QCR6_RAT
ID QCR6_RAT Reviewed; 89 AA.
AC Q5M9I5;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 124.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Spleen;
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).
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)) (By similarity). {ECO:0000250|UniProtKB:P00126,
CC ECO:0000250|UniProtKB:P07919}.
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}.
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; BC086954; AAH86954.1; -; mRNA.
DR RefSeq; NP_001009480.1; NM_001009480.1.
DR AlphaFoldDB; Q5M9I5; -.
DR SMR; Q5M9I5; -.
DR BioGRID; 265934; 1.
DR CORUM; Q5M9I5; -.
DR STRING; 10116.ENSRNOP00000016751; -.
DR iPTMnet; Q5M9I5; -.
DR PhosphoSitePlus; Q5M9I5; -.
DR jPOST; Q5M9I5; -.
DR PaxDb; Q5M9I5; -.
DR PRIDE; Q5M9I5; -.
DR GeneID; 366448; -.
DR KEGG; rno:366448; -.
DR UCSC; RGD:1305987; rat.
DR CTD; 7388; -.
DR RGD; 1305987; Uqcrh.
DR VEuPathDB; HostDB:ENSRNOG00000012550; -.
DR eggNOG; KOG4763; Eukaryota.
DR HOGENOM; CLU_115913_3_0_1; -.
DR InParanoid; Q5M9I5; -.
DR OMA; CQSKGHI; -.
DR OrthoDB; 1621720at2759; -.
DR PhylomeDB; Q5M9I5; -.
DR TreeFam; TF105036; -.
DR Reactome; R-RNO-611105; Respiratory electron transport.
DR PRO; PR:Q5M9I5; -.
DR Proteomes; UP000002494; Chromosome 5.
DR Bgee; ENSRNOG00000012550; Expressed in heart and 20 other tissues.
DR Genevisible; Q5M9I5; RN.
DR GO; GO:0005743; C:mitochondrial inner membrane; ISO:RGD.
DR GO; GO:0005750; C:mitochondrial respiratory chain complex III; IDA:RGD.
DR GO; GO:0005739; C:mitochondrion; ISO:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:RGD.
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 3: Inferred from homology;
KW Acetylation; Disulfide bond; Electron transport; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Reference proteome; Respiratory chain;
KW Transit peptide; Transport.
FT TRANSIT 1..13
FT /note="Mitochondrion"
FT /evidence="ECO:0000250|UniProtKB:P99028"
FT CHAIN 14..89
FT /note="Cytochrome b-c1 complex subunit 6, mitochondrial"
FT /id="PRO_0000035993"
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:0000250|UniProtKB:P99028"
FT MOD_RES 83
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P99028"
FT DISULFID 35..79
FT /evidence="ECO:0000250|UniProtKB:P00126"
FT DISULFID 51..65
FT /evidence="ECO:0000250|UniProtKB:P00126"
SQ SEQUENCE 89 AA; 10424 MW; 96FA0CCBCE312A28 CRC64;
MGLEDERKML TGSGDPKEEE EEELVDPLTT VREHCEQLEK CVKARERLES CDRRVSSRSQ
TEEDCTEELF DFLHARDHCV AHKLFKSLK
