位置:首页 > 蛋白库 > QCR2_YARLI
QCR2_YARLI
ID   QCR2_YARLI              Reviewed;         417 AA.
AC   Q6C2E3;
DT   27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 100.
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=YALI0F08613g;
OS   Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Dipodascaceae; Yarrowia.
OX   NCBI_TaxID=284591;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CLIB 122 / E 150;
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CR382132; CAG77976.1; -; Genomic_DNA.
DR   RefSeq; XP_505169.1; XM_505169.1.
DR   AlphaFoldDB; Q6C2E3; -.
DR   SMR; Q6C2E3; -.
DR   STRING; 4952.CAG77976; -.
DR   EnsemblFungi; CAG77976; CAG77976; YALI0_F08613g.
DR   GeneID; 2908481; -.
DR   KEGG; yli:YALI0F08613g; -.
DR   VEuPathDB; FungiDB:YALI0_F08613g; -.
DR   HOGENOM; CLU_009902_0_1_1; -.
DR   InParanoid; Q6C2E3; -.
DR   OMA; WVGEFFT; -.
DR   Proteomes; UP000001300; Chromosome F.
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:0004222; F:metalloendopeptidase activity; IBA:GO_Central.
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:0006508; P:proteolysis; IEA:InterPro.
DR   InterPro; IPR011249; Metalloenz_LuxS/M16.
DR   InterPro; IPR011765; Pept_M16_N.
DR   InterPro; IPR001431; Pept_M16_Zn_BS.
DR   InterPro; IPR007863; Peptidase_M16_C.
DR   Pfam; PF00675; Peptidase_M16; 1.
DR   Pfam; PF05193; Peptidase_M16_C; 1.
DR   SUPFAM; SSF63411; SSF63411; 2.
DR   PROSITE; PS00143; INSULINASE; 1.
PE   3: Inferred from homology;
KW   Electron transport; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW   Reference proteome; Respiratory chain; Transit peptide; Transport.
FT   TRANSIT         1..22
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000250"
FT   CHAIN           23..417
FT                   /note="Cytochrome b-c1 complex subunit 2, mitochondrial"
FT                   /id="PRO_0000026800"
SQ   SEQUENCE   417 AA;  44230 MW;  44418C003EE3F0DC CRC64;
     MTRGVPRLAV AARHFSTAEA AGVKVAAQDG QSPISDLSVV LRGGSRYATV PGVSHILEKF
     AFQNTVPKSA LRFVRELELF GGKLYTHTTR EHIVLRTQFL KQDLPYFVDA FANVLKETKF
     QQFELTERVA PVAELDLLKR ESDPAFTALE AAHEVAFRTG LGNSVYAQGY SPVTLEDVKE
     FARQVYAKQN VAVVGNNVVP ADLQQLVGTA FADLQEGSKV TQAGTTTLHG GEARVRTSTG
     NALTIALPIA EPKPVYHALA SFLGGPASMP WSVGASPLAQ ATVGTHTSVK ATYHNYGDAG
     LFAITIKGDS PAEISQVAHK AVQALKDTGA EVTEEQAARA YAKSKFAAAE AFENPDSSAS
     VIGMELLSGV SRIAPENVQK FTPAELSEAA AQLSASAKPV VAAVGQVHAL PFADELF
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024