UCRI2_ARATH
ID UCRI2_ARATH Reviewed; 274 AA.
AC Q9LYR2; Q8LD84;
DT 25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Cytochrome b-c1 complex subunit Rieske-2, mitochondrial {ECO:0000305};
DE EC=7.1.1.8 {ECO:0000250|UniProtKB:P08067};
DE AltName: Full=Complex III subunit 5-2 {ECO:0000305};
DE AltName: Full=Rieske iron-sulfur protein 2 {ECO:0000305};
DE Short=RISP2 {ECO:0000305};
DE AltName: Full=Ubiquinol-cytochrome c reductase iron-sulfur subunit 2 {ECO:0000303|PubMed:18305213};
DE Flags: Precursor;
GN Name=UCR1-2 {ECO:0000303|PubMed:18305213};
GN OrderedLocusNames=At5g13440 {ECO:0000312|Araport:AT5G13440};
GN ORFNames=T22N19.90 {ECO:0000312|EMBL:CAB87151.1};
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=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 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 SUBCELLULAR LOCATION, AND SUBUNIT.
RX PubMed=11870776;
RX DOI=10.1002/1522-2683(200202)23:4<640::aid-elps640>3.0.co;2-f;
RA Werhahn W., Braun H.P.;
RT "Biochemical dissection of the mitochondrial proteome from Arabidopsis
RT thaliana by three-dimensional gel electrophoresis.";
RL Electrophoresis 23:640-646(2002).
RN [6]
RP SUBCELLULAR LOCATION, METAL-BINDING, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=12606038; DOI=10.1016/s0014-5793(03)00101-7;
RA Herald V.L., Heazlewood J.L., Day D.A., Millar A.H.;
RT "Proteomic identification of divalent metal cation binding proteins in
RT plant mitochondria.";
RL FEBS Lett. 537:96-100(2003).
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 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).
RN [9]
RP SUBUNIT, 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. The Rieske protein is a catalytic core subunit
CC containing a [2Fe-2S] iron-sulfur cluster. It cycles between 2
CC conformational states during catalysis to transfer electrons from the
CC quinol bound in the Q(0) site in cytochrome b to cytochrome c1.
CC {ECO:0000250|UniProtKB:P08067}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a quinol + 2 Fe(III)-[cytochrome c](out) = a quinone + 2
CC Fe(II)-[cytochrome c](out) + 2 H(+)(out); Xref=Rhea:RHEA:11484,
CC Rhea:RHEA-COMP:10350, Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:24646, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034,
CC ChEBI:CHEBI:132124; EC=7.1.1.8;
CC Evidence={ECO:0000250|UniProtKB:P08067};
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00628};
CC Note=Binds 1 [2Fe-2S] cluster per subunit (By similarity). Binds to
CC divalent metal cations (PubMed:12606038). {ECO:0000255|PROSITE-
CC ProRule:PRU00628, ECO:0000269|PubMed:12606038};
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:11870776, PubMed:18189341, PubMed:18305213). The
CC complex exists as an obligatory dimer and forms supercomplexes (SCs) in
CC the inner mitochondrial membrane with NADH-ubiquinone oxidoreductase
CC (complex I, CI), resulting in different assemblies (supercomplexes
CC SCI(1)III(2) and SCI(2)III(4)) (PubMed:12970493).
CC {ECO:0000269|PubMed:11870776, ECO:0000269|PubMed:12970493,
CC ECO:0000269|PubMed:18189341, ECO:0000269|PubMed:18305213}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:11870776, ECO:0000269|PubMed:12606038,
CC ECO:0000269|PubMed:18189341}; Single-pass membrane protein
CC {ECO:0000250|UniProtKB:P08067}.
CC -!- MISCELLANEOUS: The Rieske protein is a high potential 2Fe-2S protein.
CC {ECO:0000250|UniProtKB:P08067}.
CC -!- SIMILARITY: Belongs to the Rieske iron-sulfur protein family.
CC {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; AL163572; CAB87151.1; -; Genomic_DNA.
DR EMBL; CP002688; AED91894.1; -; Genomic_DNA.
DR EMBL; AF370533; AAK48960.1; -; mRNA.
DR EMBL; AY081510; AAM10072.1; -; mRNA.
DR EMBL; AY086148; AAM63353.1; -; mRNA.
DR PIR; T48591; T48591.
DR RefSeq; NP_196848.1; NM_121347.4.
DR AlphaFoldDB; Q9LYR2; -.
DR SMR; Q9LYR2; -.
DR IntAct; Q9LYR2; 1.
DR MINT; Q9LYR2; -.
DR STRING; 3702.AT5G13440.1; -.
DR PaxDb; Q9LYR2; -.
DR PRIDE; Q9LYR2; -.
DR EnsemblPlants; AT5G13440.1; AT5G13440.1; AT5G13440.
DR GeneID; 831185; -.
DR Gramene; AT5G13440.1; AT5G13440.1; AT5G13440.
DR KEGG; ath:AT5G13440; -.
DR Araport; AT5G13440; -.
DR TAIR; locus:2181675; AT5G13440.
DR eggNOG; KOG1671; Eukaryota.
DR HOGENOM; CLU_055690_0_0_1; -.
DR InParanoid; Q9LYR2; -.
DR OMA; RAKNPEW; -.
DR OrthoDB; 1174160at2759; -.
DR PhylomeDB; Q9LYR2; -.
DR BioCyc; ARA:AT5G13440-MON; -.
DR BioCyc; MetaCyc:AT5G13440-MON; -.
DR PRO; PR:Q9LYR2; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LYR2; baseline and differential.
DR GO; GO:0031966; C:mitochondrial membrane; IDA:UniProtKB.
DR GO; GO:0005750; C:mitochondrial respiratory chain complex III; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IDA:TAIR.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0008121; F:ubiquinol-cytochrome-c reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0006122; P:mitochondrial electron transport, ubiquinol to cytochrome c; IBA:GO_Central.
DR Gene3D; 2.102.10.10; -; 1.
DR InterPro; IPR017941; Rieske_2Fe-2S.
DR InterPro; IPR036922; Rieske_2Fe-2S_sf.
DR InterPro; IPR014349; Rieske_Fe-S_prot.
DR InterPro; IPR005805; Rieske_Fe-S_prot_C.
DR InterPro; IPR004192; Rieske_TM.
DR InterPro; IPR006317; Ubiquinol_cyt_c_Rdtase_Fe-S-su.
DR PANTHER; PTHR10134; PTHR10134; 1.
DR Pfam; PF00355; Rieske; 1.
DR Pfam; PF02921; UCR_TM; 1.
DR PRINTS; PR00162; RIESKE.
DR SUPFAM; SSF50022; SSF50022; 1.
DR TIGRFAMs; TIGR01416; Rieske_proteo; 1.
DR PROSITE; PS51296; RIESKE; 1.
PE 1: Evidence at protein level;
KW 2Fe-2S; Disulfide bond; Electron transport; Iron; Iron-sulfur; Membrane;
KW Metal-binding; Mitochondrion; Mitochondrion inner membrane;
KW Reference proteome; Respiratory chain; Transit peptide; Translocase;
KW Transmembrane; Transmembrane helix; Transport.
FT TRANSIT 1..62
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 63..274
FT /note="Cytochrome b-c1 complex subunit Rieske-2,
FT mitochondrial"
FT /id="PRO_0000441898"
FT TOPO_DOM 63..111
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000250|UniProtKB:P08067"
FT TRANSMEM 112..134
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 135..274
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000250|UniProtKB:P08067"
FT DOMAIN 203..272
FT /note="Rieske"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT REGION 29..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 217
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 219
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 236
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 239
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT DISULFID 222..238
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT CONFLICT 19
FT /note="A -> V (in Ref. 4; AAM63353)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 274 AA; 29902 MW; 5A7ADCB8460420FF CRC64;
MLRVAGRRLF SVSQRSSTAT SFVLSRDHTL SDGGNSSSAS RSVPSADLSS FNSYHRSVIR
GFASQVITQG NEIGFGSEVP ATVEAVKTPN SKIVYDDHNH ERYPPGDPSK RAFAYFVLSG
GRFVYASVLR LLVLKLIVSM SASKDVLALA SLEVDLGSIE PGTTVTVKWR GKPVFIRRRT
EDDIKLANSV DVGSLRDPQE DSVRVKNPEW LIVVGVCTHL GCIPLPNAGD YGGWFCPCHG
SHYDISGRIR KGPAPYNLEV PTYSFLEENK LLIG
