QCR6_MOUSE
ID QCR6_MOUSE Reviewed; 89 AA.
AC P99028; Q542K2; Q9CQP4;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 29-AUG-2001, sequence version 2.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Cytochrome b-c1 complex subunit 6, mitochondrial;
DE AltName: Full=Complex III subunit 6;
DE AltName: Full=Complex III subunit VIII;
DE AltName: Full=Cytochrome c1 non-heme 11 kDa protein;
DE AltName: Full=Mitochondrial hinge protein;
DE AltName: Full=Ubiquinol-cytochrome c reductase complex 11 kDa protein;
DE Flags: Precursor;
GN Name=Uqcrh;
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=Embryo, Kidney, Oviduct, and Thymus;
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=FVB/N; 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 14-25.
RC TISSUE=Liver;
RA Sanchez J.-C., Rouge V., Frutiger S., Hughes G., Yan J.X., Hoogland C.,
RA Appel R.D., Binz P.-A., Hochstrasser D.F., Cowthorne M.;
RL Submitted (AUG-1998) to UniProtKB.
RN [4]
RP PROTEIN SEQUENCE OF 18-32; 45-54 AND 59-76, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain, and Hippocampus;
RA Lubec G., Klug S., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [5]
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 [6]
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 [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-40 AND LYS-83, AND IDENTIFICATION
RP BY MASS 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).
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:P00127}.
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). {ECO:0000250|UniProtKB:P00126,
CC ECO:0000269|PubMed:19026783}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:P00127}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P00127}; Intermembrane side
CC {ECO:0000250|UniProtKB:P00127}.
CC -!- SIMILARITY: Belongs to the UQCRH/QCR6 family. {ECO:0000305}.
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DR EMBL; AK003266; BAB22681.1; -; mRNA.
DR EMBL; AK003539; BAB22845.1; -; mRNA.
DR EMBL; AK012552; BAB28312.1; -; mRNA.
DR EMBL; AK018712; BAB31360.1; -; mRNA.
DR EMBL; AK054005; BAC35617.1; -; mRNA.
DR EMBL; AK088185; BAC40195.1; -; mRNA.
DR EMBL; BC011388; AAH11388.1; -; mRNA.
DR CCDS; CCDS38846.1; -.
DR RefSeq; NP_079917.1; NM_025641.3.
DR PDB; 7O37; EM; 3.20 A; H/S=14-89.
DR PDB; 7O3C; EM; 3.30 A; H/S=14-89.
DR PDB; 7O3E; EM; 3.60 A; H/S=14-89.
DR PDB; 7O3H; EM; 2.60 A; H/S=14-89.
DR PDBsum; 7O37; -.
DR PDBsum; 7O3C; -.
DR PDBsum; 7O3E; -.
DR PDBsum; 7O3H; -.
DR AlphaFoldDB; P99028; -.
DR SMR; P99028; -.
DR BioGRID; 211565; 59.
DR ComplexPortal; CPX-563; Mitochondrial respiratory chain complex III.
DR CORUM; P99028; -.
DR IntAct; P99028; 2.
DR STRING; 10090.ENSMUSP00000077744; -.
DR iPTMnet; P99028; -.
DR PhosphoSitePlus; P99028; -.
DR SwissPalm; P99028; -.
DR SWISS-2DPAGE; P99028; -.
DR EPD; P99028; -.
DR jPOST; P99028; -.
DR MaxQB; P99028; -.
DR PaxDb; P99028; -.
DR PeptideAtlas; P99028; -.
DR PRIDE; P99028; -.
DR ProteomicsDB; 300220; -.
DR TopDownProteomics; P99028; -.
DR DNASU; 66576; -.
DR Ensembl; ENSMUST00000078676; ENSMUSP00000077744; ENSMUSG00000063882.
DR GeneID; 66576; -.
DR KEGG; mmu:66576; -.
DR UCSC; uc008ufv.1; mouse.
DR CTD; 7388; -.
DR MGI; MGI:1913826; Uqcrh.
DR VEuPathDB; HostDB:ENSMUSG00000063882; -.
DR eggNOG; KOG4763; Eukaryota.
DR GeneTree; ENSGT00390000003860; -.
DR HOGENOM; CLU_115913_3_0_1; -.
DR InParanoid; P99028; -.
DR OMA; CQSKGHI; -.
DR OrthoDB; 1621720at2759; -.
DR PhylomeDB; P99028; -.
DR TreeFam; TF105036; -.
DR Reactome; R-MMU-611105; Respiratory electron transport.
DR BioGRID-ORCS; 66576; 5 hits in 71 CRISPR screens.
DR ChiTaRS; Uqcrh; mouse.
DR PRO; PR:P99028; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; P99028; protein.
DR Bgee; ENSMUSG00000063882; Expressed in intercostal muscle and 300 other tissues.
DR ExpressionAtlas; P99028; baseline and differential.
DR Genevisible; P99028; 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:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0045333; P:cellular respiration; IC:ComplexPortal.
DR GO; GO:0006122; P:mitochondrial electron transport, ubiquinol to cytochrome c; IBA:GO_Central.
DR Gene3D; 1.10.287.20; -; 1.
DR InterPro; IPR003422; Cyt_b-c1_6.
DR InterPro; IPR023184; Ubol_cytC_Rdtase_hinge_dom.
DR InterPro; IPR036811; Ubol_cytC_Rdtase_hinge_dom_sf.
DR PANTHER; PTHR15336; PTHR15336; 1.
DR Pfam; PF02320; UCR_hinge; 1.
DR PIRSF; PIRSF000019; Bc1_11K; 1.
DR SUPFAM; SSF81531; SSF81531; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Direct protein sequencing; Disulfide bond;
KW Electron transport; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW Reference proteome; Respiratory chain; Transit peptide; Transport.
FT TRANSIT 1..13
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|Ref.3"
FT CHAIN 14..89
FT /note="Cytochrome b-c1 complex subunit 6, mitochondrial"
FT /id="PRO_0000035992"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 40
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 83
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT DISULFID 35..79
FT /evidence="ECO:0000250|UniProtKB:P00126"
FT DISULFID 51..65
FT /evidence="ECO:0000250|UniProtKB:P00126"
FT HELIX 27..36
FT /evidence="ECO:0007829|PDB:7O3H"
FT HELIX 39..56
FT /evidence="ECO:0007829|PDB:7O3H"
FT HELIX 67..83
FT /evidence="ECO:0007829|PDB:7O3H"
FT HELIX 85..87
FT /evidence="ECO:0007829|PDB:7O3H"
SQ SEQUENCE 89 AA; 10435 MW; 6E588E3BDF743E7B CRC64;
MGLEDERKML TGSGDPKEEE EEELVDPLTT VREHCEQLEK CVKARERLEL CDNRVSSRSQ
TEEDCTEELF DFLHARDHCV AHKLFKNLK
