTOCHROME C REDUCTASE COMPLEX UBIQUINONE-BINDING PROTEIN QP-C; 1.
DR   Pfam; PF02939; UcrQ; 1.
DR   SUPFAM; SSF81508; Ubiquinone-binding protein QP-C of cytochrome bc1 complex (Ubiquinol-cytochrome c reductase); 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
//