ID   UCR11_SOLTU             Reviewed;          62 AA.
AC   P48505;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 74.
DE   RecName: Full=Ubiquinol-cytochrome c reductase complex 6.7 kDa protein;
DE            Short=CR6;
OS   Solanum tuberosum (Potato).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum.
OX   NCBI_TaxID=4113;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 2-50.
RC   TISSUE=Tuber;
RX   PubMed=7737189; DOI=10.1111/j.1432-1033.1995.0878m.x;
RA   Jaensch L., Kruft V., Schmitz U.K., Braun H.-P.;
RT   "Cytochrome c reductase from potato does not comprise three core proteins
RT   but contains an additional low-molecular-mass subunit.";
RL   Eur. J. Biochem. 228:878-885(1995).
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. QCR10 has a role in CIII assembly and RIP1
CC       stability. {ECO:0000250|UniProtKB:P37299}.
CC   -!- SUBUNIT: Component of the ubiquinol-cytochrome c oxidoreductase
CC       (cytochrome b-c1 complex, complex III, CIII), a multisubunit enzyme
CC       composed of 3 respiratory subunits cytochrome b, cytochrome c1 and
CC       Rieske protein, 2 core protein subunits, and additional low-molecular
CC       weight protein subunits. The complex exists as an obligatory dimer and
CC       forms supercomplexes (SCs) in the inner mitochondrial membrane with
CC       cytochrome c oxidase (complex IV, CIV). {ECO:0000250|UniProtKB:P37299}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000250|UniProtKB:P37299}; Single-pass membrane protein
CC       {ECO:0000250|UniProtKB:P37299}.
CC   -!- SIMILARITY: Belongs to the UQCR11/QCR10 family. {ECO:0000305}.
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DR   EMBL; X82325; CAA57768.1; -; mRNA.
DR   PIR; S68969; S68969.
DR   AlphaFoldDB; P48505; -.
DR   SMR; P48505; -.
DR   STRING; 4113.PGSC0003DMT400053106; -.
DR   eggNOG; ENOG502S99R; Eukaryota.
DR   Proteomes; UP000011115; Unassembled WGS sequence.
DR   ExpressionAtlas; P48505; baseline.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0070469; C:respirasome; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Electron transport; Membrane; Mitochondrion;
KW   Mitochondrion inner membrane; Reference proteome; Respiratory chain;
KW   Transmembrane; Transmembrane helix; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:7737189"
FT   CHAIN           2..62
FT                   /note="Ubiquinol-cytochrome c reductase complex 6.7 kDa
FT                   protein"
FT                   /id="PRO_0000193562"
FT   TOPO_DOM        2..25
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000250|UniProtKB:P37299"
FT   TRANSMEM        26..44
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        45..62
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000250|UniProtKB:P37299"
SQ   SEQUENCE   62 AA;  6874 MW;  A08C15EB08F92201 CRC64;
     MTSPAAAGNG LFKFLRPKLR PQSTDIQAAA GWGVAAVTGA LWVIQPWDFL RKTFIEKQEE
     EK