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Cytochrome b-c1 complex subunit Rieske, mitochondrial (EC 1.10.2.2) (Complex III subunit 5) (Cytochrome b-c1 complex subunit 5) (Rieske iron-sulfur protein) (RISP) (Rieske protein UQCRFS1) (Ubiquinol-cytochrome c reductase iron-sulfur subunit) [Cleaved into: Cytochrome b-c1 complex subunit 9 (Su9) (Subunit 9) (8 kDa subunit 9) (Complex III subunit IX) (Cytochrome b-c1 complex subunit 11) (Ubiquinol-cytochrome c reductase 8 kDa protein)]

 UCRI_MOUSE              Reviewed;         274 AA.
Q9CR68; Q5SVV1;
13-SEP-2004, integrated into UniProtKB/Swiss-Prot.
01-JUN-2001, sequence version 1.
12-SEP-2018, entry version 137.
RecName: Full=Cytochrome b-c1 complex subunit Rieske, mitochondrial;
EC=1.10.2.2;
AltName: Full=Complex III subunit 5;
AltName: Full=Cytochrome b-c1 complex subunit 5;
AltName: Full=Rieske iron-sulfur protein;
Short=RISP;
AltName: Full=Rieske protein UQCRFS1 {ECO:0000305};
AltName: Full=Ubiquinol-cytochrome c reductase iron-sulfur subunit;
Contains:
RecName: Full=Cytochrome b-c1 complex subunit 9 {ECO:0000250|UniProtKB:P13272};
Short=Su9 {ECO:0000250|UniProtKB:P13272};
Short=Subunit 9 {ECO:0000250|UniProtKB:P13272};
AltName: Full=8 kDa subunit 9 {ECO:0000250|UniProtKB:P13272};
AltName: Full=Complex III subunit IX;
AltName: Full=Cytochrome b-c1 complex subunit 11;
AltName: Full=Ubiquinol-cytochrome c reductase 8 kDa protein {ECO:0000250|UniProtKB:P13272};
Flags: Precursor;
Name=Uqcrfs1 {ECO:0000312|MGI:MGI:1913944};
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Bone marrow, and Liver;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N; TISSUE=Mammary tumor;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
PROTEIN SEQUENCE OF 8-46; 85-92; 94-101; 131-151; 156-163; 171-177 AND
183-204, AND IDENTIFICATION BY MASS SPECTROMETRY.
STRAIN=C57BL/6J; TISSUE=Brain;
Lubec G., Kang S.U.;
Submitted (APR-2007) to UniProtKB.
[5]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[6]
PTM, IDENTIFICATION BY MASS SPECTROMETRY, SUBUNIT, INTERACTION WITH
TTC19, AND FUNCTION.
PubMed=28673544; DOI=10.1016/j.molcel.2017.06.001;
Bottani E., Cerutti R., Harbour M.E., Ravaglia S., Dogan S.A.,
Giordano C., Fearnley I.M., D'Amati G., Viscomi C.,
Fernandez-Vizarra E., Zeviani M.;
"TTC19 plays a husbandry role on UQCRFS1 turnover in the biogenesis of
mitochondrial respiratory complex III.";
Mol. Cell 67:96-105(2017).
-!- FUNCTION: Cytochrome b-c1 complex subunit Rieske, mitochondrial:
Component of the mitochondrial ubiquinol-cytochrome c reductase
complex dimer (complex III dimer), which is a respiratory chain
that generates an electrochemical potential coupled to ATP
synthesis (PubMed:28673544). Incorporation of UQCRFS1 is the
penultimate step in complex III assembly (By similarity).
{ECO:0000250|UniProtKB:P47985, ECO:0000269|PubMed:28673544}.
-!- FUNCTION: Cytochrome b-c1 complex subunit 9: Possible component of
the mitochondrial ubiquinol-cytochrome c reductase complex dimer
(complex III dimer), which is a respiratory chain that generates
an electrochemical potential coupled to ATP synthesis
(PubMed:28673544). UQCRFS1 undergoes proteolytic processing once
it is incorporated in the complex III dimer, including this
fragment, called subunit 9, which corresponds to the transit
peptide (PubMed:28673544). The proteolytic processing is necessary
for the correct insertion of UQCRFS1 in the complex III dimer, but
the persistence of UQCRFS1-derived fragments may prevent newly
imported UQCRFS1 to be processed and assembled into complex III
and is detrimental for the complex III structure and function
(PubMed:28673544). It is therefore unsure whether the UQCRFS1
fragments, including this fragment, are structural subunits
(PubMed:28673544). {ECO:0000269|PubMed:28673544}.
-!- CATALYTIC ACTIVITY: Quinol + 2 ferricytochrome c = quinone + 2
ferrocytochrome c + 2 H(+).
-!- COFACTOR:
Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:49601;
Evidence={ECO:0000255|PROSITE-ProRule:PRU00628};
Note=Binds 1 [2Fe-2S] cluster per subunit. Fe-S cluster delivery
to the Rieske protein is mediated by components of the iron sulfur
(Fe-S) cluster assembly machinery that reside in the mitochondrial
matrix (including HSC20 and LYRM7) (By similarity).
{ECO:0000250|UniProtKB:P47985, ECO:0000255|PROSITE-
ProRule:PRU00628};
-!- SUBUNIT: Binds to the mitochondrial respiratory complex III dimer.
The monomeric module of the mitochondrial respiratory complex III
contains 11 subunits: 3 respiratory subunits involved in its
catalytic activity (cytochrome b, cytochrome c1 and Rieske protein
UQCRFS1), 2 core proteins (UQCRC1/QCR1 and UQCRC2/QCR2) and 6 low-
molecular weight proteins (UQCRH/QCR6, UQCRB/QCR7, UQCRQ/QCR8,
UQCR10/QCR9, UQCR11/QCR10 and subunit 9, the cleavage product of
Rieske protein UQCRFS1) (By similarity). Incorporation of the
Rieske protein UQCRFS1 is the penultimate step in complex III
assembly (By similarity). Interacts with TTC19, which is involved
in the clearance of UQCRFS1 fragments (PubMed:28673544).
{ECO:0000250|UniProtKB:P13272, ECO:0000250|UniProtKB:P47985,
ECO:0000269|PubMed:28673544}.
-!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
{ECO:0000250|UniProtKB:Q5ZLR5}; Single-pass membrane protein
{ECO:0000250|UniProtKB:Q5ZLR5}.
-!- PTM: Proteolytic processing is necessary for the correct insertion
of UQCRFS1 in the complex III dimer (PubMed:28673544). Several
fragments are generated during UQCRFS1 insertion, most probably
due to the endogenous matrix-processing peptidase (MPP) activity
(PubMed:28673544). The action of the protease is also necessary
for the clearance of the UQCRFS1 fragments (PubMed:28673544).
{ECO:0000269|PubMed:28673544}.
-!- MISCELLANEOUS: The Rieske protein is a high potential 2Fe-2S
protein.
-!- CAUTION: Several peptides are generated during UQCRFS1 insertion
(PubMed:28673544). According to some authors, the identification
of the transit peptide as the subunit 9, does not necessary imply
that it must be considered as a structural subunit of the complex
III dimer as additional fragments from UQCRFS1 are also present
(PubMed:28673544). {ECO:0000269|PubMed:28673544}.
-----------------------------------------------------------------------
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EMBL; AK003966; BAB23097.1; -; mRNA.
EMBL; AK012180; BAB28081.1; -; mRNA.
EMBL; AK014470; BAB29374.1; -; mRNA.
EMBL; AK153139; BAE31751.1; -; mRNA.
EMBL; AK152391; BAE31179.1; -; mRNA.
EMBL; AL611944; CAI24872.1; -; Genomic_DNA.
EMBL; BC019934; AAH19934.1; -; mRNA.
CCDS; CCDS26416.1; -.
RefSeq; NP_079986.1; NM_025710.2.
UniGene; Mm.181933; -.
ProteinModelPortal; Q9CR68; -.
SMR; Q9CR68; -.
BioGrid; 211651; 2.
ComplexPortal; CPX-563; Mitochondrial respiratory chain complex III.
CORUM; Q9CR68; -.
IntAct; Q9CR68; 7.
MINT; Q9CR68; -.
STRING; 10090.ENSMUSP00000045284; -.
iPTMnet; Q9CR68; -.
PhosphoSitePlus; Q9CR68; -.
SwissPalm; Q9CR68; -.
EPD; Q9CR68; -.
MaxQB; Q9CR68; -.
PaxDb; Q9CR68; -.
PeptideAtlas; Q9CR68; -.
PRIDE; Q9CR68; -.
Ensembl; ENSMUST00000042834; ENSMUSP00000045284; ENSMUSG00000038462.
GeneID; 66694; -.
KEGG; mmu:66694; -.
UCSC; uc007pyv.2; mouse.
CTD; 7386; -.
MGI; MGI:1913944; Uqcrfs1.
eggNOG; KOG1671; Eukaryota.
eggNOG; COG0723; LUCA.
GeneTree; ENSGT00390000001014; -.
HOGENOM; HOG000255193; -.
HOVERGEN; HBG001040; -.
InParanoid; Q9CR68; -.
KO; K00411; -.
OMA; ERKAFSY; -.
OrthoDB; EOG091G0MOP; -.
PhylomeDB; Q9CR68; -.
TreeFam; TF105037; -.
PRO; PR:Q9CR68; -.
Proteomes; UP000000589; Chromosome 13.
Bgee; ENSMUSG00000038462; Expressed in 271 organ(s), highest expression level in brown adipose tissue.
Genevisible; Q9CR68; MM.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005743; C:mitochondrial inner membrane; HDA:MGI.
GO; GO:0031966; C:mitochondrial membrane; ISO:MGI.
GO; GO:0005750; C:mitochondrial respiratory chain complex III; ISO:MGI.
GO; GO:0005751; C:mitochondrial respiratory chain complex IV; ISO:MGI.
GO; GO:0005739; C:mitochondrion; IDA:MGI.
GO; GO:0043209; C:myelin sheath; IDA:UniProtKB.
GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
GO; GO:0008121; F:ubiquinol-cytochrome-c reductase activity; IEA:UniProtKB-EC.
GO; GO:0046677; P:response to antibiotic; IEA:Ensembl.
GO; GO:0042493; P:response to drug; IEA:Ensembl.
GO; GO:0009725; P:response to hormone; IEA:Ensembl.
Gene3D; 1.20.5.270; -; 1.
Gene3D; 2.102.10.10; -; 1.
InterPro; IPR037008; bc1_Rieske_TM_sf.
InterPro; IPR011070; Globular_prot_asu/bsu.
InterPro; IPR017941; Rieske_2Fe-2S.
InterPro; IPR036922; Rieske_2Fe-2S_sf.
InterPro; IPR014349; Rieske_Fe-S_prot.
InterPro; IPR005805; Rieske_Fe-S_prot_C.
InterPro; IPR004192; Rieske_TM.
InterPro; IPR015248; Ubiqinol_cyt_c_Rdtase_N.
InterPro; IPR006317; Ubiquinol_cyt_c_Rdtase_Fe-S-su.
PANTHER; PTHR10134; PTHR10134; 1.
Pfam; PF00355; Rieske; 1.
Pfam; PF09165; Ubiq-Cytc-red_N; 1.
Pfam; PF02921; UCR_TM; 1.
PRINTS; PR00162; RIESKE.
SUPFAM; SSF50022; SSF50022; 1.
SUPFAM; SSF56568; SSF56568; 1.
TIGRFAMs; TIGR01416; Rieske_proteo; 1.
PROSITE; PS51296; RIESKE; 1.
1: Evidence at protein level;
2Fe-2S; Complete proteome; Direct protein sequencing; Disulfide bond;
Electron transport; Iron; Iron-sulfur; Membrane; Metal-binding;
Mitochondrion; Mitochondrion inner membrane; Oxidoreductase;
Reference proteome; Respiratory chain; Transit peptide; Transmembrane;
Transmembrane helix; Transport.
CHAIN 1 78 Cytochrome b-c1 complex subunit 9.
{ECO:0000269|PubMed:28673544}.
/FTId=PRO_0000307244.
TRANSIT 1 78 Mitochondrion.
{ECO:0000250|UniProtKB:P47985}.
CHAIN 79 274 Cytochrome b-c1 complex subunit Rieske,
mitochondrial.
/FTId=PRO_0000030667.
TRANSMEM 103 140 Helical. {ECO:0000250}.
DOMAIN 187 272 Rieske. {ECO:0000255|PROSITE-
ProRule:PRU00628}.
METAL 217 217 Iron-sulfur (2Fe-2S).
{ECO:0000255|PROSITE-ProRule:PRU00628}.
METAL 219 219 Iron-sulfur (2Fe-2S); via pros nitrogen.
{ECO:0000255|PROSITE-ProRule:PRU00628}.
METAL 236 236 Iron-sulfur (2Fe-2S).
{ECO:0000255|PROSITE-ProRule:PRU00628}.
METAL 239 239 Iron-sulfur (2Fe-2S); via pros nitrogen.
{ECO:0000255|PROSITE-ProRule:PRU00628}.
DISULFID 222 238 {ECO:0000255|PROSITE-ProRule:PRU00628}.
SEQUENCE 274 AA; 29368 MW; 17E55DE0BBD09961 CRC64;
MLSVAARSGP FAPVLSATSR GVAGALRPLL QGAVPAASEP PVLDVKRPFL CRESLSGQAA
ARPLVATVGL NVPASVRFSH TDVKVPDFSD YRRAEVLDST KSSKESSEAR KGFSYLVTAT
TTVGVAYAAK NVVSQFVSSM SASADVLAMS KIEIKLSDIP EGKNMAFKWR GKPLFVRHRT
KKEIDQEAAV EVSQLRDPQH DLDRVKKPEW VILIGVCTHL GCVPIANAGD FGGYYCPCHG
SHYDASGRIR KGPAPLNLEV PAYEFTSDDV VVVG


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