UCRI2_TOBAC
ID UCRI2_TOBAC Reviewed; 272 AA.
AC P51132;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Cytochrome b-c1 complex subunit Rieske-2, mitochondrial;
DE EC=7.1.1.8;
DE AltName: Full=Complex III subunit 5-2;
DE AltName: Full=Rieske iron-sulfur protein 2;
DE Short=RISP2;
DE AltName: Full=Ubiquinol-cytochrome c reductase iron-sulfur subunit 2;
DE Flags: Precursor;
OS Nicotiana tabacum (Common tobacco).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC Nicotiana.
OX NCBI_TaxID=4097;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. SC58; TISSUE=Flower;
RX PubMed=8180500; DOI=10.2307/3869763;
RA Huang J., Struck F., Matzinger D.F., Levings C.S. III;
RT "Flower-enhanced expression of a nuclear-encoded mitochondrial respiratory
RT protein is associated with changes in mitochondrion number.";
RL Plant Cell 6:439-448(1994).
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. {ECO:0000255|PROSITE-
CC ProRule:PRU00628};
CC -!- SUBUNIT: Component of the ubiquinol-cytochrome c oxidoreductase
CC (cytochrome b-c1 complex, complex III, CIII), a multisubunit enzyme
CC composed of 3 respiratory subunits cytochrome b, cytochrome c1 and
CC Rieske protein, 2 core protein subunits, and several low-molecular
CC weight protein subunits. The complex exists as an obligatory dimer and
CC forms supercomplexes (SCs) in the inner mitochondrial membrane with
CC cytochrome c oxidase (complex IV, CIV). {ECO:0000250|UniProtKB:P08067}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:P08067}; Single-pass membrane protein
CC {ECO:0000250|UniProtKB:P08067}.
CC -!- TISSUE SPECIFICITY: High levels are seen in the flowers while a low
CC level expression is seen in the roots, leaves and stems.
CC -!- MISCELLANEOUS: The Rieske protein is a high potential 2Fe-2S protein.
CC -!- SIMILARITY: Belongs to the Rieske iron-sulfur protein family.
CC {ECO:0000305}.
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DR EMBL; L16810; AAA20831.1; -; mRNA.
DR PIR; T02027; T02027.
DR RefSeq; XP_016463094.1; XM_016607608.1.
DR AlphaFoldDB; P51132; -.
DR SMR; P51132; -.
DR STRING; 4097.P51132; -.
DR GeneID; 107786155; -.
DR OMA; LKFLLSM; -.
DR OrthoDB; 1174160at2759; -.
DR PhylomeDB; P51132; -.
DR Proteomes; UP000084051; Unplaced.
DR GO; GO:0005750; C:mitochondrial respiratory chain complex III; IBA:GO_Central.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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 2: Evidence at transcript 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..60
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 61..272
FT /note="Cytochrome b-c1 complex subunit Rieske-2,
FT mitochondrial"
FT /id="PRO_0000030677"
FT TOPO_DOM 61..109
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000305"
FT TRANSMEM 110..132
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 133..272
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000305"
FT DOMAIN 182..270
FT /note="Rieske"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 215
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 217
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 234
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 237
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT DISULFID 220..236
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
SQ SEQUENCE 272 AA; 29784 MW; 7D6965C8A0E211AE CRC64;
MLRIAGRRAS SLSRWPVRSV APSSSAFISA NHFSSDDDSS SPRSISPSLA SVFLHHTRGF
SSNSVSHAHD MGLVPDLPPT VAAIKNPTSK IVYDEHNHER YPPGDPSKRA FAYFVLTGGR
FVYASLVRLL ILKFVLSMSA SKDVLALASL EVDLSSIEPG TTVTVKWRGK PVFIRRRTED
DINLANSVDL GSLRDPQQDA ERVKSPEWLV VIGVCTHLGC IPLPNAGDFG GWFCPCHGSH
YDISGRIRKG PAPYNLEVPT YSFLEENKLL IG
