UCRQ1_ARATH
ID UCRQ1_ARATH Reviewed; 72 AA.
AC Q9SG91; A0A178VJR6;
DT 26-FEB-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Cytochrome b-c1 complex subunit 8-1, mitochondrial;
DE AltName: Full=Complex III subunit 8-1;
DE AltName: Full=Complex III subunit VIII;
DE AltName: Full=Ubiquinol-cytochrome c oxidoreductase subunit 8-1;
DE AltName: Full=Ubiquinol-cytochrome c reductase complex ubiquinone-binding protein QP-C;
GN Name=UCRQ-1; OrderedLocusNames=At3g10860 {ECO:0000312|Araport:AT3G10860};
GN ORFNames=T7M13.6 {ECO:0000312|EMBL:AAF19563.1};
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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
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 [5]
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 [6]
RP SUBCELLULAR LOCATION, SUBUNIT, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18189341; DOI=10.1021/pr700595p;
RA Meyer E.H., Taylor N.L., Millar A.H.;
RT "Resolving and identifying protein components of plant mitochondrial
RT respiratory complexes using three dimensions of gel electrophoresis.";
RL J. Proteome Res. 7:786-794(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. {ECO:0000250|UniProtKB:P08525}.
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) (PubMed:18189341). 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), resulting
CC in different assemblies (supercomplexes SCI(1)III(2) and SCI(2)III(4))
CC (PubMed:12970493). {ECO:0000269|PubMed:12970493,
CC ECO:0000269|PubMed:18189341}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:P08525}; Single-pass membrane protein
CC {ECO:0000250|UniProtKB:P08525}.
CC -!- SIMILARITY: Belongs to the UQCRQ/QCR8 family. {ECO:0000305}.
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DR EMBL; AC011708; AAF19563.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74964.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM65253.1; -; Genomic_DNA.
DR EMBL; BT000474; AAN17451.1; -; mRNA.
DR EMBL; BT006507; AAP21315.1; -; mRNA.
DR EMBL; AY086370; AAM64437.1; -; mRNA.
DR RefSeq; NP_001327236.1; NM_001337900.1.
DR RefSeq; NP_187697.1; NM_111923.5.
DR AlphaFoldDB; Q9SG91; -.
DR SMR; Q9SG91; -.
DR IntAct; Q9SG91; 1.
DR STRING; 3702.AT3G10860.1; -.
DR PaxDb; Q9SG91; -.
DR PRIDE; Q9SG91; -.
DR ProteomicsDB; 179648; -.
DR DNASU; 820256; -.
DR EnsemblPlants; AT3G10860.1; AT3G10860.1; AT3G10860.
DR EnsemblPlants; AT3G10860.2; AT3G10860.2; AT3G10860.
DR GeneID; 820256; -.
DR Gramene; AT3G10860.1; AT3G10860.1; AT3G10860.
DR Gramene; AT3G10860.2; AT3G10860.2; AT3G10860.
DR KEGG; ath:AT3G10860; -.
DR Araport; AT3G10860; -.
DR TAIR; locus:2103217; AT3G10860.
DR eggNOG; ENOG502S4G5; Eukaryota.
DR HOGENOM; CLU_202122_0_0_1; -.
DR InParanoid; Q9SG91; -.
DR OMA; TYWYAQY; -.
DR OrthoDB; 1617367at2759; -.
DR PhylomeDB; Q9SG91; -.
DR BioCyc; ARA:MONQT-2773; -.
DR BioCyc; MetaCyc:MONQT-2773; -.
DR PRO; PR:Q9SG91; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9SG91; baseline and differential.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005750; C:mitochondrial respiratory chain complex III; HDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0006122; P:mitochondrial electron transport, ubiquinol to cytochrome c; IEA:InterPro.
DR Gene3D; 1.20.5.210; -; 1.
DR InterPro; IPR020101; Cyt_b-c1_8-plants.
DR InterPro; IPR036642; Cyt_bc1_su8_sf.
DR PANTHER; PTHR34559; PTHR34559; 1.
DR Pfam; PF10890; Cyt_b-c1_8; 1.
DR SUPFAM; SSF81508; SSF81508; 1.
PE 1: Evidence at protein level;
KW Electron transport; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW Reference proteome; Respiratory chain; Transmembrane; Transmembrane helix;
KW Transport; Ubiquinone.
FT CHAIN 1..72
FT /note="Cytochrome b-c1 complex subunit 8-1, mitochondrial"
FT /id="PRO_0000449254"
FT TOPO_DOM 1..41
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000250|UniProtKB:P08525"
FT TRANSMEM 42..58
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 59..72
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000250|UniProtKB:P08525"
SQ SEQUENCE 72 AA; 8505 MW; D095F8AED9EFC97C CRC64;
MGKQPVKLKA VVYALSPFQQ KIMTGLWKDL PEKIHHKVSE NWISATLLVT PVVGTYWYAQ
YFKEQEKLEH RF
