QCR9_BOVIN
ID QCR9_BOVIN Reviewed; 64 AA.
AC P00130; Q3SZT3;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Cytochrome b-c1 complex subunit 9;
DE AltName: Full=Complex III subunit 9;
DE AltName: Full=Complex III subunit X;
DE AltName: Full=Cytochrome c1 non-heme 7 kDa protein;
DE AltName: Full=Ubiquinol-cytochrome c reductase complex 7.2 kDa protein;
GN Name=UQCR10;
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 2-63.
RC TISSUE=Heart;
RX PubMed=6305819;
RA Schaegger H., von Jagow G., Borchart U., Machleidt W.;
RT "Amino-acid sequence of the smallest protein of the cytochrome c1
RT subcomplex from beef heart mitochondria.";
RL Hoppe-Seyler's Z. Physiol. Chem. 364:307-311(1983).
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:P22289}.
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 (PubMed:9651245). The complex is composed of 3
CC respiratory subunits cytochrome b, cytochrome c1 and Rieske protein
CC UQCRFS1, 2 core protein subunits UQCRC1/QCR1 and UQCRC2/QCR2, and 6
CC low-molecular weight protein subunits UQCRH/QCR6, UQCRB/QCR7,
CC UQCRQ/QCR8, UQCR10/QCR9, UQCR11/QCR10 and subunit 9, the cleavage
CC product of Rieske protein UQCRFS1 (PubMed:9651245). The complex exists
CC as an obligatory dimer and forms supercomplexes (SCs) in the inner
CC mitochondrial membrane with NADH-ubiquinone oxidoreductase (complex I,
CC CI) and 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 STMP1 (By
CC similarity). {ECO:0000250|UniProtKB:Q8R1I1,
CC ECO:0000269|PubMed:27830641, ECO:0000269|PubMed:9651245}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:P22289}; Single-pass membrane protein
CC {ECO:0000250|UniProtKB:P22289}.
CC -!- SIMILARITY: Belongs to the UQCR10/QCR9 family. {ECO:0000305}.
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DR EMBL; BC102720; AAI02721.1; -; mRNA.
DR PIR; A00123; CCBO17.
DR RefSeq; NP_001107195.1; NM_001113723.2.
DR PDB; 1BCC; X-ray; 3.16 A; J=2-63.
DR PDB; 1BE3; X-ray; 3.00 A; J=2-63.
DR PDB; 1BGY; X-ray; 3.00 A; J/V=2-63.
DR PDB; 1L0L; X-ray; 2.35 A; J=2-63.
DR PDB; 1L0N; X-ray; 2.60 A; J=2-63.
DR PDB; 1NTK; X-ray; 2.60 A; J=2-63.
DR PDB; 1NTM; X-ray; 2.40 A; J=2-63.
DR PDB; 1NTZ; X-ray; 2.60 A; J=2-63.
DR PDB; 1NU1; X-ray; 3.20 A; J=2-63.
DR PDB; 1PP9; X-ray; 2.10 A; J/W=2-63.
DR PDB; 1PPJ; X-ray; 2.10 A; J/W=2-63.
DR PDB; 1QCR; X-ray; 2.70 A; J=5-63.
DR PDB; 1SQB; X-ray; 2.69 A; J=2-63.
DR PDB; 1SQP; X-ray; 2.70 A; J=2-63.
DR PDB; 1SQQ; X-ray; 3.00 A; J=2-63.
DR PDB; 1SQV; X-ray; 2.85 A; J=2-63.
DR PDB; 1SQX; X-ray; 2.60 A; J=2-63.
DR PDB; 2A06; X-ray; 2.10 A; J/W=2-63.
DR PDB; 2BCC; X-ray; 3.50 A; J=2-63.
DR PDB; 2FYU; X-ray; 2.26 A; J=2-63.
DR PDB; 2YBB; EM; 19.00 A; J/j=2-63.
DR PDB; 3BCC; X-ray; 3.70 A; J=2-63.
DR PDB; 4D6T; X-ray; 3.57 A; J/W=1-64.
DR PDB; 4D6U; X-ray; 4.09 A; J/W=1-64.
DR PDB; 5GPN; EM; 5.40 A; J/L=2-63.
DR PDB; 5KLV; X-ray; 2.65 A; J=2-64.
DR PDB; 5LUF; EM; 9.10 A; j/v=2-63.
DR PDB; 5NMI; X-ray; 3.50 A; J/W=1-64.
DR PDB; 5OKD; X-ray; 3.10 A; J=1-64.
DR PDB; 6FO0; EM; 4.10 A; J/W=1-64.
DR PDB; 6FO2; EM; 4.40 A; J/W=1-64.
DR PDB; 6FO6; EM; 4.10 A; J/W=1-64.
DR PDB; 6HAW; X-ray; 3.45 A; J=3-61.
DR PDB; 6NHG; X-ray; 2.80 A; J=2-64.
DR PDB; 6XVF; X-ray; 3.50 A; J=3-61.
DR PDB; 6ZFS; X-ray; 3.50 A; J=3-61.
DR PDB; 6ZFT; X-ray; 3.30 A; J=3-61.
DR PDB; 6ZFU; X-ray; 3.50 A; J=3-61.
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; P00130; -.
DR SMR; P00130; -.
DR CORUM; P00130; -.
DR DIP; DIP-38972N; -.
DR IntAct; P00130; 3.
DR STRING; 9913.ENSBTAP00000001208; -.
DR PaxDb; P00130; -.
DR PRIDE; P00130; -.
DR Ensembl; ENSBTAT00000001208; ENSBTAP00000001208; ENSBTAG00000000913.
DR GeneID; 616109; -.
DR KEGG; bta:616109; -.
DR CTD; 29796; -.
DR VEuPathDB; HostDB:ENSBTAG00000000913; -.
DR VGNC; VGNC:36693; UQCR10.
DR eggNOG; KOG3494; Eukaryota.
DR GeneTree; ENSGT00390000014052; -.
DR HOGENOM; CLU_171977_2_0_1; -.
DR InParanoid; P00130; -.
DR OMA; DIKHRYI; -.
DR OrthoDB; 1624769at2759; -.
DR TreeFam; TF324385; -.
DR EvolutionaryTrace; P00130; -.
DR Proteomes; UP000009136; Chromosome 17.
DR Bgee; ENSBTAG00000000913; Expressed in cardiac ventricle and 106 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; 1.20.5.260; -; 1.
DR InterPro; IPR008027; QCR9.
DR InterPro; IPR036656; QCR9_sf.
DR PANTHER; PTHR12980; PTHR12980; 1.
DR Pfam; PF05365; UCR_UQCRX_QCR9; 1.
DR SUPFAM; SSF81514; SSF81514; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Electron transport; Membrane;
KW 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:6305819"
FT CHAIN 2..64
FT /note="Cytochrome b-c1 complex subunit 9"
FT /id="PRO_0000193552"
FT TOPO_DOM 2..21
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000269|PubMed:9651245"
FT TRANSMEM 22..47
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:9651245"
FT TOPO_DOM 48..64
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000269|PubMed:9651245"
FT HELIX 6..13
FT /evidence="ECO:0007829|PDB:1PP9"
FT STRAND 15..17
FT /evidence="ECO:0007829|PDB:5NMI"
FT HELIX 18..47
FT /evidence="ECO:0007829|PDB:1PP9"
FT TURN 48..51
FT /evidence="ECO:0007829|PDB:1PP9"
FT HELIX 53..56
FT /evidence="ECO:0007829|PDB:1PP9"
FT HELIX 57..59
FT /evidence="ECO:0007829|PDB:1PP9"
SQ SEQUENCE 64 AA; 7458 MW; D48CDB1344504049 CRC64;
MVAPTLTARL YSLLFRRTST FALTIVVGAL FFERAFDQGA DAIYEHINEG KLWKHIKHKY
ENKE
