UCRI_COLPO
ID UCRI_COLPO Reviewed; 274 AA.
AC Q69BK0;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Cytochrome b-c1 complex subunit Rieske, mitochondrial;
DE EC=7.1.1.8;
DE AltName: Full=Complex III subunit 5;
DE AltName: Full=Cytochrome b-c1 complex subunit 5;
DE AltName: Full=Rieske iron-sulfur protein;
DE Short=RISP;
DE AltName: Full=Rieske protein UQCRFS1 {ECO:0000305};
DE AltName: Full=Ubiquinol-cytochrome c reductase iron-sulfur subunit;
DE Contains:
DE RecName: Full=Cytochrome b-c1 complex subunit 9 {ECO:0000250|UniProtKB:P13272};
DE Short=Su9 {ECO:0000250|UniProtKB:P13272};
DE Short=Subunit 9 {ECO:0000250|UniProtKB:P13272};
DE AltName: Full=8 kDa subunit 9 {ECO:0000250|UniProtKB:P13272};
DE AltName: Full=Complex III subunit IX;
DE AltName: Full=Cytochrome b-c1 complex subunit 11;
DE AltName: Full=UQCRFS1 mitochondrial targeting sequence;
DE Short=UQCRFS1 MTS;
DE AltName: Full=Ubiquinol-cytochrome c reductase 8 kDa protein {ECO:0000250|UniProtKB:P13272};
DE Flags: Precursor;
GN Name=UQCRFS1;
OS Colobus polykomos (Western black-and-white colobus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Colobinae; Colobus.
OX NCBI_TaxID=9572;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Doan J.W., Wildman D.E., Schmidt T.R., Weiss M.L., Goodman M.,
RA Grossman L.I.;
RT "Molecular evolution of the iron sulfur protein and subunit 9 of complex
RT III of the electron transport chain in primates.";
RL Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: [Cytochrome b-c1 complex subunit Rieske, mitochondrial]:
CC Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit
CC transmembrane complex that is part of the mitochondrial electron
CC transport chain which drives oxidative phosphorylation. The respiratory
CC chain contains 3 multisubunit complexes succinate dehydrogenase
CC (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-
CC c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV,
CC CIV), that cooperate to transfer electrons derived from NADH and
CC succinate to molecular oxygen, creating an electrochemical gradient
CC over the inner membrane that drives transmembrane transport and the ATP
CC synthase. The cytochrome b-c1 complex catalyzes electron transfer from
CC ubiquinol to cytochrome c, linking this redox reaction to translocation
CC of protons across the mitochondrial inner membrane, with protons being
CC carried across the membrane as hydrogens on the quinol. In the process
CC called Q cycle, 2 protons are consumed from the matrix, 4 protons are
CC released into the intermembrane space and 2 electrons are passed to
CC cytochrome c. The Rieske protein is a catalytic core subunit containing
CC a [2Fe-2S] iron-sulfur cluster. It cycles between 2 conformational
CC states during catalysis to transfer electrons from the quinol bound in
CC the Q(0) site in cytochrome b to cytochrome c1 (By similarity).
CC Incorporation of UQCRFS1 is the penultimate step in complex III
CC assembly (By similarity). {ECO:0000250|UniProtKB:P08067,
CC ECO:0000250|UniProtKB:P47985}.
CC -!- FUNCTION: [Cytochrome b-c1 complex subunit 9]: Component of the
CC ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex
CC III, CIII). UQCRFS1 undergoes proteolytic processing once it is
CC incorporated in the complex III dimer. One of the fragments, called
CC subunit 9, corresponds to its mitochondrial targeting sequence (MTS)
CC (By similarity). The proteolytic processing is necessary for the
CC correct insertion of UQCRFS1 in the complex III dimer, but the
CC persistence of UQCRFS1-derived fragments may prevent newly imported
CC UQCRFS1 to be processed and assembled into complex III and is
CC detrimental for the complex III structure and function (By similarity).
CC {ECO:0000250|UniProtKB:P13272, ECO:0000250|UniProtKB:P47985,
CC ECO:0000250|UniProtKB:Q9CR68}.
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. Fe-S cluster delivery to the
CC Rieske protein is mediated by components of the iron sulfur (Fe-S)
CC cluster assembly machinery that reside in the mitochondrial matrix
CC (including HSC20 and LYRM7) (By similarity).
CC {ECO:0000250|UniProtKB:P47985, ECO:0000255|PROSITE-ProRule:PRU00628};
CC -!- SUBUNIT: [Cytochrome b-c1 complex subunit Rieske, mitochondrial]:
CC Component of the ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1
CC complex, complex III, CIII), a multisubunit enzyme composed of 11
CC subunits. The complex is composed of 3 respiratory subunits cytochrome
CC b, cytochrome c1 and Rieske protein UQCRFS1, 2 core protein subunits
CC UQCRC1/QCR1 and UQCRC2/QCR2, and 6 low-molecular weight protein
CC subunits UQCRH/QCR6, UQCRB/QCR7, UQCRQ/QCR8, UQCR10/QCR9, UQCR11/QCR10
CC and subunit 9, the cleavage product of Rieske protein UQCRFS1. 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) and cytochrome c oxidase (complex IV, CIV), resulting
CC in different assemblies (supercomplex SCI(1)III(2)IV(1) and megacomplex
CC MCI(2)III(2)IV(2)) (By similarity). Incorporation of the Rieske protein
CC UQCRFS1 is the penultimate step in complex III assembly. Interacts with
CC TTC19, which is involved in the clearance of UQCRFS1 fragments (By
CC similarity). {ECO:0000250|UniProtKB:P13272,
CC ECO:0000250|UniProtKB:P47985}.
CC -!- SUBUNIT: [Cytochrome b-c1 complex subunit 9]: Component of the
CC ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex
CC III, CIII). Subunit 9 corresponds to the mitochondrial targeting
CC sequence (MTS) of Rieske protein UQCRFS1. It is retained after
CC processing and incorporated inside complex III, where it remains bound
CC to the complex and localizes between the 2 core subunits UQCRC1/QCR1
CC and UQCRC2/QCR2. {ECO:0000250|UniProtKB:P13272}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:Q5ZLR5}; Single-pass membrane protein
CC {ECO:0000250|UniProtKB:Q5ZLR5}.
CC -!- PTM: Proteolytic processing is necessary for the correct insertion of
CC UQCRFS1 in the complex III dimer. Several fragments are generated
CC during UQCRFS1 insertion, most probably due to the endogenous matrix-
CC processing peptidase (MPP) activity of the 2 core protein subunits
CC UQCRC1/QCR1 and UQCRC2/QCR2, which are homologous to the 2
CC mitochondrial-processing peptidase (MPP) subunits beta-MPP and alpha-
CC MPP respectively. The action of the protease is also necessary for the
CC clearance of the UQCRFS1 fragments. {ECO:0000250|UniProtKB:Q9CR68}.
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}.
CC -!- CAUTION: Several peptides are generated during UQCRFS1 insertion.
CC According to some authors, the identification of the transit peptide as
CC the subunit 9, does not necessary imply that it must be considered as a
CC structural subunit of the complex III dimer as additional fragments
CC from UQCRFS1 are also present. {ECO:0000250|UniProtKB:P13272,
CC ECO:0000250|UniProtKB:P47985}.
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DR EMBL; AY387508; AAR32736.1; -; Genomic_DNA.
DR EMBL; AY387507; AAR32736.1; JOINED; Genomic_DNA.
DR AlphaFoldDB; Q69BK0; -.
DR SMR; Q69BK0; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0070469; C:respirasome; IEA:UniProtKB-KW.
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:0008121; F:ubiquinol-cytochrome-c reductase activity; IEA:UniProtKB-EC.
DR Gene3D; 1.20.5.270; -; 1.
DR Gene3D; 2.102.10.10; -; 1.
DR InterPro; IPR037008; bc1_Rieske_TM_sf.
DR InterPro; IPR011070; Globular_prot_asu/bsu.
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; IPR015248; Ubiqinol_cyt_c_Rdtase_N.
DR InterPro; IPR006317; Ubiquinol_cyt_c_Rdtase_Fe-S-su.
DR PANTHER; PTHR10134; PTHR10134; 1.
DR Pfam; PF00355; Rieske; 1.
DR Pfam; PF09165; Ubiq-Cytc-red_N; 1.
DR Pfam; PF02921; UCR_TM; 1.
DR PRINTS; PR00162; RIESKE.
DR SUPFAM; SSF50022; SSF50022; 1.
DR SUPFAM; SSF56568; SSF56568; 1.
DR TIGRFAMs; TIGR01416; Rieske_proteo; 1.
DR PROSITE; PS51296; RIESKE; 1.
PE 3: Inferred from homology;
KW 2Fe-2S; Disulfide bond; Electron transport; Iron; Iron-sulfur; Membrane;
KW Metal-binding; Mitochondrion; Mitochondrion inner membrane;
KW Respiratory chain; Transit peptide; Translocase; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..78
FT /note="Cytochrome b-c1 complex subunit 9"
FT /evidence="ECO:0000250|UniProtKB:Q9CR68"
FT /id="PRO_0000307239"
FT CHAIN 79..274
FT /note="Cytochrome b-c1 complex subunit Rieske,
FT mitochondrial"
FT /id="PRO_0000030662"
FT TOPO_DOM 79..103
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000250|UniProtKB:P13272"
FT TRANSMEM 104..140
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P13272"
FT TOPO_DOM 141..274
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000250|UniProtKB:P13272"
FT DOMAIN 187..272
FT /note="Rieske"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 217
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250|UniProtKB:P13272"
FT BINDING 219
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250|UniProtKB:P13272"
FT BINDING 236
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250|UniProtKB:P13272"
FT BINDING 239
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250|UniProtKB:P13272"
FT BINDING 241
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250|UniProtKB:P13272"
FT DISULFID 222..238
FT /evidence="ECO:0000250|UniProtKB:P13272"
SQ SEQUENCE 274 AA; 29605 MW; E0FEEC422F556D93 CRC64;
MLSVAARSGP FAPVLSATSR GVAGALRPLV QAAVPATSEP PVLDLKRPFL SRESLSGQAV
RRPLVASVGL NVPASVCYSH TDVKVPDFCD YRRPEVLDST KSSRESSEAR KSFSYMVTAV
TTVGVAYAAK NAVTQFVSSM SASADVLAMA KIEVKLSDIP EGKNMAFKWR GKPLFVRHRT
QKEIEQEAAV ELSQLRDPQH DLDRVKKPEW VILIGVCTHL GCVPIANAGD FGGYYCPCHG
SHYDASGRIR LGPAPLNLEV PTYEFTSDDM VVVG
