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QCR9_DROME
ID   QCR9_DROME              Reviewed;          55 AA.
AC   Q9XY35;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 161.
DE   RecName: Full=Cytochrome b-c1 complex subunit 9;
DE   AltName: Full=Complex III subunit 9;
DE   AltName: Full=Complex III subunit X;
DE   AltName: Full=Protein oxen;
DE   AltName: Full=Ubiquinol-cytochrome c reductase complex 6.3 kDa protein;
GN   Name=ox; Synonyms=Qcr10, Qcr9; ORFNames=CG8764;
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Benevolenskaya E.V., Frolov M.V., Birchler J.A.;
RT   "The oxen gene is a modifier of gene expression in Drosophila.";
RL   Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley;
RX   PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA   Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA   Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA   George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA   Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA   Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA   Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA   An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA   Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA   Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA   Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA   Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA   Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA   Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA   Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA   Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA   Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA   Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA   Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA   Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA   Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA   Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA   McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA   Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA   Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA   Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA   Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA   Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA   Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA   Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA   Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA   Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA   Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA   Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA   Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=Berkeley;
RX   PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA   Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA   Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA   Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA   Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA   Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA   Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT   review.";
RL   Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
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:P22289}.
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:P22289}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000250|UniProtKB:P22289}; Single-pass membrane protein
CC       {ECO:0000250|UniProtKB:P22289}.
CC   -!- SIMILARITY: Belongs to the UQCR10/QCR9 family. {ECO:0000305}.
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DR   EMBL; AF017783; AAD28637.1; -; Genomic_DNA.
DR   EMBL; AE013599; AAF58459.1; -; Genomic_DNA.
DR   RefSeq; NP_476985.1; NM_057637.5.
DR   AlphaFoldDB; Q9XY35; -.
DR   SMR; Q9XY35; -.
DR   BioGRID; 69656; 31.
DR   DIP; DIP-23798N; -.
DR   IntAct; Q9XY35; 1.
DR   STRING; 7227.FBpp0086974; -.
DR   PaxDb; Q9XY35; -.
DR   PRIDE; Q9XY35; -.
DR   DNASU; 45401; -.
DR   EnsemblMetazoa; FBtr0087861; FBpp0086974; FBgn0011227.
DR   GeneID; 45401; -.
DR   KEGG; dme:Dmel_CG8764; -.
DR   CTD; 45401; -.
DR   FlyBase; FBgn0011227; ox.
DR   VEuPathDB; VectorBase:FBgn0011227; -.
DR   eggNOG; KOG3494; Eukaryota.
DR   HOGENOM; CLU_171977_2_0_1; -.
DR   InParanoid; Q9XY35; -.
DR   OMA; DIKHRYI; -.
DR   OrthoDB; 1624769at2759; -.
DR   PhylomeDB; Q9XY35; -.
DR   Reactome; R-DME-611105; Respiratory electron transport.
DR   BioGRID-ORCS; 45401; 0 hits in 1 CRISPR screen.
DR   GenomeRNAi; 45401; -.
DR   PRO; PR:Q9XY35; -.
DR   Proteomes; UP000000803; Chromosome 2R.
DR   Bgee; FBgn0011227; Expressed in second segment of antenna (Drosophila) and 33 other tissues.
DR   ExpressionAtlas; Q9XY35; baseline and differential.
DR   Genevisible; Q9XY35; DM.
DR   GO; GO:0005750; C:mitochondrial respiratory chain complex III; ISS:FlyBase.
DR   GO; GO:0006122; P:mitochondrial electron transport, ubiquinol to cytochrome c; ISS:FlyBase.
DR   Gene3D; 1.20.5.260; -; 1.
DR   InterPro; IPR008027; QCR9.
DR   InterPro; IPR036656; QCR9_sf.
DR   PANTHER; PTHR12980; PTHR12980; 1.
DR   Pfam; PF05365; UCR_UQCRX_QCR9; 1.
DR   SUPFAM; SSF81514; SSF81514; 1.
PE   3: Inferred from homology;
KW   Electron transport; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW   Reference proteome; Respiratory chain; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN           1..55
FT                   /note="Cytochrome b-c1 complex subunit 9"
FT                   /id="PRO_0000193555"
FT   TOPO_DOM        1..15
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000250|UniProtKB:P22289"
FT   TRANSMEM        16..41
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P22289"
FT   TOPO_DOM        42..55
FT                   /note="Chloroplast intermembrane"
FT                   /evidence="ECO:0000250|UniProtKB:P22289"
SQ   SEQUENCE   55 AA;  6294 MW;  A4A172E460818247 CRC64;
     MKVIYNTLFK RTSTYAVAII ASAFFFERAL DVTSVAIFEG INKGKLWKDI KGKYE
 
 
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