Reviewed, UniProtKB/Swiss-Prot Q09154 (UCRI_SCHPO)

Names and origin

Protein names

Recommended name:
    Cytochrome b-c1 complex subunit Rieske, mitochondrial
    EC=1.10.2.2
Alternative name(s):
    Ubiquinol-cytochrome c reductase iron-sulfur subunit
    Rieske iron-sulfur protein
      Short name=RISP
    Complex III subunit 5

Gene names

Name:	rip1
ORF Names:	SPBC16H5.06

Organism

Schizosaccharomyces pombe (Fission yeast) [Complete proteome]

Taxonomic identifier

4896 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

Protein attributes

Sequence length	228 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is a respiratory chain that generates an electrochemical potential coupled to ATP synthesis.
Catalytic activity	QH(2) + 2 ferricytochrome c = Q + 2 ferrocytochrome c + 2 H(+).
Cofactor	Binds 1 2Fe-2S cluster per subunit By similarity.
Subunit structure	Fungal bc1 complex contains 10 subunits; 3 respiratory subunits, 2 core proteins and 5 low-molecular weight proteins By similarity.
Subcellular location	Mitochondrion inner membrane.
Miscellaneous	The Rieske protein is a high potential 2Fe-2S protein.
Sequence similarities	Contains 1 Rieske domain.

Ontologies

Keywords
Biological process	Electron transport Respiratory chain Transport
Cellular component	Membrane Mitochondrion Mitochondrion inner membrane
Domain	Transit peptide Transmembrane
Ligand	2Fe-2S Iron Iron-sulfur Metal-binding
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	mitochondrial electron transport, ubiquinol to cytochrome c Ref.1 Inferred from genetic interaction. Source: GeneDB_SPombe transport Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW mitochondrial respiratory chain complex III Ref.1 Inferred from genetic interaction. Source: GeneDB_SPombe
Molecular function	2 iron, 2 sulfur cluster binding Inferred from electronic annotation. Source: InterPro electron carrier activity Inferred from electronic annotation. Source: InterPro iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW ubiquinol-cytochrome-c reductase activity Ref.1 Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – ?		Mitochondrion Potential
	Chain	? – 228		Cytochrome b-c1 complex subunit Rieske, mitochondrial		PRO_0000030682
Regions
	Domain	139 – 227	89	Rieske
Sites
	Metal binding	172	1	Iron-sulfur (2Fe-2S) By similarity
	Metal binding	174	1	Iron-sulfur (2Fe-2S); via pros nitrogen By similarity
	Metal binding	191	1	Iron-sulfur (2Fe-2S) By similarity
	Metal binding	194	1	Iron-sulfur (2Fe-2S); via pros nitrogen By similarity
Amino acid modifications
	Disulfide bond	177 ↔ 193		By similarity
Experimental info
	Sequence conflict	183	1	A → R in AAC49359. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q09154-1 [UniParc]. Last modified January 11, 2001. Version 2. Checksum: C50CC8BA159E31B2	FASTA	228	24,740
	10 20 30 40 50 60 MLAKQFISKS LASSLRRLLP VSSTASSLKG SMMTIPKFTS IRTYTDSPEM PDFSEYQTKS 70 80 90 100 110 120 TGDRSRVISY AMVGTMGALT AAGAQATVHD FLASWSASAD VLAMSKAEVD LSKIPEGKNL 130 140 150 160 170 180 VVKWQGKPVF IRHRTPEEIQ EANSVDISTL RDPQADSDRV QKPEWLVMIG VCTHLGCVPI 190 200 210 220 GEAGDYGGWF CPCHGSHYDI SGRIRRGPAP LNLAIPAYTF EGSKIIIG

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Heterologous complementation of a Rieske iron-sulfur protein-deficient Saccharomyces cerevisiae by the Rip1 gene of Schizosaccharomyces pombe." Dirago J., Bruel C., Graham L.A., Slonimski P., Trumpower B.L. J. Biol. Chem. 271:15341-15345(1996) [PubMed: 8663290] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"The genome sequence of Schizosaccharomyces pombe." Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P. Nature 415:871-880(2002) [PubMed: 11859360] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 38366 / 972.

Cross-references

Sequence databases
EMBLGenBankDDBJ	U40480 mRNA. Translation: AAC49359.1. CU329671 Genomic DNA. Translation: CAA17904.1.
PIR	T39619.
RefSeq	NP_595941.1.
3D structure databases
HSSP	HSSP built from PDB template 1RIE based on UniProtKB P13272.
SMR	Q09154. Positions 51-228.
ModBase	Search...
Genome annotation databases
GeneID	2540075.
KEGG	spo:SPBC16H5.06.
NMPDR	fig|4896.1.peg.1807.
Organism-specific databases
GeneDB_Spombe	SPBC16H5.06.
Enzyme and pathway databases
BioCyc	SPOM-XXX-01:SPOM-XXX-01-004006-MON.
Gene expression databases
ArrayExpress	Q09154.
Family and domain databases
InterPro	IPR014349. Rieske. IPR005805. Rieske_C. IPR006317. Rieske_proteo. IPR005806. Rieske_reg. IPR004192. UCR_TM_region. [Graphical view]
PANTHER	PTHR10134. Rieske. 1 hit.
Pfam	PF00355. Rieske. 1 hit. PF02921. UCR_TM. 1 hit. [Graphical view]
PRINTS	PR00162. RIESKE.
TIGRFAMs	TIGR01416. Rieske_proteo. 1 hit.
PROSITE	PS51296. RIESKE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

UCRI_SCHPO

Accession

Primary (citable) accession number: Q09154
Secondary accession number(s): O42942

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	January 11, 2001
Last modified:	November 25, 2008
This is version 68 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)