ID   QCR6_SCHPO              Reviewed;         214 AA.
AC   O42932;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=Cytochrome b-c1 complex subunit 6;
DE   AltName: Full=Complex III subunit 6;
DE   AltName: Full=Mitochondrial hinge protein;
DE   AltName: Full=Ubiquinol-cytochrome c reductase complex subunit 6;
GN   Name=qcr6; ORFNames=SPBC16C6.08c;
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:P00127}.
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:P00127}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000250|UniProtKB:P00127}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:P00127}; Intermembrane side
CC       {ECO:0000250|UniProtKB:P00127}.
CC   -!- SIMILARITY: Belongs to the UQCRH/QCR6 family. {ECO:0000305}.
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DR   EMBL; CU329671; CAA16921.1; -; Genomic_DNA.
DR   PIR; T39559; T39559.
DR   RefSeq; NP_596806.1; NM_001023827.2.
DR   AlphaFoldDB; O42932; -.
DR   SMR; O42932; -.
DR   BioGRID; 276677; 20.
DR   STRING; 4896.SPBC16C6.08c.1; -.
DR   iPTMnet; O42932; -.
DR   MaxQB; O42932; -.
DR   PaxDb; O42932; -.
DR   PRIDE; O42932; -.
DR   EnsemblFungi; SPBC16C6.08c.1; SPBC16C6.08c.1:pep; SPBC16C6.08c.
DR   PomBase; SPBC16C6.08c; qcr6.
DR   VEuPathDB; FungiDB:SPBC16C6.08c; -.
DR   eggNOG; KOG4763; Eukaryota.
DR   HOGENOM; CLU_1289608_0_0_1; -.
DR   InParanoid; O42932; -.
DR   OMA; CARDCAD; -.
DR   Reactome; R-SPO-611105; Respiratory electron transport.
DR   PRO; PR:O42932; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0005750; C:mitochondrial respiratory chain complex III; ISS:PomBase.
DR   GO; GO:0005739; C:mitochondrion; HDA:PomBase.
DR   GO; GO:0006122; P:mitochondrial electron transport, ubiquinol to cytochrome c; ISS:PomBase.
DR   GO; GO:1902600; P:proton transmembrane transport; IEA:GOC.
DR   Gene3D; 1.10.287.20; -; 1.
DR   InterPro; IPR023184; Ubol_cytC_Rdtase_hinge_dom.
DR   InterPro; IPR036811; Ubol_cytC_Rdtase_hinge_dom_sf.
DR   Pfam; PF02320; UCR_hinge; 1.
DR   SUPFAM; SSF81531; SSF81531; 1.
PE   3: Inferred from homology;
KW   Disulfide bond; Electron transport; Membrane; Mitochondrion;
KW   Mitochondrion inner membrane; Reference proteome; Respiratory chain;
KW   Transport.
FT   CHAIN           1..214
FT                   /note="Cytochrome b-c1 complex subunit 6"
FT                   /id="PRO_0000307212"
FT   REGION          25..157
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        36..69
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        80..124
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        125..149
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        157..204
FT                   /evidence="ECO:0000250|UniProtKB:P00126"
FT   DISULFID        173..190
FT                   /evidence="ECO:0000250|UniProtKB:P00127"
SQ   SEQUENCE   214 AA;  24308 MW;  C3840C91637DAA92 CRC64;
     MSFWKNLFTS AFTPISAEAD ELIKEDRKQF EENTPSKKNF ETQSPDEPSP KTTDSTGARD
     ANLSLKTQEP IVSADDAKGA QGKGADEKEE KKETIQPPEE VKTEPPQPEE KEGKEAKEPE
     EPPKEEAEEP QEGGEEEEEE EEEEEITDPL EKMTQECMDA PDCKEVKHHF EECTARVTKK
     VEQGDKSEDC IEEFFHLYHC ARDCADPKVF KVLV