QCR9_SCHPO
ID QCR9_SCHPO Reviewed; 67 AA.
AC O74433;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 25-MAY-2022, entry version 132.
DE RecName: Full=Cytochrome b-c1 complex subunit 9;
DE AltName: Full=Complex III subunit 9;
DE AltName: Full=Cytochrome c1 non-heme 7.3 kDa protein;
DE AltName: Full=Ubiquinol-cytochrome c reductase complex 7.3 kDa protein;
GN Name=qcr9; ORFNames=SPCC1682.01;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
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 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:P22289}.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA20667.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CU329672; CAA20667.1; ALT_INIT; Genomic_DNA.
DR PIR; T41058; T41058.
DR RefSeq; NP_587794.3; NM_001022787.3.
DR AlphaFoldDB; O74433; -.
DR SMR; O74433; -.
DR STRING; 4896.SPCC1682.01.1; -.
DR MaxQB; O74433; -.
DR PaxDb; O74433; -.
DR PRIDE; O74433; -.
DR GeneID; 2539153; -.
DR KEGG; spo:SPCC1682.01; -.
DR PomBase; SPCC1682.01; qcr9.
DR eggNOG; KOG3494; Eukaryota.
DR InParanoid; O74433; -.
DR PhylomeDB; O74433; -.
DR Reactome; R-SPO-611105; Respiratory electron transport.
DR PRO; PR:O74433; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0005750; C:mitochondrial respiratory chain complex III; ISO:PomBase.
DR GO; GO:0005739; C:mitochondrion; HDA:PomBase.
DR GO; GO:0006122; P:mitochondrial electron transport, ubiquinol to cytochrome c; ISO:PomBase.
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 3: Inferred from homology;
KW Electron transport; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW Reference proteome; Respiratory chain; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..67
FT /note="Cytochrome b-c1 complex subunit 9"
FT /id="PRO_0000193557"
FT TOPO_DOM 1..17
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000250|UniProtKB:P22289"
FT TRANSMEM 18..43
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P22289"
FT TOPO_DOM 44..67
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000250|UniProtKB:P22289"
SQ SEQUENCE 67 AA; 7800 MW; E5D5BD3F2E6F155E CRC64;
MASSTIYNIF FRRNSSFYAT IFVSAFFAKI GFDVFTDSVW KRANAGLTWD EVKPRFLNKD
EDAEDDE
