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   27-MAR-2024, entry version 178.
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   PDB; 7DGQ; EM; 5.00 A; A2/q=1-111.
DR   PDB; 7DGR; EM; 4.60 A; A1/q=1-111.
DR   PDB; 7DGS; EM; 7.80 A; A1/q=1-111.
DR   PDB; 7DKF; EM; 8.30 A; F1/R1=1-111.
DR   PDB; 7R3V; X-ray; 3.20 A; F=12-110.
DR   PDB; 7TAY; X-ray; 2.95 A; F=2-111.
DR   PDB; 7TZ6; EM; 2.88 A; F/S=2-111.
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   PDBsum; 7DGQ; -.
DR   PDBsum; 7DGR; -.
DR   PDBsum; 7DGS; -.
DR   PDBsum; 7DKF; -.
DR   PDBsum; 7R3V; -.
DR   PDBsum; 7TAY; -.
DR   PDBsum; 7TZ6; -.
DR   AlphaFoldDB; P00129; -.
DR   EMDB; EMD-26203; -.
DR   SMR; P00129; -.
DR   CORUM; P00129; -.
DR   DIP; DIP-1082N; -.
DR   IntAct; P00129; 3.
DR   STRING; 9913.ENSBTAP00000001993; -.
DR   iPTMnet; P00129; -.
DR   PaxDb; 9913-ENSBTAP00000001993; -.
DR   Ensembl; ENSBTAT00000001993.3; ENSBTAP00000001993.2; ENSBTAG00000001521.3.
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; YRFITAH; -.
DR   OrthoDB; 5477553at2759; -.
DR   TreeFam; TF105035; -.
DR   Reactome; R-BTA-611105; Respiratory electron transport.
DR   EvolutionaryTrace; P00129; -.
DR   Proteomes; UP000009136; Chromosome 14.
DR   Bgee; ENSBTAG00000001521; Expressed in cardiac ventricle and 105 other cell types or 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; Cytochrome b-c1 complex subunit 7; 1.
DR   InterPro; IPR003197; QCR7.
DR   InterPro; IPR036544; QCR7_sf.
DR   PANTHER; PTHR12022:SF0; CYTOCHROME B-C1 COMPLEX SUBUNIT 7; 1.
DR   PANTHER; PTHR12022; UBIQUINOL-CYTOCHROME C REDUCTASE COMPLEX 14 KD PROTEIN; 1.
DR   Pfam; PF02271; UCR_14kD; 1.
DR   PIRSF; PIRSF000022; Bc1_14K; 1.
DR   SUPFAM; SSF81524; 14 kDa protein 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; 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
//