QCR2_CANGA
ID QCR2_CANGA Reviewed; 364 AA.
AC Q6FSJ3;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 93.
DE RecName: Full=Cytochrome b-c1 complex subunit 2, mitochondrial;
DE AltName: Full=Complex III subunit 2;
DE AltName: Full=Core protein II;
DE AltName: Full=Ubiquinol-cytochrome-c reductase complex core protein 2;
DE Flags: Precursor;
GN Name=QCR2; OrderedLocusNames=CAGL0G10131g;
OS Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS Y-65) (Yeast) (Torulopsis glabrata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC Nakaseomyces/Candida clade.
OX NCBI_TaxID=284593;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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:P07257}.
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:P07257}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:P07257}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P07257}; Matrix side
CC {ECO:0000250|UniProtKB:P07257}.
CC -!- SIMILARITY: Belongs to the peptidase M16 family. UQCRC2/QCR2 subfamily.
CC {ECO:0000305}.
CC -!- CAUTION: Does not seem to have a protease activity as it lack the zinc-
CC binding site. {ECO:0000305}.
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DR EMBL; CR380953; CAG59728.1; -; Genomic_DNA.
DR RefSeq; XP_446801.1; XM_446801.1.
DR AlphaFoldDB; Q6FSJ3; -.
DR SMR; Q6FSJ3; -.
DR STRING; 5478.XP_446801.1; -.
DR EnsemblFungi; CAG59728; CAG59728; CAGL0G10131g.
DR GeneID; 2887999; -.
DR KEGG; cgr:CAGL0G10131g; -.
DR CGD; CAL0130835; CAGL0G10131g.
DR VEuPathDB; FungiDB:CAGL0G10131g; -.
DR eggNOG; KOG2583; Eukaryota.
DR HOGENOM; CLU_009902_0_1_1; -.
DR InParanoid; Q6FSJ3; -.
DR Proteomes; UP000002428; Chromosome G.
DR GO; GO:0030061; C:mitochondrial crista; IEA:EnsemblFungi.
DR GO; GO:0005750; C:mitochondrial respiratory chain complex III; IEA:EnsemblFungi.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0008121; F:ubiquinol-cytochrome-c reductase activity; IEA:EnsemblFungi.
DR GO; GO:0006122; P:mitochondrial electron transport, ubiquinol to cytochrome c; IEA:EnsemblFungi.
DR InterPro; IPR011249; Metalloenz_LuxS/M16.
DR InterPro; IPR011765; Pept_M16_N.
DR Pfam; PF00675; Peptidase_M16; 1.
DR SUPFAM; SSF63411; SSF63411; 2.
PE 3: Inferred from homology;
KW Electron transport; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW Reference proteome; Respiratory chain; Transit peptide; Transport.
FT TRANSIT 1..15
FT /note="Mitochondrion"
FT /evidence="ECO:0000250"
FT CHAIN 16..364
FT /note="Cytochrome b-c1 complex subunit 2, mitochondrial"
FT /id="PRO_0000026795"
SQ SEQUENCE 364 AA; 40335 MW; 831D04A35145DA24 CRC64;
MLSRGQLLRS SARHYSIVTK DLPGNLSVLR VKVHAGSRYA NKDGIAHLLS RFNFQNTNTK
SALRLVRESE LLGGCTKSTV DREYITLEAR FLKENLPYYV NALSNVLYKT SFRPHELPES
VIPAAKYDLA VADSNPIFQA EDLLYNISFR NGLGNPVLYD SVEKVSIDDL KEFSSKVYTK
ENIEIEGVGI NEADLKKFVT ESLFNSLPQG SNLASSAKSE IFTGKESRLR RIGESVASVG
IPVASKDFGK FQALEAYLSS ELFPLTDLLS EVKFTKYPDV GFLTFSVKNG DATVVSENIK
KVVGELKKSQ DISKATELAK LKLGTETSSP VDIKFDGVKD FKLDDKFNFA AVGDVSKLPF
RDQL
