QCR61_ARATH
ID QCR61_ARATH Reviewed; 69 AA.
AC Q0WWE3; Q8LDP7; Q9XI58;
DT 26-FEB-2020, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 25-MAY-2022, entry version 133.
DE RecName: Full=Cytochrome b-c1 complex subunit 6-1, mitochondrial;
DE AltName: Full=Complex III subunit 6-1;
DE AltName: Full=Complex III subunit VI;
DE AltName: Full=Mitochondrial hinge protein;
DE AltName: Full=Ubiquinol-cytochrome c oxidoreductase subunit 6-1;
GN Name=QCR6-1; OrderedLocusNames=At1g15120 {ECO:0000312|Araport:AT1G15120};
GN ORFNames=F9L1.5 {ECO:0000312|EMBL:AAD39640.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Quinitio C., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia; TISSUE=Rosette leaf;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP SUBUNIT.
RX PubMed=12970493; DOI=10.1104/pp.103.024620;
RA Eubel H., Jansch L., Braun H.P.;
RT "New insights into the respiratory chain of plant mitochondria.
RT Supercomplexes and a unique composition of complex II.";
RL Plant Physiol. 133:274-286(2003).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
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 10 subunits. The complex is composed of 3 respiratory
CC subunits cytochrome b (MT-CYB), cytochrome c1 (CYC1-1 or CYC1-2) and
CC Rieske protein (UCR1-1 or UCR1-2), 2 core protein subunits MPPalpha1
CC (or MPPalpha2) and MPPB, and 5 low-molecular weight protein subunits
CC QCR7-1 (or QCR7-2), UCRQ-1 (or UCRQ-2), QCR9, UCRY and probably QCR6-1
CC (or QCR6-2) (Probable). The complex exists as an obligatory dimer and
CC forms supercomplexes (SCs) in the inner mitochondrial membrane with
CC NADH-ubiquinone oxidoreductase (complex I, CI), resulting in different
CC assemblies (supercomplexes SCI(1)III(2) and SCI(2)III(4))
CC (PubMed:12970493). {ECO:0000269|PubMed:12970493, ECO:0000305}.
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 -!- SEQUENCE CAUTION:
CC Sequence=AAD39640.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC007591; AAD39640.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE29267.1; -; Genomic_DNA.
DR EMBL; AK226409; BAE98555.1; -; mRNA.
DR EMBL; BT028948; ABI49495.1; -; mRNA.
DR EMBL; AK318966; BAH57081.1; -; mRNA.
DR EMBL; AY085872; AAM63085.1; -; mRNA.
DR PIR; H86284; H86284.
DR RefSeq; NP_172964.1; NM_101380.3.
DR AlphaFoldDB; Q0WWE3; -.
DR SMR; Q0WWE3; -.
DR STRING; 3702.AT1G15120.2; -.
DR PRIDE; Q0WWE3; -.
DR ProteomicsDB; 191872; -.
DR EnsemblPlants; AT1G15120.1; AT1G15120.1; AT1G15120.
DR GeneID; 838075; -.
DR Gramene; AT1G15120.1; AT1G15120.1; AT1G15120.
DR KEGG; ath:AT1G15120; -.
DR Araport; AT1G15120; -.
DR HOGENOM; CLU_115913_2_1_1; -.
DR OMA; YQACTRR; -.
DR PhylomeDB; Q0WWE3; -.
DR PRO; PR:Q0WWE3; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q0WWE3; baseline and differential.
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 1: Evidence at protein level;
KW Disulfide bond; Electron transport; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Reference proteome; Respiratory chain;
KW Transport.
FT CHAIN 1..69
FT /note="Cytochrome b-c1 complex subunit 6-1, mitochondrial"
FT /id="PRO_0000449256"
FT DISULFID 17..59
FT /evidence="ECO:0000255|PIRSR:PIRSR000019-1"
FT DISULFID 31..45
FT /evidence="ECO:0000255|PIRSR:PIRSR000019-1"
FT CONFLICT 37
FT /note="G -> S (in Ref. 6; AAM63085)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 69 AA; 7983 MW; B86C249474155C11 CRC64;
MADDEVVDPK KYLEESCKPK CVKPLLEYQA CVKRIQGDDS GHKHCTGQYF DYWQCIDKCV
APKLFAKLK
