QCR8_MOUSE
ID QCR8_MOUSE Reviewed; 82 AA.
AC Q9CQ69;
DT 31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Cytochrome b-c1 complex subunit 8;
DE AltName: Full=Complex III subunit 8;
DE AltName: Full=Complex III subunit VIII;
DE AltName: Full=Ubiquinol-cytochrome c reductase complex 9.5 kDa protein;
DE AltName: Full=Ubiquinol-cytochrome c reductase complex ubiquinone-binding protein QP-C;
GN Name=Uqcrq;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Cerebellum, Embryo, Kidney, and Pancreas;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Mammary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PROTEIN SEQUENCE OF 4-40 AND 49-71, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [4]
RP SUBUNIT.
RX PubMed=19026783; DOI=10.1016/j.molcel.2008.10.021;
RA Acin-Perez R., Fernandez-Silva P., Peleato M.L., Perez-Martos A.,
RA Enriquez J.A.;
RT "Respiratory active mitochondrial supercomplexes.";
RL Mol. Cell 32:529-539(2008).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-33, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-33, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23576753; DOI=10.1073/pnas.1302961110;
RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B.,
RA Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.;
RT "Label-free quantitative proteomics of the lysine acetylome in mitochondria
RT identifies substrates of SIRT3 in metabolic pathways.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013).
RN [8]
RP INTERACTION WITH BRAWNIN.
RX PubMed=32161263; DOI=10.1038/s41467-020-14999-2;
RA Zhang S., Reljic B., Liang C., Kerouanton B., Francisco J.C., Peh J.H.,
RA Mary C., Jagannathan N.S., Olexiouk V., Tang C., Fidelito G., Nama S.,
RA Cheng R.K., Wee C.L., Wang L.C., Duek Roggli P., Sampath P., Lane L.,
RA Petretto E., Sobota R.M., Jesuthasan S., Tucker-Kellogg L., Reversade B.,
RA Menschaert G., Sun L., Stroud D.A., Ho L.;
RT "Mitochondrial peptide BRAWNIN is essential for vertebrate respiratory
RT complex III assembly.";
RL Nat. Commun. 11:1312-1312(2020).
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:P08525}.
CC -!- SUBUNIT: Component of the ubiquinol-cytochrome c oxidoreductase
CC (cytochrome b-c1 complex, complex III, CIII), a multisubunit enzyme
CC composed of 11 subunits. The complex is composed of 3 respiratory
CC subunits cytochrome b, cytochrome c1 and Rieske protein UQCRFS1, 2 core
CC protein subunits UQCRC1/QCR1 and UQCRC2/QCR2, and 6 low-molecular
CC weight protein subunits UQCRH/QCR6, UQCRB/QCR7, UQCRQ/QCR8,
CC UQCR10/QCR9, UQCR11/QCR10 and subunit 9, the cleavage product of Rieske
CC protein UQCRFS1 (By similarity). The complex exists as an obligatory
CC dimer and forms supercomplexes (SCs) in the inner mitochondrial
CC membrane with NADH-ubiquinone oxidoreductase (complex I, CI) and
CC cytochrome c oxidase (complex IV, CIV), resulting in different
CC assemblies (supercomplex SCI(1)III(2)IV(1) and megacomplex
CC MCI(2)III(2)IV(2)) (PubMed:19026783). Interacts with BRAWNIN
CC (PubMed:32161263). {ECO:0000250|UniProtKB:P13271,
CC ECO:0000269|PubMed:19026783, ECO:0000269|PubMed:32161263}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:P08525}; Single-pass membrane protein
CC {ECO:0000250|UniProtKB:P08525}.
CC -!- SIMILARITY: Belongs to the UQCRQ/QCR8 family. {ECO:0000305}.
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DR EMBL; AK007982; BAB25388.1; -; mRNA.
DR EMBL; AK002389; BAB22063.1; -; mRNA.
DR EMBL; AK003160; BAB22613.1; -; mRNA.
DR EMBL; AK005374; BAB23983.1; -; mRNA.
DR EMBL; BC028519; AAH28519.1; -; mRNA.
DR CCDS; CCDS36151.1; -.
DR RefSeq; NP_001313543.1; NM_001326614.1.
DR RefSeq; NP_079628.1; NM_025352.3.
DR PDB; 7O37; EM; 3.20 A; G/R=2-82.
DR PDB; 7O3C; EM; 3.30 A; G/R=2-82.
DR PDB; 7O3E; EM; 3.60 A; G/R=2-82.
DR PDB; 7O3H; EM; 2.60 A; G/R=2-82.
DR PDBsum; 7O37; -.
DR PDBsum; 7O3C; -.
DR PDBsum; 7O3E; -.
DR PDBsum; 7O3H; -.
DR AlphaFoldDB; Q9CQ69; -.
DR SMR; Q9CQ69; -.
DR BioGRID; 204458; 7.
DR ComplexPortal; CPX-563; Mitochondrial respiratory chain complex III.
DR CORUM; Q9CQ69; -.
DR IntAct; Q9CQ69; 5.
DR STRING; 10090.ENSMUSP00000053145; -.
DR iPTMnet; Q9CQ69; -.
DR PhosphoSitePlus; Q9CQ69; -.
DR EPD; Q9CQ69; -.
DR jPOST; Q9CQ69; -.
DR MaxQB; Q9CQ69; -.
DR PaxDb; Q9CQ69; -.
DR PeptideAtlas; Q9CQ69; -.
DR PRIDE; Q9CQ69; -.
DR ProteomicsDB; 301903; -.
DR TopDownProteomics; Q9CQ69; -.
DR Antibodypedia; 45197; 130 antibodies from 27 providers.
DR DNASU; 22272; -.
DR Ensembl; ENSMUST00000061326; ENSMUSP00000053145; ENSMUSG00000044894.
DR Ensembl; ENSMUST00000109021; ENSMUSP00000104649; ENSMUSG00000044894.
DR GeneID; 22272; -.
DR KEGG; mmu:22272; -.
DR UCSC; uc007ivy.2; mouse.
DR CTD; 27089; -.
DR MGI; MGI:107807; Uqcrq.
DR VEuPathDB; HostDB:ENSMUSG00000044894; -.
DR eggNOG; KOG4116; Eukaryota.
DR GeneTree; ENSGT00390000004029; -.
DR HOGENOM; CLU_156007_2_0_1; -.
DR InParanoid; Q9CQ69; -.
DR OMA; SWGTQEF; -.
DR OrthoDB; 1523793at2759; -.
DR PhylomeDB; Q9CQ69; -.
DR TreeFam; TF300281; -.
DR Reactome; R-MMU-611105; Respiratory electron transport.
DR BioGRID-ORCS; 22272; 25 hits in 73 CRISPR screens.
DR ChiTaRS; Uqcrq; mouse.
DR PRO; PR:Q9CQ69; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q9CQ69; protein.
DR Bgee; ENSMUSG00000044894; Expressed in interventricular septum and 276 other tissues.
DR ExpressionAtlas; Q9CQ69; baseline and differential.
DR Genevisible; Q9CQ69; MM.
DR GO; GO:0005743; C:mitochondrial inner membrane; HDA:MGI.
DR GO; GO:0005750; C:mitochondrial respiratory chain complex III; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR GO; GO:0045333; P:cellular respiration; IC:ComplexPortal.
DR GO; GO:0021680; P:cerebellar Purkinje cell layer development; IEP:UniProtKB.
DR GO; GO:0021766; P:hippocampus development; IEP:UniProtKB.
DR GO; GO:0021854; P:hypothalamus development; IEP:UniProtKB.
DR GO; GO:0030901; P:midbrain development; IEP:UniProtKB.
DR GO; GO:0006122; P:mitochondrial electron transport, ubiquinol to cytochrome c; IBA:GO_Central.
DR GO; GO:0021548; P:pons development; IEP:UniProtKB.
DR GO; GO:0021860; P:pyramidal neuron development; IEP:UniProtKB.
DR GO; GO:0021539; P:subthalamus development; IEP:UniProtKB.
DR GO; GO:0021794; P:thalamus development; IEP:UniProtKB.
DR Gene3D; 1.20.5.210; -; 1.
DR InterPro; IPR004205; Cyt_bc1_su8.
DR InterPro; IPR036642; Cyt_bc1_su8_sf.
DR PANTHER; PTHR12119; PTHR12119; 1.
DR Pfam; PF02939; UcrQ; 1.
DR SUPFAM; SSF81508; SSF81508; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Direct protein sequencing; Electron transport;
KW Membrane; Mitochondrion; Mitochondrion inner membrane; Phosphoprotein;
KW Reference proteome; Respiratory chain; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..82
FT /note="Cytochrome b-c1 complex subunit 8"
FT /id="PRO_0000193545"
FT TOPO_DOM 1..39
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000250|UniProtKB:P13271"
FT TRANSMEM 40..68
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P13271"
FT TOPO_DOM 69..82
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000250|UniProtKB:P13271"
FT MOD_RES 16
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14949"
FT MOD_RES 33
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 33
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT STRAND 13..19
FT /evidence="ECO:0007829|PDB:7O3H"
FT TURN 21..23
FT /evidence="ECO:0007829|PDB:7O3H"
FT HELIX 30..70
FT /evidence="ECO:0007829|PDB:7O3H"
FT TURN 75..78
FT /evidence="ECO:0007829|PDB:7O3H"
SQ SEQUENCE 82 AA; 9768 MW; BE0E295EAA1BC23F CRC64;
MGREFGNLAR IRHVISYSLS PFEQRAFPSY FSKGIPNVLR RTRERILRVA PPFVVVYLIY
TWGNQEFEQS KRKNPAMYEN DK
