UCRI_CHICK
ID UCRI_CHICK Reviewed; 272 AA.
AC Q5ZLR5;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 114.
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=Complex III subunit IX;
DE AltName: Full=UQCRFS1 mitochondrial targeting sequence;
DE Short=UQCRFS1 MTS;
DE Flags: Precursor;
GN Name=UQCRFS1; ORFNames=RCJMB04_5b19;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (3.16 ANGSTROMS) OF 77-272, TRANSMEMBRANE HELIX, AND
RP SUBCELLULAR LOCATION.
RX PubMed=9565029; DOI=10.1038/33612;
RA Zhang Z., Huang L., Shulmeister V.M., Chi Y.I., Kim K.K., Hung L.W.,
RA Crofts A.R., Berry E.A., Kim S.H.;
RT "Electron transfer by domain movement in cytochrome bc1.";
RL Nature 392:677-684(1998).
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:0000269|PubMed:9565029}; Single-pass membrane protein
CC {ECO:0000269|PubMed:9565029}.
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; AJ719669; CAG31328.1; -; mRNA.
DR RefSeq; NP_001005843.1; NM_001005843.1.
DR PDB; 1BCC; X-ray; 3.16 A; E=77-272.
DR PDB; 2BCC; X-ray; 3.50 A; E=77-272.
DR PDB; 3BCC; X-ray; 3.70 A; E=77-272.
DR PDB; 3CWB; X-ray; 3.51 A; E/R=77-272, I/V=45-76.
DR PDB; 3H1H; X-ray; 3.16 A; E/R=77-272, I/V=45-76.
DR PDB; 3H1I; X-ray; 3.53 A; E/R=77-272, I/V=45-76.
DR PDB; 3H1J; X-ray; 3.00 A; E/R=77-272, I/V=45-76.
DR PDB; 3H1K; X-ray; 3.48 A; E/R=77-272, I/V=45-76.
DR PDB; 3H1L; X-ray; 3.21 A; E/R=77-272, I/V=45-76.
DR PDB; 3L70; X-ray; 2.75 A; E/R=77-272, I/V=45-76.
DR PDB; 3L71; X-ray; 2.84 A; E/R=77-272, I/V=45-76.
DR PDB; 3L72; X-ray; 3.06 A; E/R=77-272, I/V=45-76.
DR PDB; 3L73; X-ray; 3.04 A; E/R=77-272, I/V=45-76.
DR PDB; 3L74; X-ray; 2.76 A; E/R=77-272, I/V=45-76.
DR PDB; 3L75; X-ray; 2.79 A; E/R=77-272, I/V=45-76.
DR PDB; 3TGU; X-ray; 2.70 A; E/R=77-272, I/V=2-76.
DR PDB; 4U3F; X-ray; 3.23 A; E/R=77-272, I/V=2-76.
DR PDBsum; 1BCC; -.
DR PDBsum; 2BCC; -.
DR PDBsum; 3BCC; -.
DR PDBsum; 3CWB; -.
DR PDBsum; 3H1H; -.
DR PDBsum; 3H1I; -.
DR PDBsum; 3H1J; -.
DR PDBsum; 3H1K; -.
DR PDBsum; 3H1L; -.
DR PDBsum; 3L70; -.
DR PDBsum; 3L71; -.
DR PDBsum; 3L72; -.
DR PDBsum; 3L73; -.
DR PDBsum; 3L74; -.
DR PDBsum; 3L75; -.
DR PDBsum; 3TGU; -.
DR PDBsum; 4U3F; -.
DR AlphaFoldDB; Q5ZLR5; -.
DR SMR; Q5ZLR5; -.
DR STRING; 9031.ENSGALP00000041886; -.
DR PaxDb; Q5ZLR5; -.
DR Ensembl; ENSGALT00000044199; ENSGALP00000041886; ENSGALG00000025819.
DR GeneID; 415752; -.
DR KEGG; gga:415752; -.
DR CTD; 7386; -.
DR VEuPathDB; HostDB:geneid_415752; -.
DR eggNOG; KOG1671; Eukaryota.
DR GeneTree; ENSGT00390000001014; -.
DR HOGENOM; CLU_055690_0_1_1; -.
DR InParanoid; Q5ZLR5; -.
DR OMA; KRTWLIA; -.
DR OrthoDB; 1174160at2759; -.
DR PhylomeDB; Q5ZLR5; -.
DR TreeFam; TF105037; -.
DR Reactome; R-GGA-611105; Respiratory electron transport.
DR EvolutionaryTrace; Q5ZLR5; -.
DR PRO; PR:Q5ZLR5; -.
DR Proteomes; UP000000539; Chromosome 11.
DR Bgee; ENSGALG00000025819; Expressed in heart and 12 other tissues.
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; 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 1: Evidence at protein level;
KW 2Fe-2S; 3D-structure; Disulfide bond; Electron transport; Iron;
KW Iron-sulfur; Membrane; Metal-binding; Mitochondrion;
KW Mitochondrion inner membrane; Reference proteome; Respiratory chain;
KW Transit peptide; Translocase; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..76
FT /note="Cytochrome b-c1 complex subunit 9"
FT /evidence="ECO:0000250|UniProtKB:Q9CR68"
FT /id="PRO_0000441933"
FT CHAIN 77..272
FT /note="Cytochrome b-c1 complex subunit Rieske,
FT mitochondrial"
FT /id="PRO_0000342403"
FT TOPO_DOM 77..104
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000250|UniProtKB:P13272"
FT TRANSMEM 105..138
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:9565029"
FT TOPO_DOM 139..272
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000250|UniProtKB:P13272"
FT DOMAIN 185..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:0000269|PubMed:9565029,
FT ECO:0007744|PDB:3H1H, ECO:0007744|PDB:3H1I,
FT ECO:0007744|PDB:3H1J"
FT BINDING 217
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000269|PubMed:9565029,
FT ECO:0007744|PDB:3H1H, ECO:0007744|PDB:3H1I,
FT ECO:0007744|PDB:3H1J"
FT BINDING 218
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000269|PubMed:9565029,
FT ECO:0007744|PDB:3H1H, ECO:0007744|PDB:3H1I"
FT BINDING 234
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000269|PubMed:9565029,
FT ECO:0007744|PDB:3H1H, ECO:0007744|PDB:3H1I,
FT ECO:0007744|PDB:3H1J"
FT BINDING 237
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000269|PubMed:9565029,
FT ECO:0007744|PDB:3H1H, ECO:0007744|PDB:3H1I,
FT ECO:0007744|PDB:3H1J"
FT BINDING 239
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000269|PubMed:9565029,
FT ECO:0007744|PDB:3H1H, ECO:0007744|PDB:3H1I,
FT ECO:0007744|PDB:3H1J"
FT DISULFID 220..236
FT /evidence="ECO:0000269|PubMed:9565029,
FT ECO:0007744|PDB:3H1H, ECO:0007744|PDB:3H1I,
FT ECO:0007744|PDB:3H1J"
FT TURN 51..55
FT /evidence="ECO:0007829|PDB:3TGU"
FT STRAND 64..70
FT /evidence="ECO:0007829|PDB:3TGU"
FT STRAND 73..75
FT /evidence="ECO:0007829|PDB:3L74"
FT HELIX 78..80
FT /evidence="ECO:0007829|PDB:3TGU"
FT TURN 87..89
FT /evidence="ECO:0007829|PDB:3TGU"
FT HELIX 92..94
FT /evidence="ECO:0007829|PDB:3TGU"
FT TURN 101..104
FT /evidence="ECO:0007829|PDB:3TGU"
FT HELIX 105..137
FT /evidence="ECO:0007829|PDB:3TGU"
FT HELIX 142..146
FT /evidence="ECO:0007829|PDB:3TGU"
FT STRAND 150..152
FT /evidence="ECO:0007829|PDB:3TGU"
FT TURN 154..156
FT /evidence="ECO:0007829|PDB:3H1J"
FT STRAND 159..161
FT /evidence="ECO:0007829|PDB:4U3F"
FT STRAND 162..167
FT /evidence="ECO:0007829|PDB:3TGU"
FT STRAND 170..176
FT /evidence="ECO:0007829|PDB:3TGU"
FT STRAND 179..183
FT /evidence="ECO:0007829|PDB:3TGU"
FT TURN 184..186
FT /evidence="ECO:0007829|PDB:3TGU"
FT STRAND 193..195
FT /evidence="ECO:0007829|PDB:3L74"
FT TURN 199..201
FT /evidence="ECO:0007829|PDB:3TGU"
FT STRAND 206..212
FT /evidence="ECO:0007829|PDB:3TGU"
FT TURN 216..218
FT /evidence="ECO:0007829|PDB:3TGU"
FT STRAND 223..225
FT /evidence="ECO:0007829|PDB:3TGU"
FT STRAND 230..234
FT /evidence="ECO:0007829|PDB:3TGU"
FT TURN 235..237
FT /evidence="ECO:0007829|PDB:3TGU"
FT STRAND 238..242
FT /evidence="ECO:0007829|PDB:3TGU"
FT TURN 243..245
FT /evidence="ECO:0007829|PDB:3TGU"
FT STRAND 249..251
FT /evidence="ECO:0007829|PDB:3TGU"
FT STRAND 265..267
FT /evidence="ECO:0007829|PDB:3H1J"
FT STRAND 268..271
FT /evidence="ECO:0007829|PDB:3TGU"
SQ SEQUENCE 272 AA; 29387 MW; 3E60AD2419D26C25 CRC64;
MLSVAARSGP FAPYLSAAAH AVPGPLKALA PAALRAEKVV LDLKRPLLCR ESMSGRSARR
DLVAGISLNA PASVRYVHND VTVPDFSAYR REDVMDATTS SQTSSEDRKG FSYLVTATAC
VATAYAAKNV VTQFISSLSA SADVLALSKI EIKLSDIPEG KNVAFKWRGK PLFVRHRTQA
EINQEAEVDV SKLRDPQHDL DRVKKPEWVI LVGVCTHLGC VPIANSGDFG GYYCPCHGSH
YDASGRIRKG PAPYNLEVPT YQFVGDDLVV VG
