ID   QCR7_FASHE              Reviewed;         130 AA.
AC   O01369; O02349;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 2.
DT   25-MAY-2022, entry version 81.
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=Ubiquinol-cytochrome c reductase complex 14 kDa protein;
GN   Name=UBCRBP;
OS   Fasciola hepatica (Liver fluke).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC   Digenea; Plagiorchiida; Echinostomata; Echinostomatoidea; Fasciolidae;
OC   Fasciola.
OX   NCBI_TaxID=6192;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9297698; DOI=10.1016/s0166-6851(97)00097-2;
RA   Davis R.E., Hodgson S.;
RT   "Gene linkage and steady state RNAs suggest trans-splicing may be
RT   associated with a polycistronic transcript in Schistosoma mansoni.";
RL   Mol. Biochem. Parasitol. 89:25-39(1997).
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 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:P00128}.
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}.
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DR   EMBL; U91748; AAC47730.1; -; Genomic_DNA.
DR   AlphaFoldDB; O01369; -.
DR   SMR; O01369; -.
DR   GO; GO:0005750; C:mitochondrial respiratory chain complex III; IEA:InterPro.
DR   GO; GO:0006122; P:mitochondrial electron transport, ubiquinol to cytochrome c; IEA:InterPro.
DR   Gene3D; 1.10.1090.10; -; 1.
DR   InterPro; IPR003197; QCR7.
DR   InterPro; IPR036544; QCR7_sf.
DR   PANTHER; PTHR12022; PTHR12022; 1.
DR   Pfam; PF02271; UCR_14kD; 1.
DR   SUPFAM; SSF81524; SSF81524; 1.
PE   3: Inferred from homology;
KW   Electron transport; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW   Respiratory chain; Transport.
FT   CHAIN           1..130
FT                   /note="Cytochrome b-c1 complex subunit 7"
FT                   /id="PRO_0000193528"
SQ   SEQUENCE   130 AA;  15331 MW;  55B4BCEB9F1333CE CRC64;
     MATLRASVER VASAYRMRLK QMTDLQQKVK AFQFSNSYYN QLGLLYHDVI PHSPLIAEAV
     RRLPREETEA RDFRIARAFQ LSASKTVLPK EQWTAIEDDI PYLDPYIEVA KKEWKEKAEW
     DHFVNPETYP