QCR2_SCHPO
ID QCR2_SCHPO Reviewed; 426 AA.
AC P78761;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1999, sequence version 2.
DT 03-AUG-2022, entry version 142.
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; ORFNames=SPCC613.10;
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 71-426.
RC STRAIN=PR745;
RX PubMed=9501991; DOI=10.1093/dnares/4.6.363;
RA Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H.;
RT "Identification of open reading frames in Schizosaccharomyces pombe
RT cDNAs.";
RL DNA Res. 4:363-369(1997).
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; CU329672; CAA21062.1; -; Genomic_DNA.
DR EMBL; D89109; BAA13772.1; -; mRNA.
DR PIR; T41476; T41476.
DR PIR; T42086; T42086.
DR RefSeq; NP_587698.1; NM_001022693.2.
DR AlphaFoldDB; P78761; -.
DR SMR; P78761; -.
DR BioGRID; 275557; 1.
DR STRING; 4896.SPCC613.10.1; -.
DR iPTMnet; P78761; -.
DR MaxQB; P78761; -.
DR PaxDb; P78761; -.
DR PRIDE; P78761; -.
DR EnsemblFungi; SPCC613.10.1; SPCC613.10.1:pep; SPCC613.10.
DR GeneID; 2538983; -.
DR KEGG; spo:SPCC613.10; -.
DR PomBase; SPCC613.10; qcr2.
DR VEuPathDB; FungiDB:SPCC613.10; -.
DR eggNOG; KOG2583; Eukaryota.
DR HOGENOM; CLU_009902_0_1_1; -.
DR InParanoid; P78761; -.
DR OMA; WVGEFFT; -.
DR PhylomeDB; P78761; -.
DR PRO; PR:P78761; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0005750; C:mitochondrial respiratory chain complex III; ISS:PomBase.
DR GO; GO:0005739; C:mitochondrion; HDA:PomBase.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0005198; F:structural molecule activity; ISS: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 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 2: Evidence at transcript level;
KW Electron transport; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW Reference proteome; Respiratory chain; Transit peptide; Transport.
FT TRANSIT 1..30
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 31..426
FT /note="Cytochrome b-c1 complex subunit 2, mitochondrial"
FT /id="PRO_0000026799"
SQ SEQUENCE 426 AA; 45651 MW; 3D91428A27240A2C CRC64;
MKSFTRNLRR FQTPRRNLHG ISYTPKKVEG VSFAGRETPT ATGSLSVVIN AGSRYQPDAG
VSHLLEKFAF KTTEERSALR ITRESELLGG QLSTQITREH IILTARFLNE YLEYYARLLA
EVVDATKFLP FQLTEEVLPT ARIESELFRE DILRVAMAKL HEKAFHRGIG NEVYLPASAS
PSISEIKDFA SKAYVKSNFS VISSGPDVQK ASDLCAKYFA VIPDGSPLKS APTKISSGES
RVYSKGTNYF CLGFPAPAAS PELFVLSSIL GGDAAVKWSH GNTLLAKAAG TASEYKATAV
ADLTPYSDAS LLSVVISGSC PKAIKATASE SFKALKSLSS NIPNDVVKSG IAMAKTKYLS
AFEPVTLNAI SASSLVSASK GSDAFISGFD KVTPASISKV VSSLLAKPAS TVAVGNLDVL
PYYDEL
