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QCR7_KLULA
ID   QCR7_KLULA              Reviewed;         127 AA.
AC   P49345;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   25-MAY-2022, entry version 122.
DE   RecName: Full=Cytochrome b-c1 complex subunit 7;
DE   AltName: Full=Complex III subunit 7;
DE   AltName: Full=Complex III subunit VII;
DE   AltName: Full=Ubiquinol-cytochrome c reductase complex 14 kDa protein;
GN   Name=QCR7; OrderedLocusNames=KLLA0C00825g;
OS   Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS   NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX   NCBI_TaxID=284590;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX   PubMed=7948033; DOI=10.1016/0167-4781(94)90235-6;
RA   Mulder W., Scholten I.H.J.M., van Roon H., Grivell L.A.;
RT   "Isolation and characterisation of the linked genes APA2 and QCR7, coding
RT   for Ap4A phosphorylase II and the 14 kDa subunit VII of the mitochondrial
RT   bc1-complex in the yeast Kluyveromyces lactis.";
RL   Biochim. Biophys. Acta 1219:719-723(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
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:P00128}.
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:P00128}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000250|UniProtKB:P00128}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:P00128}; Matrix side
CC       {ECO:0000250|UniProtKB:P00128}.
CC   -!- SIMILARITY: Belongs to the UQCRB/QCR7 family. {ECO:0000305}.
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DR   EMBL; X76027; CAA53617.1; -; Genomic_DNA.
DR   EMBL; CR382123; CAH01082.1; -; Genomic_DNA.
DR   PIR; S50213; S50213.
DR   RefSeq; XP_452231.1; XM_452231.1.
DR   AlphaFoldDB; P49345; -.
DR   SMR; P49345; -.
DR   STRING; 28985.XP_452231.1; -.
DR   EnsemblFungi; CAH01082; CAH01082; KLLA0_C00825g.
DR   GeneID; 2892603; -.
DR   KEGG; kla:KLLA0_C00825g; -.
DR   eggNOG; KOG3440; Eukaryota.
DR   HOGENOM; CLU_115154_1_0_1; -.
DR   InParanoid; P49345; -.
DR   OMA; FDEDVHY; -.
DR   Proteomes; UP000000598; Chromosome C.
DR   GO; GO:0099617; C:matrix side of mitochondrial inner membrane; IEA:EnsemblFungi.
DR   GO; GO:0005750; C:mitochondrial respiratory chain complex III; IEA:EnsemblFungi.
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   GO; GO:0034551; P:mitochondrial respiratory chain complex III assembly; IEA:EnsemblFungi.
DR   Gene3D; 1.10.1090.10; -; 1.
DR   InterPro; IPR003197; QCR7.
DR   InterPro; IPR036544; QCR7_sf.
DR   PANTHER; PTHR12022; PTHR12022; 1.
DR   Pfam; PF02271; UCR_14kD; 1.
DR   PIRSF; PIRSF000022; Bc1_14K; 1.
DR   SUPFAM; SSF81524; SSF81524; 1.
PE   3: Inferred from homology;
KW   Electron transport; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW   Reference proteome; Respiratory chain; Transport.
FT   CHAIN           1..127
FT                   /note="Cytochrome b-c1 complex subunit 7"
FT                   /id="PRO_0000193534"
SQ   SEQUENCE   127 AA;  14663 MW;  7195CD85B3418876 CRC64;
     MPQTFTSIAK IGDYILRTPA LAKVVVPIAH QFINLSGYRK MGLRFDDLIE EENELAQTAL
     RRLPADESYA RIYRIINAHQ LSLSHHLLPK DKWTKPEDDI PYLTPYLLEA EAFVKEKEEL
     DNLEVAK
 
 
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