QCR2_CANAL
ID QCR2_CANAL Reviewed; 374 AA.
AC P83782; A0A1D8PNN7; Q59QS9;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-OCT-2011, sequence version 2.
DT 03-AUG-2022, entry version 76.
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=Cytoplasmic antigenic protein 5;
DE AltName: Full=Ubiquinol-cytochrome-c reductase complex core protein 2;
DE Flags: Precursor;
GN Name=QCR2; OrderedLocusNames=CAALFM_C503350WA;
GN ORFNames=CaO19.10167, CaO19.2644;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
RN [4]
RP PROTEIN SEQUENCE OF 221-231, AND ANTIGENICITY.
RC STRAIN=SC5314 / ATCC MYA-2876; TISSUE=Protoplast;
RX PubMed=15378761; DOI=10.1002/pmic.200400903;
RA Pitarch A., Abian J., Carrascal M., Sanchez M., Nombela C., Gil C.;
RT "Proteomics-based identification of novel Candida albicans antigens for
RT diagnosis of systemic candidiasis in patients with underlying hematological
RT malignancies.";
RL Proteomics 4:3084-3106(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 -!- MISCELLANEOUS: Has antigenic properties. Elicits a specific immune
CC response in systemic candidiasis human patients undergoing malignant
CC hematological disorders.
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; CP017627; AOW29749.1; -; Genomic_DNA.
DR RefSeq; XP_712027.1; XM_706934.1.
DR PDB; 7RJA; EM; 3.00 A; B/L=1-374.
DR PDB; 7RJB; EM; 3.20 A; B=1-374.
DR PDB; 7RJC; EM; 3.30 A; B=1-374.
DR PDB; 7RJD; EM; 3.20 A; B=1-374.
DR PDB; 7RJE; EM; 3.30 A; B/L=1-374.
DR PDBsum; 7RJA; -.
DR PDBsum; 7RJB; -.
DR PDBsum; 7RJC; -.
DR PDBsum; 7RJD; -.
DR PDBsum; 7RJE; -.
DR AlphaFoldDB; P83782; -.
DR SMR; P83782; -.
DR BioGRID; 1229424; 1.
DR STRING; 237561.P83782; -.
DR COMPLUYEAST-2DPAGE; P83782; -.
DR PRIDE; P83782; -.
DR GeneID; 3646352; -.
DR KEGG; cal:CAALFM_C503350WA; -.
DR CGD; CAL0000188005; QCR2.
DR VEuPathDB; FungiDB:C5_03350W_A; -.
DR eggNOG; KOG2583; Eukaryota.
DR HOGENOM; CLU_009902_0_1_1; -.
DR InParanoid; P83782; -.
DR OMA; YKYQDAG; -.
DR OrthoDB; 1000258at2759; -.
DR PRO; PR:P83782; -.
DR Proteomes; UP000000559; Chromosome 5.
DR GO; GO:0016020; C:membrane; IDA:CGD.
DR GO; GO:0030061; C:mitochondrial crista; IEA:EnsemblFungi.
DR GO; GO:0005750; C:mitochondrial respiratory chain complex III; IEA:EnsemblFungi.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:CGD.
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 InterPro; IPR007863; Peptidase_M16_C.
DR Pfam; PF00675; Peptidase_M16; 1.
DR Pfam; PF05193; Peptidase_M16_C; 1.
DR SUPFAM; SSF63411; SSF63411; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Electron transport; Membrane;
KW Mitochondrion; Mitochondrion inner membrane; Reference proteome;
KW Respiratory chain; Transit peptide; Transport.
FT TRANSIT 1..11
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 12..374
FT /note="Cytochrome b-c1 complex subunit 2, mitochondrial"
FT /id="PRO_0000089305"
FT STRAND 18..22
FT /evidence="ECO:0007829|PDB:7RJA"
FT STRAND 27..29
FT /evidence="ECO:0007829|PDB:7RJA"
FT STRAND 32..35
FT /evidence="ECO:0007829|PDB:7RJA"
FT TURN 40..42
FT /evidence="ECO:0007829|PDB:7RJA"
FT HELIX 47..54
FT /evidence="ECO:0007829|PDB:7RJA"
FT TURN 55..57
FT /evidence="ECO:0007829|PDB:7RJB"
FT STRAND 60..62
FT /evidence="ECO:0007829|PDB:7RJE"
FT HELIX 64..74
FT /evidence="ECO:0007829|PDB:7RJA"
FT STRAND 77..82
FT /evidence="ECO:0007829|PDB:7RJA"
FT STRAND 87..94
FT /evidence="ECO:0007829|PDB:7RJA"
FT HELIX 95..97
FT /evidence="ECO:0007829|PDB:7RJA"
FT HELIX 98..109
FT /evidence="ECO:0007829|PDB:7RJA"
FT HELIX 116..121
FT /evidence="ECO:0007829|PDB:7RJA"
FT HELIX 124..135
FT /evidence="ECO:0007829|PDB:7RJA"
FT HELIX 138..150
FT /evidence="ECO:0007829|PDB:7RJA"
FT STRAND 151..153
FT /evidence="ECO:0007829|PDB:7RJE"
FT HELIX 154..156
FT /evidence="ECO:0007829|PDB:7RJA"
FT HELIX 169..176
FT /evidence="ECO:0007829|PDB:7RJA"
FT HELIX 182..184
FT /evidence="ECO:0007829|PDB:7RJA"
FT STRAND 185..192
FT /evidence="ECO:0007829|PDB:7RJA"
FT HELIX 194..203
FT /evidence="ECO:0007829|PDB:7RJA"
FT HELIX 205..208
FT /evidence="ECO:0007829|PDB:7RJA"
FT STRAND 229..233
FT /evidence="ECO:0007829|PDB:7RJA"
FT STRAND 235..246
FT /evidence="ECO:0007829|PDB:7RJA"
FT HELIX 248..250
FT /evidence="ECO:0007829|PDB:7RJA"
FT HELIX 251..261
FT /evidence="ECO:0007829|PDB:7RJA"
FT STRAND 269..271
FT /evidence="ECO:0007829|PDB:7RJA"
FT HELIX 272..275
FT /evidence="ECO:0007829|PDB:7RJA"
FT STRAND 280..285
FT /evidence="ECO:0007829|PDB:7RJA"
FT STRAND 290..299
FT /evidence="ECO:0007829|PDB:7RJA"
FT HELIX 300..314
FT /evidence="ECO:0007829|PDB:7RJA"
FT HELIX 319..324
FT /evidence="ECO:0007829|PDB:7RJA"
FT HELIX 326..336
FT /evidence="ECO:0007829|PDB:7RJA"
FT STRAND 339..341
FT /evidence="ECO:0007829|PDB:7RJA"
FT STRAND 358..363
FT /evidence="ECO:0007829|PDB:7RJA"
FT TURN 365..367
FT /evidence="ECO:0007829|PDB:7RJA"
FT HELIX 371..373
FT /evidence="ECO:0007829|PDB:7RJA"
SQ SEQUENCE 374 AA; 39558 MW; 47018DF7D1968EC1 CRC64;
MLSRASIRAY SSIPNSVKIA AKESATDLTK LSVIINNAGS KTGKSGVSHL LSKFTFLNNG
AKSALRFTRE SELLGGTFES KVTRDALILN TTFLKQDLPY YVEALGNVVS NTQFAPHEFN
EIVLPTANAE TKLANANPAF KGVEKLHEIT FRRGLGNPLF YNESTPIKLE EVAQFSKEQF
SGENISIVAE GANEEDLTKF VSESAFCYLP SSSSNGAKAL PTNTFTGQEA RVPSSGASSA
LIGIPVKPAD FGKYEVLSAA IGTSTLPSTS TPLAQIPGAT SHLYKYQDAG LFVISVSGEA
SQVAQGIKQA KSVAESVSSS ALSEAVKAAE LSVALQSTVD SPLNVKVVAE EAPISKFNYV
AVGDLDVLPY ADEL
