Q08822 (ETFD_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Probable electron transfer flavoprotein-ubiquinone oxidoreductase, mitochondrial
Short name=ETF-QO
Short name=ETF-ubiquinone oxidoreductase
EC=1.5.5.1

Alternative name(s):
Changed intracellular redox state protein 2
Electron-transferring-flavoprotein dehydrogenase
Short name=ETF dehydrogenase

Gene names

Name:	CIR2
Ordered Locus Names:	YOR356W

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	631 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Accepts electrons from ETF and reduces ubiquinone By similarity.
Catalytic activity	Reduced electron-transferring flavoprotein + ubiquinone = electron-transferring flavoprotein + ubiquinol.
Cofactor	Binds 1 4Fe-4S cluster By similarity. FAD By similarity.
Subcellular location	Mitochondrion inner membrane Ref.3 Ref.4 Ref.6 Ref.7.
Disruption phenotype	Displays higher growth rate and higher sensitivity to superoxide and heat stress, on nonfermentable carbon sources. Leads to decreased intracellular oxidation upon heat shock. Ref.8
Miscellaneous	Present with 3320 molecules/cell in log phase SD medium. Ref.5
Sequence similarities	Belongs to the ETF-QO/fixC family. Contains 1 4Fe-4S ferredoxin-type domain.

Ontologies

Keywords
Biological process	Electron transport Transport
Cellular component	Membrane Mitochondrion Mitochondrion inner membrane
Domain	Transit peptide
Ligand	4Fe-4S FAD Flavoprotein Iron Iron-sulfur Metal-binding Ubiquinone
Molecular function	Oxidoreductase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW transport Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	mitochondrial inner membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW electron-transferring-flavoprotein dehydrogenase activity Inferred from electronic annotation. Source: EC metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ECM4	P36156	1	EBI-6705,EBI-2042717

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – ?		Mitochondrion Potential
	Chain	? – 631		Probable electron transfer flavoprotein-ubiquinone oxidoreductase, mitochondrial		PRO_0000008667
Regions
	Domain	591 – 620	30	4Fe-4S ferredoxin-type
	Nucleotide binding	65 – 79	15	FAD Potential
Sites
	Metal binding	574	1	Iron-sulfur (4Fe-4S) Potential
	Metal binding	600	1	Iron-sulfur (4Fe-4S) Potential
	Metal binding	603	1	Iron-sulfur (4Fe-4S) Potential
	Metal binding	606	1	Iron-sulfur (4Fe-4S) Potential

Sequences

	Sequence		Length	Mass (Da)
	Q08822 [UniParc]. Last modified November 1, 1997. Version 1. Checksum: 7493F67093D88391	FASTA	631	69,634
	10 20 30 40 50 60 MIKFTNENLI RGIRMTISAK SRHLALGTDM TRKFSLSCRF LNKANLTEEE KELLNEPRAR 70 80 90 100 110 120 DYVDVCIVGG GPAGLATAIK LKQLDNSSGT GQLRVVVLEK SSVLGGQTVS GAILEPGVWK 130 140 150 160 170 180 ELFPDEKSDI GIPLPKELAT LVTKEHLKFL KGKWAISVPE PSQMINKGRN YIVSLNQVVG 190 200 210 220 230 240 YLGEKAEEVG VEVYPGIAVS DLIYDENNAV KGVITKDAGI SKSGKPKETF ERGMEFWARQ 250 260 270 280 290 300 TVLAEGCHGS LTKQALAKYD LRKGRQHQTY GLGIKEVWEV KPENFNKGFA AHTMGYPLTN 310 320 330 340 350 360 DVYGGGFQYH FGDGLVTVGL VVGLDYKNPY VSPYKEFQKM KHHPYYSKVL EGGKCIAYAA 370 380 390 400 410 420 RALNEGGLQS VPKLNFPGGV LVGASAGFMN VPKIKGTHTA MKSGLLAAES IFESIKGLPV 430 440 450 460 470 480 LEEVEDEDAK MAMFDKEATI NLESYESAFK ESSIYKELYE VRNIRPSFSG KLGGYGGMIY 490 500 510 520 530 540 SGIDSLILKG KVPWTLKFDE KNDGEILEPA SKYKPIEYPK PDGVISFDIL TSVSRTGTYH 550 560 570 580 590 600 DDDEPCHLRV PGQDMVKYAE RSFPVWKGVE SRFCPAGVYE FVKDEKSPVG TRLQINSQNC 610 620 630 IHCKTCDIKA PRQDITWKVP EGGDGPKYTL T

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XV." Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A., Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B., Dang V.-D. , de Haan M., Delius H., Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K. Nature 387:98-102(1997) [PubMed: 9169874] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[2]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[3]	"Yeast mitochondrial dehydrogenases are associated in a supramolecular complex." Grandier-Vazeille X., Bathany K., Chaignepain S., Camougrand N., Manon S., Schmitter J.-M. Biochemistry 40:9758-9769(2001) [PubMed: 11502169] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION.
[4]	"Global analysis of protein localization in budding yeast." Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K. Nature 425:686-691(2003) [PubMed: 14562095] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[5]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[6]	"The proteome of Saccharomyces cerevisiae mitochondria." Sickmann A., Reinders J., Wagner Y., Joppich C., Zahedi R.P., Meyer H.E., Schoenfisch B., Perschil I., Chacinska A., Guiard B., Rehling P., Pfanner N., Meisinger C. Proc. Natl. Acad. Sci. U.S.A. 100:13207-13212(2003) [PubMed: 14576278] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY. Strain: ATCC 76625 / YPH499.
[7]	"Toward the complete yeast mitochondrial proteome: multidimensional separation techniques for mitochondrial proteomics." Reinders J., Zahedi R.P., Pfanner N., Meisinger C., Sickmann A. J. Proteome Res. 5:1543-1554(2006) [PubMed: 16823961] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[8]	"The Saccharomyces cerevisiae genes, AIM45, YGR207c/CIR1 and YOR356w/CIR2, are involved in cellular redox state under stress conditions." Lopes J., Pinto M.J., Rodrigues A., Vasconcelos F., Oliveira R. Open Microbiol. J. 4:75-82(2010) [PubMed: 21253464] [Abstract] Cited for: DISRUPTION PHENOTYPE.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Z75264 Genomic DNA. Translation: CAA99685.1. BK006948 Genomic DNA. Translation: DAA11117.1.
PIR	S67268.
RefSeq	NP_015001.1. NM_001183776.1.
3D structure databases
ProteinModelPortal	Q08822.
SMR	Q08822. Positions 28-630.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-6685N.
IntAct	Q08822. 5 interactions.
MINT	MINT-617086.
STRING	Q08822.
Proteomic databases
PeptideAtlas	Q08822.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YOR356W; YOR356W; YOR356W.
GeneID	854538.
KEGG	sce:YOR356W.
NMPDR	fig|4932.3.peg.6120.
Organism-specific databases
CYGD	YOR356w.
SGD	S000005883. CIR2.
Phylogenomic databases
eggNOG	fuNOG04128.
GeneTree	EFGT00050000004409.
HOGENOM	HBG291987.
OMA	LKNSWVW.
OrthoDB	EOG4TXG16.
Gene expression databases
ArrayExpress	Q08822.
Genevestigator	Q08822.
GermOnline	YOR356W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR017896. 4Fe4S_Fe-S-bd. IPR007859. ETFD_OxRdtase. IPR006076. FAD-dep_OxRdtase. [Graphical view]
KO	K00311.
Pfam	PF01266. DAO. 1 hit. PF05187. ETF_QO. 1 hit. [Graphical view]
PROSITE	PS51379. 4FE4S_FER_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	976937.

Entry information

Entry name

ETFD_YEAST

Accession

Primary (citable) accession number: Q08822
Secondary accession number(s): D6W351

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1997
Last modified:	December 14, 2011
This is version 104 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program