UCRI_HUMAN
ID UCRI_HUMAN Reviewed; 274 AA.
AC P47985; A8K519; Q6NVX5; Q9UPH2;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 2.
DT 03-AUG-2022, entry version 211.
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 {ECO:0000312|HGNC:HGNC:12587};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ALA-6.
RX PubMed=2158323;
RA Nishikimi M., Hosokawa Y., Toda H., Suzuki H., Ozawa T.;
RT "The primary structure of human Rieske iron-sulfur protein of mitochondrial
RT cytochrome bc1 complex deduced from cDNA analysis.";
RL Biochem. Int. 20:155-160(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ALA-6.
RX PubMed=7721092; DOI=10.1016/0378-1119(94)00683-j;
RA Pennacchio L., Bergmann A., Fukushima A., Salemi A., Okubo K., Lennon G.;
RT "Structure, sequence and location of the UQCRFS1 gene for the human Rieske
RT Fe-S protein.";
RL Gene 155:207-211(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ALA-6.
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ALA-6.
RC TISSUE=Brain, Lung, and Lymph;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP PROTEIN SEQUENCE OF 79-90.
RC TISSUE=Kidney;
RX PubMed=9150947; DOI=10.1002/elps.1150180343;
RA Sarto C., Marocchi A., Sanchez J.-C., Giannone B., Frutiger S., Golaz O.,
RA Wilkins M.R., Doro G., Cappellano F., Hughes G.J., Hochstrasser D.F.,
RA Mocarelli P.;
RT "Renal cell carcinoma and normal kidney protein expression.";
RL Electrophoresis 18:599-604(1997).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [9]
RP PROTEOLYTIC PROCESSING, IDENTIFICATION BY MASS SPECTROMETRY, SUBUNIT,
RP INTERACTION WITH TTC19, AND FUNCTION.
RX PubMed=28673544; DOI=10.1016/j.molcel.2017.06.001;
RA Bottani E., Cerutti R., Harbour M.E., Ravaglia S., Dogan S.A., Giordano C.,
RA Fearnley I.M., D'Amati G., Viscomi C., Fernandez-Vizarra E., Zeviani M.;
RT "TTC19 plays a husbandry role on UQCRFS1 turnover in the biogenesis of
RT mitochondrial respiratory complex III.";
RL Mol. Cell 67:96-105(2017).
RN [10]
RP SUBUNIT, FUNCTION, AND COFACTOR.
RX PubMed=28380382; DOI=10.1016/j.cmet.2017.03.010;
RA Maio N., Kim K.S., Singh A., Rouault T.A.;
RT "A single adaptable cochaperone-scaffold complex delivers nascent iron-
RT sulfur clusters to mammalian respiratory chain complexes I-III.";
RL Cell Metab. 25:945-953(2017).
RN [11]
RP INVOLVEMENT IN MC3DN10, VARIANTS MC3DN10 ASP-14 AND 204-ARG--GLY-274 DEL,
RP CHARACTERIZATION OF VARIANTS MC3DN10 ASP-14 AND 204-ARG--GLY-274 DEL,
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=31883641; DOI=10.1016/j.ajhg.2019.12.005;
RA Gusic M., Schottmann G., Feichtinger R.G., Du C., Scholz C., Wagner M.,
RA Mayr J.A., Lee C.Y., Yepez V.A., Lorenz N., Morales-Gonzalez S.,
RA Panneman D.M., Roetig A., Rodenburg R.J.T., Wortmann S.B., Prokisch H.,
RA Schuelke M.;
RT "Bi-allelic UQCRFS1 variants are associated with mitochondrial complex III
RT deficiency, cardiomyopathy, and alopecia totalis.";
RL Am. J. Hum. Genet. 106:102-111(2020).
RN [12]
RP STRUCTURE BY ELECTRON MICROSCOPY (3.40 ANGSTROMS) OF 1-57 AND 79-274.
RX PubMed=28844695; DOI=10.1016/j.cell.2017.07.050;
RA Guo R., Zong S., Wu M., Gu J., Yang M.;
RT "Architecture of human mitochondrial respiratory megacomplex I2III2IV2.";
RL Cell 170:1247-1257(2017).
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
CC (PubMed:31883641). The respiratory chain contains 3 multisubunit
CC complexes succinate dehydrogenase (complex II, CII), ubiquinol-
CC cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III,
CC CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to
CC transfer electrons derived from NADH and succinate to molecular oxygen,
CC creating an electrochemical gradient over the inner membrane that
CC drives transmembrane transport and the ATP synthase. The cytochrome b-
CC c1 complex catalyzes electron transfer from ubiquinol to cytochrome c,
CC linking this redox reaction to translocation of protons across the
CC mitochondrial inner membrane, with protons being carried across the
CC membrane as hydrogens on the quinol. In the process called Q cycle, 2
CC protons are consumed from the matrix, 4 protons are released into the
CC intermembrane space and 2 electrons are passed to cytochrome c. The
CC Rieske protein is a catalytic core subunit containing a [2Fe-2S] iron-
CC sulfur cluster. It cycles between 2 conformational states during
CC catalysis to transfer electrons from the quinol bound in the Q(0) site
CC in cytochrome b to cytochrome c1 (By similarity). Incorporation of
CC UQCRFS1 is the penultimate step in complex III assembly
CC (PubMed:28673544). {ECO:0000250|UniProtKB:P08067,
CC ECO:0000269|PubMed:28673544, ECO:0000269|PubMed:31883641}.
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 The proteolytic processing is necessary for the correct insertion of
CC UQCRFS1 in the complex III dimer, but the persistence of UQCRFS1-
CC derived fragments may prevent newly imported UQCRFS1 to be processed
CC and assembled into complex III and is detrimental for the complex III
CC structure and function. {ECO:0000269|PubMed:28673544}.
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:0000250|UniProtKB:P13272};
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). {ECO:0000269|PubMed:28380382};
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 (By
CC similarity). The complex exists as an obligatory dimer and forms
CC supercomplexes (SCs) in the inner mitochondrial membrane with NADH-
CC ubiquinone oxidoreductase (complex I, CI) and cytochrome c oxidase
CC (complex IV, CIV), resulting in different assemblies (supercomplex
CC SCI(1)III(2)IV(1) and megacomplex MCI(2)III(2)IV(2)) (PubMed:28844695).
CC Incorporation of the Rieske protein UQCRFS1 is the penultimate step in
CC complex III assembly (PubMed:28380382). Interacts with TTC19, which is
CC involved in the clearance of UQCRFS1 fragments (PubMed:28673544).
CC {ECO:0000250|UniProtKB:P13272, ECO:0000269|PubMed:28380382,
CC ECO:0000269|PubMed:28673544, ECO:0000269|PubMed:28844695}.
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:0000269|PubMed:28844695}.
CC -!- INTERACTION:
CC P47985; Q5U5X0: LYRM7; NbExp=14; IntAct=EBI-1045520, EBI-13943106;
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000305|PubMed:31883641}; 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:0000269|PubMed:28673544}.
CC -!- DISEASE: Mitochondrial complex III deficiency, nuclear 10 (MC3DN10)
CC [MIM:618775]: A form of mitochondrial complex III deficiency, a
CC disorder of the mitochondrial respiratory chain resulting in a highly
CC variable phenotype depending on which tissues are affected. MC3DN10 is
CC an autosomal recessive form characterized by fetal bradycardia, poor
CC feeding, hypotonia, hypertrophic cardiomyopathy, alopecia totalis, low
CC mitochondrial complex III activity and lactic acidosis.
CC {ECO:0000269|PubMed:31883641}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
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 (PubMed:28673544). According to some authors, the identification of the
CC transit peptide as the subunit 9, does not necessary imply that it must
CC be considered as a structural subunit of the complex III dimer as
CC additional fragments from UQCRFS1 are also present (PubMed:28673544).
CC {ECO:0000269|PubMed:28673544}.
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DR EMBL; L32977; AAC41754.1; -; Genomic_DNA.
DR EMBL; L32917; AAC41754.1; JOINED; Genomic_DNA.
DR EMBL; AK291134; BAF83823.1; -; mRNA.
DR EMBL; AC007786; AAD38242.1; -; Genomic_DNA.
DR EMBL; BC000649; AAH00649.1; -; mRNA.
DR EMBL; BC010035; AAH10035.1; -; mRNA.
DR EMBL; BC067832; AAH67832.1; -; mRNA.
DR CCDS; CCDS12415.1; -.
DR RefSeq; NP_005994.2; NM_006003.2.
DR PDB; 5XTE; EM; 3.40 A; B/O=1-57, C/P=79-274.
DR PDB; 5XTH; EM; 3.90 A; AB/AO=1-57, AC/AP=79-274.
DR PDB; 5XTI; EM; 17.40 A; AB/AO=1-57, AC/AP=79-274.
DR PDBsum; 5XTE; -.
DR PDBsum; 5XTH; -.
DR PDBsum; 5XTI; -.
DR AlphaFoldDB; P47985; -.
DR SMR; P47985; -.
DR BioGRID; 113232; 220.
DR ComplexPortal; CPX-560; Mitochondrial respiratory chain complex III.
DR IntAct; P47985; 38.
DR MINT; P47985; -.
DR STRING; 9606.ENSP00000306397; -.
DR DrugBank; DB07763; (5S)-3-ANILINO-5-(2,4-DIFLUOROPHENYL)-5-METHYL-1,3-OXAZOLIDINE-2,4-DIONE.
DR DrugBank; DB07778; (S)-famoxadone.
DR DrugBank; DB04141; 2-Hexyloxy-6-Hydroxymethyl-Tetrahydro-Pyran-3,4,5-Triol.
DR DrugBank; DB08453; 2-Nonyl-4-quinolinol 1-oxide.
DR DrugBank; DB07636; 5-Heptyl-6-hydroxy-1,3-benzothiazole-4,7-dione.
DR DrugBank; DB04799; 6-Hydroxy-5-undecyl-4,7-benzothiazoledione.
DR DrugBank; DB07401; Azoxystrobin.
DR DrugBank; DB08330; METHYL (2Z)-3-METHOXY-2-{2-[(E)-2-PHENYLVINYL]PHENYL}ACRYLATE.
DR DrugBank; DB08690; Ubiquinone Q2.
DR iPTMnet; P47985; -.
DR PhosphoSitePlus; P47985; -.
DR SwissPalm; P47985; -.
DR BioMuta; UQCRFS1; -.
DR DMDM; 143811471; -.
DR OGP; P47985; -.
DR REPRODUCTION-2DPAGE; IPI00026964; -.
DR SWISS-2DPAGE; P47985; -.
DR UCD-2DPAGE; P47985; -.
DR EPD; P47985; -.
DR jPOST; P47985; -.
DR MassIVE; P47985; -.
DR MaxQB; P47985; -.
DR PaxDb; P47985; -.
DR PeptideAtlas; P47985; -.
DR PRIDE; P47985; -.
DR ProteomicsDB; 55828; -.
DR TopDownProteomics; P47985; -.
DR Antibodypedia; 28808; 302 antibodies from 34 providers.
DR DNASU; 7386; -.
DR Ensembl; ENST00000304863.6; ENSP00000306397.3; ENSG00000169021.6.
DR GeneID; 7386; -.
DR KEGG; hsa:7386; -.
DR MANE-Select; ENST00000304863.6; ENSP00000306397.3; NM_006003.3; NP_005994.2.
DR UCSC; uc002nsd.3; human.
DR CTD; 7386; -.
DR DisGeNET; 7386; -.
DR GeneCards; UQCRFS1; -.
DR HGNC; HGNC:12587; UQCRFS1.
DR HPA; ENSG00000169021; Tissue enhanced (skeletal muscle, tongue).
DR MalaCards; UQCRFS1; -.
DR MIM; 191327; gene.
DR MIM; 618775; phenotype.
DR neXtProt; NX_P47985; -.
DR OpenTargets; ENSG00000169021; -.
DR Orphanet; 1460; Isolated complex III deficiency.
DR PharmGKB; PA37218; -.
DR VEuPathDB; HostDB:ENSG00000169021; -.
DR eggNOG; KOG1671; Eukaryota.
DR GeneTree; ENSGT00390000001014; -.
DR HOGENOM; CLU_055690_0_1_1; -.
DR InParanoid; P47985; -.
DR OMA; DFLLNMS; -.
DR OrthoDB; 1174160at2759; -.
DR PhylomeDB; P47985; -.
DR TreeFam; TF105037; -.
DR BioCyc; MetaCyc:HS09867-MON; -.
DR PathwayCommons; P47985; -.
DR Reactome; R-HSA-611105; Respiratory electron transport.
DR SignaLink; P47985; -.
DR SIGNOR; P47985; -.
DR BioGRID-ORCS; 7386; 512 hits in 1072 CRISPR screens.
DR ChiTaRS; UQCRFS1; human.
DR GeneWiki; UQCRFS1; -.
DR GenomeRNAi; 7386; -.
DR Pharos; P47985; Tbio.
DR PRO; PR:P47985; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; P47985; protein.
DR Bgee; ENSG00000169021; Expressed in gastrocnemius and 96 other tissues.
DR Genevisible; P47985; HS.
DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:ComplexPortal.
DR GO; GO:0005750; C:mitochondrial respiratory chain complex III; IDA:UniProtKB.
DR GO; GO:0005751; C:mitochondrial respiratory chain complex IV; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
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:0045333; P:cellular respiration; IC:ComplexPortal.
DR GO; GO:0006122; P:mitochondrial electron transport, ubiquinol to cytochrome c; IBA:GO_Central.
DR GO; GO:0034551; P:mitochondrial respiratory chain complex III assembly; IMP:UniProtKB.
DR GO; GO:0022904; P:respiratory electron transport chain; IMP:UniProtKB.
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; Direct protein sequencing; Disease variant;
KW Disulfide bond; Electron transport; Iron; Iron-sulfur; Membrane;
KW Metal-binding; Mitochondrion; Mitochondrion inner membrane;
KW Primary mitochondrial disease; Reference proteome; Respiratory chain;
KW Transit peptide; Translocase; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..78
FT /note="Cytochrome b-c1 complex subunit 9"
FT /evidence="ECO:0000269|PubMed:28673544"
FT /id="PRO_0000307241"
FT CHAIN 79..274
FT /note="Cytochrome b-c1 complex subunit Rieske,
FT mitochondrial"
FT /id="PRO_0000030664"
FT TOPO_DOM 79..103
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000269|PubMed:28844695"
FT TRANSMEM 104..140
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:28844695"
FT TOPO_DOM 141..274
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000269|PubMed:28844695"
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"
FT VARIANT 6
FT /note="S -> A (in dbSNP:rs8100724)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:2158323,
FT ECO:0000269|PubMed:7721092"
FT /id="VAR_051863"
FT VARIANT 14
FT /note="V -> D (in MC3DN10; loss of localization to
FT mitochondrial inner membrane; the mutant protein is
FT distributed over the entire cytosol and in the nucleus;
FT dbSNP:rs1568346416)"
FT /evidence="ECO:0000269|PubMed:31883641"
FT /id="VAR_083879"
FT VARIANT 204..274
FT /note="Missing (in MC3DN10; decreased protein abundance)"
FT /evidence="ECO:0000269|PubMed:31883641"
FT /id="VAR_083880"
FT CONFLICT 73
FT /note="P -> H (in Ref. 5; AAH67832)"
FT /evidence="ECO:0000305"
FT HELIX 4..6
FT /evidence="ECO:0007829|PDB:5XTE"
FT STRAND 14..19
FT /evidence="ECO:0007829|PDB:5XTE"
FT TURN 31..33
FT /evidence="ECO:0007829|PDB:5XTE"
FT STRAND 34..36
FT /evidence="ECO:0007829|PDB:5XTE"
FT TURN 89..91
FT /evidence="ECO:0007829|PDB:5XTE"
FT HELIX 94..96
FT /evidence="ECO:0007829|PDB:5XTE"
FT STRAND 97..101
FT /evidence="ECO:0007829|PDB:5XTE"
FT HELIX 104..141
FT /evidence="ECO:0007829|PDB:5XTE"
FT HELIX 144..149
FT /evidence="ECO:0007829|PDB:5XTE"
FT STRAND 164..169
FT /evidence="ECO:0007829|PDB:5XTE"
FT STRAND 172..178
FT /evidence="ECO:0007829|PDB:5XTE"
FT HELIX 181..189
FT /evidence="ECO:0007829|PDB:5XTE"
FT TURN 192..194
FT /evidence="ECO:0007829|PDB:5XTE"
FT STRAND 195..197
FT /evidence="ECO:0007829|PDB:5XTE"
FT HELIX 201..204
FT /evidence="ECO:0007829|PDB:5XTE"
FT STRAND 210..216
FT /evidence="ECO:0007829|PDB:5XTE"
FT TURN 218..220
FT /evidence="ECO:0007829|PDB:5XTE"
FT STRAND 225..227
FT /evidence="ECO:0007829|PDB:5XTE"
FT STRAND 232..235
FT /evidence="ECO:0007829|PDB:5XTE"
FT TURN 237..239
FT /evidence="ECO:0007829|PDB:5XTE"
FT STRAND 242..244
FT /evidence="ECO:0007829|PDB:5XTE"
FT STRAND 249..253
FT /evidence="ECO:0007829|PDB:5XTE"
FT STRAND 263..265
FT /evidence="ECO:0007829|PDB:5XTE"
FT STRAND 270..273
FT /evidence="ECO:0007829|PDB:5XTE"
SQ SEQUENCE 274 AA; 29668 MW; 8DB51634DEB039B0 CRC64;
MLSVASRSGP FAPVLSATSR GVAGALRPLV QATVPATPEQ PVLDLKRPFL SRESLSGQAV
RRPLVASVGL NVPASVCYSH TDIKVPDFSE YRRLEVLDST KSSRESSEAR KGFSYLVTGV
TTVGVAYAAK NAVTQFVSSM SASADVLALA KIEIKLSDIP EGKNMAFKWR GKPLFVRHRT
QKEIEQEAAV ELSQLRDPQH DLDRVKKPEW VILIGVCTHL GCVPIANAGD FGGYYCPCHG
SHYDASGRIR LGPAPLNLEV PTYEFTSDDM VIVG
