ID   QCR7_CYBJA              Reviewed;         126 AA.
AC   P46268;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   25-MAY-2022, entry version 83.
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=QCR7;
OS   Cyberlindnera jadinii (Torula yeast) (Pichia jadinii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Phaffomycetaceae; Cyberlindnera.
OX   NCBI_TaxID=4903;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 22023 / CBS 621 / JCM 9624 / NBRC 10707 / NCYC 769 / NRRL
RC   Y-7586 / VKM Y-74;
RX   PubMed=7615060; DOI=10.1016/0014-5793(95)00611-c;
RA   Boumans H., Berden J.A., Grivell L.A.;
RT   "Identification of additional homologues of subunits VII and VIII of the
RT   ubiquinol-cytochrome c oxidoreductase enables definition of consensus
RT   sequences.";
RL   FEBS Lett. 368:105-109(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. {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}.
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DR   EMBL; U20215; AAA86879.1; -; Genomic_DNA.
DR   PIR; S66280; S66280.
DR   AlphaFoldDB; P46268; -.
DR   SMR; P46268; -.
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   PIRSF; PIRSF000022; Bc1_14K; 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..126
FT                   /note="Cytochrome b-c1 complex subunit 7"
FT                   /id="PRO_0000193536"
SQ   SEQUENCE   126 AA;  14129 MW;  A7C254937F82C56F CRC64;
     MASHTSIVKA GDFILRTPVL RSIFVPAAKL FCAYSGYRQL GLKFDDLIHE ENPTVQKALS
     RLPKDEIYAR NFRMLTAAQC GITHHLLSAD KALKPSEDTP YLLPYLLELE AEAAERVELD
     NVEVAK