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QCR6_MACFA
ID   QCR6_MACFA              Reviewed;          91 AA.
AC   Q8SPH5;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   25-MAY-2022, entry version 88.
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; ORFNames=QnpA-14164;
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Parietal cortex;
RX   PubMed=11991714; DOI=10.1006/geno.2002.6753;
RA   Osada N., Kusuda J., Hirata M., Tanuma R., Hida M., Sugano S., Hirai M.,
RA   Hashimoto K.;
RT   "Search for genes positively selected during primate evolution by 5'-end-
RT   sequence screening of cynomolgus monkey cDNAs.";
RL   Genomics 79:657-662(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: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}.
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DR   EMBL; AB072026; BAB86815.1; -; mRNA.
DR   RefSeq; XP_005543544.2; XM_005543487.2.
DR   AlphaFoldDB; Q8SPH5; -.
DR   SMR; Q8SPH5; -.
DR   STRING; 9541.XP_005543544.1; -.
DR   GeneID; 102136267; -.
DR   KEGG; mcf:102136267; -.
DR   eggNOG; KOG4763; Eukaryota.
DR   OrthoDB; 1621720at2759; -.
DR   Proteomes; UP000233100; Unplaced.
DR   GO; GO:0005750; C:mitochondrial respiratory chain complex III; IEA:InterPro.
DR   GO; GO:0006122; P:mitochondrial electron transport, ubiquinol to cytochrome c; IEA:InterPro.
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..91
FT                   /note="Cytochrome b-c1 complex subunit 6, mitochondrial"
FT                   /id="PRO_0000035991"
FT   REGION          1..30
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         42
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P99028"
FT   MOD_RES         85
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P99028"
FT   DISULFID        37..81
FT                   /evidence="ECO:0000250|UniProtKB:P00126"
FT   DISULFID        53..67
FT                   /evidence="ECO:0000250|UniProtKB:P00126"
SQ   SEQUENCE   91 AA;  10776 MW;  EF95D5BDF47EEF5E CRC64;
     MGLEDERKML TESGDPEKEE EEEEELVDPL TTVREQCEQL EKCVKARERL ELCDKRVSSR
     SRTEEDCTEE LLDFLHARDH CVAYKLFNNL K
 
 
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