QCR10_MOUSE
ID QCR10_MOUSE Reviewed; 56 AA.
AC Q9CPX8; Q3TFX1;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Cytochrome b-c1 complex subunit 10;
DE AltName: Full=Complex III subunit 10;
DE AltName: Full=Complex III subunit XI;
DE AltName: Full=Ubiquinol-cytochrome c reductase complex 6.4 kDa protein;
GN Name=Uqcr11; Synonyms=Uqcr;
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=BALB/cJ, and C57BL/6J; TISSUE=Brain, Heart, and Hippocampus;
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=Kidney;
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 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).
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. QCR10 has a role in CIII assembly and RIP1
CC stability. {ECO:0000250|UniProtKB:P37299}.
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:P07552,
CC ECO:0000269|PubMed:19026783}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:P37299}; Single-pass membrane protein
CC {ECO:0000250|UniProtKB:P37299}.
CC -!- SIMILARITY: Belongs to the UQCR11/QCR10 family. {ECO:0000305}.
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DR EMBL; AK003033; BAB22521.1; -; mRNA.
DR EMBL; AK003443; BAB22793.1; -; mRNA.
DR EMBL; AK013513; BAB28890.1; -; mRNA.
DR EMBL; AK167946; BAE39949.1; -; mRNA.
DR EMBL; AK168974; BAE40777.1; -; mRNA.
DR EMBL; BC034408; AAH34408.1; -; mRNA.
DR CCDS; CCDS35981.1; -.
DR RefSeq; NP_079926.1; NM_025650.2.
DR PDB; 7O37; EM; 3.20 A; K/V=1-56.
DR PDB; 7O3C; EM; 3.30 A; K/V=1-56.
DR PDB; 7O3H; EM; 2.60 A; K/V=1-56.
DR PDBsum; 7O37; -.
DR PDBsum; 7O3C; -.
DR PDBsum; 7O3H; -.
DR AlphaFoldDB; Q9CPX8; -.
DR SMR; Q9CPX8; -.
DR ComplexPortal; CPX-563; Mitochondrial respiratory chain complex III.
DR CORUM; Q9CPX8; -.
DR STRING; 10090.ENSMUSP00000020372; -.
DR EPD; Q9CPX8; -.
DR jPOST; Q9CPX8; -.
DR MaxQB; Q9CPX8; -.
DR PaxDb; Q9CPX8; -.
DR PRIDE; Q9CPX8; -.
DR ProteomicsDB; 301901; -.
DR TopDownProteomics; Q9CPX8; -.
DR DNASU; 66594; -.
DR Ensembl; ENSMUST00000020372; ENSMUSP00000020372; ENSMUSG00000020163.
DR GeneID; 66594; -.
DR KEGG; mmu:66594; -.
DR UCSC; uc007gde.1; mouse.
DR CTD; 10975; -.
DR MGI; MGI:1913844; Uqcr11.
DR VEuPathDB; HostDB:ENSMUSG00000020163; -.
DR eggNOG; ENOG502S9FZ; Eukaryota.
DR GeneTree; ENSGT00390000018299; -.
DR HOGENOM; CLU_211742_0_0_1; -.
DR InParanoid; Q9CPX8; -.
DR OMA; ASMWGAV; -.
DR OrthoDB; 1621371at2759; -.
DR PhylomeDB; Q9CPX8; -.
DR TreeFam; TF105034; -.
DR BioGRID-ORCS; 66594; 7 hits in 70 CRISPR screens.
DR ChiTaRS; Uqcr11; mouse.
DR PRO; PR:Q9CPX8; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q9CPX8; protein.
DR Bgee; ENSMUSG00000020163; Expressed in right kidney and 93 other tissues.
DR Genevisible; Q9CPX8; 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:0006122; P:mitochondrial electron transport, ubiquinol to cytochrome c; IC:ComplexPortal.
DR InterPro; IPR029027; Single_a-helix_sf.
DR InterPro; IPR015089; UQCR.
DR PANTHER; PTHR15420; PTHR15420; 1.
DR Pfam; PF08997; UCR_6-4kD; 1.
DR SUPFAM; SSF81518; SSF81518; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Electron transport; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Reference proteome; Respiratory chain;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..56
FT /note="Cytochrome b-c1 complex subunit 10"
FT /id="PRO_0000193561"
FT TOPO_DOM 1..12
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000250|UniProtKB:P07552"
FT TRANSMEM 13..35
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P07552"
FT TOPO_DOM 36..56
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000250|UniProtKB:P07552"
FT HELIX 3..5
FT /evidence="ECO:0007829|PDB:7O37"
FT HELIX 8..36
FT /evidence="ECO:0007829|PDB:7O3H"
FT HELIX 39..42
FT /evidence="ECO:0007829|PDB:7O3H"
FT HELIX 47..51
FT /evidence="ECO:0007829|PDB:7O3H"
SQ SEQUENCE 56 AA; 6539 MW; EAF75D79D41B5713 CRC64;
MLSRFLGPRY RELARNWIPT AGMWGTVGAV GLVWATDWRL ILDWVPYING KFKKDD
