QCR8_AILME
ID QCR8_AILME Reviewed; 82 AA.
AC Q2L897;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 25-MAY-2022, entry version 81.
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 Ailuropoda melanoleuca (Giant panda).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ailuropoda.
OX NCBI_TaxID=9646;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Hou W., Peng Z., Chen Y., Wu X., Tang Z.;
RT "cDNA cloning and sequence analysis of ubiquinol-cytochrome c reductase
RT complex ubiquinone-binding protein (QP-C) from giant panda.";
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
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 (By similarity). 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)) (By similarity). Interacts with BRAWNIN (By
CC similarity). {ECO:0000250|UniProtKB:O14949,
CC ECO:0000250|UniProtKB:P13271, ECO:0000250|UniProtKB:Q9CQ69}.
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; DQ349120; ABC72132.1; -; mRNA.
DR RefSeq; XP_002912950.1; XM_002912904.3.
DR AlphaFoldDB; Q2L897; -.
DR SMR; Q2L897; -.
DR STRING; 9646.ENSAMEP00000018758; -.
DR PRIDE; Q2L897; -.
DR Ensembl; ENSAMET00000019510; ENSAMEP00000018758; ENSAMEG00000017762.
DR GeneID; 100483229; -.
DR KEGG; aml:100483229; -.
DR CTD; 27089; -.
DR eggNOG; KOG4116; Eukaryota.
DR GeneTree; ENSGT00390000004029; -.
DR HOGENOM; CLU_156007_2_0_1; -.
DR InParanoid; Q2L897; -.
DR OMA; SWGTQEF; -.
DR OrthoDB; 1523793at2759; -.
DR TreeFam; TF300281; -.
DR Proteomes; UP000008912; Unassembled WGS sequence.
DR GO; GO:0005750; C:mitochondrial respiratory chain complex III; IEA:Ensembl.
DR GO; GO:0021680; P:cerebellar Purkinje cell layer development; IEA:Ensembl.
DR GO; GO:0021766; P:hippocampus development; IEA:Ensembl.
DR GO; GO:0021854; P:hypothalamus development; IEA:Ensembl.
DR GO; GO:0030901; P:midbrain development; IEA:Ensembl.
DR GO; GO:0006122; P:mitochondrial electron transport, ubiquinol to cytochrome c; IEA:InterPro.
DR GO; GO:0021548; P:pons development; IEA:Ensembl.
DR GO; GO:0021860; P:pyramidal neuron development; IEA:Ensembl.
DR GO; GO:0021539; P:subthalamus development; IEA:Ensembl.
DR GO; GO:0021794; P:thalamus development; IEA:Ensembl.
DR Gene3D; 1.20.5.210; -; 1.
DR InterPro; IPR004205; Cyt_bc1_su8.
DR InterPro; IPR036642; Cyt_bc1_su8_sf.
DR PANTHER; PTHR12119; PTHR12119; 1.
DR Pfam; PF02939; UcrQ; 1.
DR SUPFAM; SSF81508; SSF81508; 1.
PE 3: Inferred from homology;
KW Acetylation; Electron transport; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Reference proteome; Respiratory chain;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..82
FT /note="Cytochrome b-c1 complex subunit 8"
FT /id="PRO_0000253746"
FT TOPO_DOM 1..39
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000250|UniProtKB:P13271"
FT TRANSMEM 40..68
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P13271"
FT TOPO_DOM 69..82
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000250|UniProtKB:P13271"
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"
SQ SEQUENCE 82 AA; 9732 MW; E485EA6AACC903B2 CRC64;
MGREFGNLTR MRHVITYSLS PFEQRAFPHY FSKGIPNVLR RMRACVLRVV PPFVAFYLVY
TWGTQEFENS KRKNPAAYEN DK
