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UCRI4_TOBAC
ID   UCRI4_TOBAC             Reviewed;         236 AA.
AC   P51134;
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-4, mitochondrial;
DE            EC=7.1.1.8;
DE   AltName: Full=Complex III subunit 5-4;
DE   AltName: Full=Rieske iron-sulfur protein 4;
DE            Short=RISP4;
DE   AltName: Full=Ubiquinol-cytochrome c reductase iron-sulfur subunit 4;
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   -!- 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; L16812; AAA20833.1; -; mRNA.
DR   PIR; T02020; T02020.
DR   RefSeq; NP_001312342.1; NM_001325413.1.
DR   AlphaFoldDB; P51134; -.
DR   SMR; P51134; -.
DR   STRING; 4097.P51134; -.
DR   GeneID; 107786155; -.
DR   KEGG; nta:107786155; -.
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..24
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..236
FT                   /note="Cytochrome b-c1 complex subunit Rieske-4,
FT                   mitochondrial"
FT                   /id="PRO_0000030679"
FT   TOPO_DOM        25..73
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        74..96
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        97..236
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000305"
FT   DOMAIN          146..234
FT                   /note="Rieske"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT   BINDING         179
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT   BINDING         181
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT   BINDING         198
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT   BINDING         201
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT   DISULFID        184..200
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
SQ   SEQUENCE   236 AA;  25822 MW;  AEDFC23B7EE40D0F CRC64;
     MINFGSCWGL ASVTSNSFSI ISGFSSNSVS HAHDMGLVPD LPPTVAAIKN PTSKIVYDEH
     NHERYPPGDP SKRAFAYFVL TGGRFVYASL VRLLILKFVL SMSASKDVLA LASLEVDLSS
     IEPGTTVTVK WRGKPVFIRR RTEDDINLAN SVDLGSLRDP QQDAERVKSP EWLVVIGVCT
     HLGCIPLPNA GDFGGWFCPC HGSHYDISGR IRKGPAPYNL EVPTYSFLEE NKLLIG
 
 
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