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Protein

Cytochrome b-c1 complex subunit Rieske, mitochondrial

Gene

UQCRFS1

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 (By similarity). Incorporation of UQCRFS1 is the penultimate step in complex III assembly (By similarity).By similarity
Cytochrome b-c1 complex subunit 9: 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:2996928, PubMed:8386158). UQCRFS1 undergoes proteolytic processing once it is incorporated in the complex III dimer (PubMed:2996928, PubMed:8386158). One of the fragments, called subunit 9, corresponds to the transit peptide (PubMed:2996928, PubMed:8386158). 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 (By similarity). It is unsure whether the UQCRFS1 fragments, including subunit 9, are structural subunits (By similarity).By similarity2 Publications

Miscellaneous

The Rieske protein is a high potential 2Fe-2S protein.

Catalytic activityi

Quinol + 2 ferricytochrome c = quinone + 2 ferrocytochrome c + 2 H+.

Cofactori

[2Fe-2S] clusterNote: 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).PROSITE-ProRule annotationBy similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi217Iron-sulfur (2Fe-2S)1
Metal bindingi219Iron-sulfur (2Fe-2S); via pros nitrogen1
Metal bindingi236Iron-sulfur (2Fe-2S)1
Metal bindingi239Iron-sulfur (2Fe-2S); via pros nitrogen1

GO - Molecular functioni

Keywordsi

Molecular functionOxidoreductase
Biological processElectron transport, Respiratory chain, Transport
Ligand2Fe-2S, Iron, Iron-sulfur, Metal-binding

Protein family/group databases

TCDBi3.D.3.2.1. the proton-translocating quinol:cytochrome c reductase (qcr) superfamily.

Names & Taxonomyi

Protein namesi
Recommended name:
Cytochrome b-c1 complex subunit Rieske, mitochondrial (EC:1.10.2.2)
Alternative name(s):
Complex III subunit 5
Cytochrome b-c1 complex subunit 5
Rieske iron-sulfur protein
Short name:
RISP
Rieske protein UQCRFS1
Ubiquinol-cytochrome c reductase iron-sulfur subunit
Cleaved into the following chain:
Cytochrome b-c1 complex subunit 91 Publication
Short name:
Su91 Publication
Short name:
Subunit 91 Publication
Alternative name(s):
8 kDa subunit 91 Publication
Complex III subunit IX
Cytochrome b-c1 complex subunit 11
Ubiquinol-cytochrome c reductase 8 kDa protein1 Publication
Gene namesi
Name:UQCRFS1
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Unplaced

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transmembranei103 – 140HelicalAdd BLAST38

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion inner membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 78Mitochondrion2 PublicationsAdd BLAST78
ChainiPRO_00000306591 – 78Cytochrome b-c1 complex subunit 91 PublicationAdd BLAST78
ChainiPRO_000003066079 – 274Cytochrome b-c1 complex subunit Rieske, mitochondrialAdd BLAST196

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi222 ↔ 238PROSITE-ProRule annotation1 Publication

Post-translational modificationi

Proteolytic processing is necessary for the correct insertion of UQCRFS1 in the complex III dimer (By similarity). Several fragments are generated during UQCRFS1 insertion, most probably due to the endogenous matrix-processing peptidase (MPP) activity (By similarity). The action of the protease is also necessary for the clearance of the UQCRFS1 fragments (By similarity).By similarity

Keywords - PTMi

Disulfide bond

Proteomic databases

PeptideAtlasiP13272.
PRIDEiP13272.

Interactioni

Subunit structurei

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 (By similarity).By similarity

Protein-protein interaction databases

CORUMiP13272.
DIPiDIP-38974N.
IntActiP13272. 3 interactors.

Structurei

Secondary structure

1274
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi5 – 7Combined sources3
Beta strandi8 – 10Combined sources3
Beta strandi12 – 19Combined sources8
Beta strandi22 – 24Combined sources3
Beta strandi27 – 29Combined sources3
Helixi30 – 33Combined sources4
Beta strandi34 – 36Combined sources3
Beta strandi43 – 45Combined sources3
Helixi52 – 55Combined sources4
Beta strandi61 – 63Combined sources3
Beta strandi65 – 72Combined sources8
Beta strandi75 – 77Combined sources3
Helixi80 – 82Combined sources3
Turni89 – 91Combined sources3
Helixi94 – 96Combined sources3
Beta strandi99 – 101Combined sources3
Helixi104 – 140Combined sources37
Helixi144 – 147Combined sources4
Beta strandi150 – 155Combined sources6
Helixi156 – 158Combined sources3
Beta strandi161 – 163Combined sources3
Beta strandi164 – 169Combined sources6
Beta strandi172 – 178Combined sources7
Helixi181 – 188Combined sources8
Helixi192 – 194Combined sources3
Beta strandi195 – 197Combined sources3
Helixi201 – 203Combined sources3
Beta strandi205 – 207Combined sources3
Beta strandi210 – 214Combined sources5
Turni218 – 220Combined sources3
Beta strandi225 – 227Combined sources3
Turni229 – 231Combined sources3
Beta strandi232 – 236Combined sources5
Turni237 – 240Combined sources4
Beta strandi241 – 244Combined sources4
Beta strandi245 – 247Combined sources3
Beta strandi249 – 253Combined sources5
Beta strandi263 – 273Combined sources11

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1BCCX-ray3.16A192-195[»]
E79-274[»]
1BE3X-ray3.00E79-274[»]
I1-78[»]
1BGYX-ray3.00E/Q79-274[»]
I/U1-78[»]
1L0LX-ray2.35E79-274[»]
I1-78[»]
1L0NX-ray2.60E79-274[»]
I1-78[»]
1NTKX-ray2.60E79-274[»]
I1-57[»]
1NTMX-ray2.40E79-274[»]
I1-57[»]
1NTZX-ray2.60E79-274[»]
I1-57[»]
1NU1X-ray3.20E79-274[»]
I1-57[»]
1PP9X-ray2.10E/R79-274[»]
I/V1-78[»]
1PPJX-ray2.10E/R79-274[»]
I/V1-78[»]
1QCRX-ray2.70E79-274[»]
I21-48[»]
1RIEX-ray1.50A146-274[»]
1SQBX-ray2.69E79-274[»]
I1-78[»]
1SQPX-ray2.70E79-274[»]
I1-78[»]
1SQQX-ray3.00E79-274[»]
I1-78[»]
1SQVX-ray2.85E79-274[»]
I1-78[»]
1SQXX-ray2.60E79-274[»]
I1-78[»]
2A06X-ray2.10E/R79-274[»]
I/V1-78[»]
2FYUX-ray2.26E79-274[»]
I1-78[»]
2YBBelectron microscopy19.00E/e79-274[»]
I/i14-78[»]
4D6TX-ray3.57E/I/R/V1-274[»]
4D6UX-ray4.09E/I/R/V1-274[»]
5GPNelectron microscopy5.40I/U1-78[»]
5KLVX-ray2.65E79-274[»]
I1-78[»]
5LUFelectron microscopy9.10e/q79-274[»]
i/u1-78[»]
5NMIX-ray3.50E/I/R/V1-274[»]
ProteinModelPortaliP13272.
SMRiP13272.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP13272.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini187 – 272RieskePROSITE-ProRule annotationAdd BLAST86

Keywords - Domaini

Transit peptide, Transmembrane, Transmembrane helix

Phylogenomic databases

HOVERGENiHBG001040.
InParanoidiP13272.
KOiK00411.

Family and domain databases

Gene3Di1.20.5.270. 1 hit.
2.102.10.10. 1 hit.
InterProiView protein in InterPro
IPR037008. bc1_Rieske_TM_sf.
IPR011070. Globular_prot_asu/bsu.
IPR017941. Rieske_2Fe-2S.
IPR036922. Rieske_2Fe-2S_sf.
IPR014349. Rieske_Fe-S_prot.
IPR005805. Rieske_Fe-S_prot_C.
IPR004192. Rieske_TM.
IPR015248. Ubiqinol_cyt_c_Rdtase_N.
IPR006317. Ubiquinol_cyt_c_Rdtase_Fe-S-su.
PANTHERiPTHR10134. PTHR10134. 1 hit.
PfamiView protein in Pfam
PF00355. Rieske. 1 hit.
PF09165. Ubiq-Cytc-red_N. 1 hit.
PF02921. UCR_TM. 1 hit.
PRINTSiPR00162. RIESKE.
SUPFAMiSSF50022. SSF50022. 1 hit.
SSF56568. SSF56568. 1 hit.
TIGRFAMsiTIGR01416. Rieske_proteo. 1 hit.
PROSITEiView protein in PROSITE
PS51296. RIESKE. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P13272-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLSVAARSGP FAPVLSATSR GVAGALRPLV QAAVPATSES PVLDLKRSVL
60 70 80 90 100
CRESLRGQAA GRPLVASVSL NVPASVRYSH TDIKVPDFSD YRRPEVLDST
110 120 130 140 150
KSSKESSEAR KGFSYLVTAT TTVGVAYAAK NVVSQFVSSM SASADVLAMS
160 170 180 190 200
KIEIKLSDIP EGKNMAFKWR GKPLFVRHRT KKEIDQEAAV EVSQLRDPQH
210 220 230 240 250
DLERVKKPEW VILIGVCTHL GCVPIANAGD FGGYYCPCHG SHYDASGRIR
260 270
KGPAPLNLEV PSYEFTSDDM VIVG
Length:274
Mass (Da):29,547
Last modified:February 1, 1996 - v3
Checksum:i7C5FC17D2A0DD1C9
GO

Sequence cautioni

The sequence AAA30515 differs from that shown. Reason: Frameshift at several positions.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti150S → A AA sequence (PubMed:3036596).Curated1
Sequence conflicti269D → G AA sequence (PubMed:3036596).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M34336 mRNA. Translation: AAA30515.1. Sequence problems.
S58789 mRNA. Translation: AAB26197.1.
BC115994 mRNA. Translation: AAI15995.1.
BC133620 mRNA. Translation: AAI33621.1.
BC133632 mRNA. Translation: AAI33633.1.
PIRiA46063. A34660.
RefSeqiNP_777238.1. NM_174813.2.
UniGeneiBt.265.

Genome annotation databases

GeneIDi287020.
KEGGibta:287020.

Similar proteinsi

Entry informationi

Entry nameiUCRI_BOVIN
AccessioniPrimary (citable) accession number: P13272
Secondary accession number(s): A3KN53, P07588, Q1LZH6
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: February 1, 1996
Last modified: November 22, 2017
This is version 162 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Caution

Several peptides are generated during UQCRFS1 insertion. 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.By similarity

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references