ID   QCR72_ARATH             Reviewed;         122 AA.
AC   F4JWS8;
DT   05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   03-AUG-2022, entry version 68.
DE   RecName: Full=Cytochrome b-c1 complex subunit 7-2, mitochondrial;
DE   AltName: Full=Complex III subunit 7-2;
DE   AltName: Full=Complex III subunit VII;
DE   AltName: Full=Ubiquinol-cytochrome c oxidoreductase subunit 7-2;
GN   Name=QCR7-2; OrderedLocusNames=At5g25450; ORFNames=F18G18.190, T14C9.20;
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=11130714; DOI=10.1038/35048507;
RA   Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA   Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA   Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA   Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA   Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA   O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA   Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA   Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA   Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA   Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA   Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA   Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA   Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA   Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA   Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA   Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA   McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA   Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA   Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA   Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA   Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA   Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA   Bevan M., Fransz P.F.;
RT   "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL   Nature 408:823-826(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   PROTEIN SEQUENCE OF 68-104, SUBUNIT, SUBCELLULAR LOCATION, AND
RP   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).
RN   [4]
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   [5]
RP   SUBUNIT, IDENTIFICATION BY MASS SPECTROMETRY, AND NOMENCLATURE.
RC   STRAIN=cv. Columbia;
RX   PubMed=18305213; DOI=10.1104/pp.107.111260;
RA   Zsigmond L., Rigo G., Szarka A., Szekely G., Oetvoes K., Darula Z.,
RA   Medzihradszky K.F., Koncz C., Koncz Z., Szabados L.;
RT   "Arabidopsis PPR40 connects abiotic stress responses to mitochondrial
RT   electron transport.";
RL   Plant Physiol. 146:1721-1737(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:P00128}.
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, PubMed:18305213). The complex exists as
CC       an obligatory dimer and forms supercomplexes (SCs) in the inner
CC       mitochondrial membrane with NADH-ubiquinone oxidoreductase (complex I,
CC       CI), resulting in different assemblies (supercomplexes SCI(1)III(2) and
CC       SCI(2)III(4)) (PubMed:12970493). {ECO:0000269|PubMed:12970493,
CC       ECO:0000269|PubMed:18189341, ECO:0000269|PubMed:18305213}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000269|PubMed:18189341}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:P00128}; Matrix side
CC       {ECO:0000250|UniProtKB:P00128}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=1;
CC         Comment=A number of isoforms are produced. According to EST
CC         sequences.;
CC       Name=1;
CC         IsoId=F4JWS8-1; Sequence=Displayed;
CC   -!- SIMILARITY: Belongs to the UQCRB/QCR7 family. {ECO:0000305}.
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DR   EMBL; AC006258; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC006601; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CP002688; AED93444.1; -; Genomic_DNA.
DR   RefSeq; NP_197927.1; NM_122455.4. [F4JWS8-1]
DR   AlphaFoldDB; F4JWS8; -.
DR   SMR; F4JWS8; -.
DR   BioGRID; 17894; 19.
DR   IntAct; F4JWS8; 1.
DR   STRING; 3702.AT5G25450.1; -.
DR   PaxDb; F4JWS8; -.
DR   PRIDE; F4JWS8; -.
DR   ProteomicsDB; 226028; -. [F4JWS8-1]
DR   EnsemblPlants; AT5G25450.1; AT5G25450.1; AT5G25450. [F4JWS8-1]
DR   GeneID; 832619; -.
DR   Gramene; AT5G25450.1; AT5G25450.1; AT5G25450. [F4JWS8-1]
DR   KEGG; ath:AT5G25450; -.
DR   Araport; AT5G25450; -.
DR   TAIR; locus:2145527; AT5G25450.
DR   eggNOG; KOG3440; Eukaryota.
DR   HOGENOM; CLU_115154_3_0_1; -.
DR   OMA; FIDPRKN; -.
DR   PhylomeDB; F4JWS8; -.
DR   BioCyc; MetaCyc:MONQT-2769; -.
DR   PRO; PR:F4JWS8; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; F4JWS8; baseline and differential.
DR   Genevisible; F4JWS8; AT.
DR   GO; GO:0005750; C:mitochondrial respiratory chain complex III; HDA:TAIR.
DR   GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR   GO; GO:0009536; C:plastid; HDA:TAIR.
DR   GO; GO:0006122; P:mitochondrial electron transport, ubiquinol to cytochrome c; IBA:GO_Central.
DR   Gene3D; 1.10.1090.10; -; 1.
DR   InterPro; IPR003197; QCR7.
DR   InterPro; IPR036544; QCR7_sf.
DR   PANTHER; PTHR12022; PTHR12022; 1.
DR   Pfam; PF02271; UCR_14kD; 1.
DR   PIRSF; PIRSF000022; Bc1_14K; 1.
DR   SUPFAM; SSF81524; SSF81524; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Direct protein sequencing; Electron transport;
KW   Membrane; Mitochondrion; Mitochondrion inner membrane; Reference proteome;
KW   Respiratory chain; Transport.
FT   CHAIN           1..122
FT                   /note="Cytochrome b-c1 complex subunit 7-2, mitochondrial"
FT                   /id="PRO_0000418645"
SQ   SEQUENCE   122 AA;  14596 MW;  995B42332195DCF3 CRC64;
     MASFLQRLVD PRKNFLARMH MKSVSNRLRR YGLRYDDLYD PLYDLDIKEA LNRLPREIVD
     ARNQRLMRAM DLSMKHEYLP DNLQAVQTPF RSYLQDMLAL VKRERAEREA LGALPLYQRT
     IP