Reviewed, UniProtKB/Swiss-Prot P38071 (ETR1_YEAST)

Names and origin

Protein names

Recommended name:
    Enoyl-[acyl-carrier protein] reductase [NADPH, B-specific], mitochondrial
    EC=1.3.1.10
Alternative name(s):
    Trans-2-enoyl-CoA reductase
    EC=1.3.1.38
    Mitochondrial respiratory function protein 1

Gene names

Name:	ETR1
Synonyms:	MRF1, MRF1'
Ordered Locus Names:	YBR026C
ORF Names:	YBR0310

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	380 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	Required for respiration and the maintenance of the mitochondrial compartment. May have a role in the mitochondrial synthesis of fatty acids.
Catalytic activity	Acyl-[acyl-carrier-protein] + NADP(+) = trans-2,3-dehydroacyl-[acyl-carrier-protein] + NADPH. Acyl-CoA + NADP(+) = trans-2,3-dehydroacyl-CoA + NADPH.
Subunit structure	Homodimer or in a complex with other proteins. Interacts with ARS1.
Subcellular location	Mitochondrion matrix.
Miscellaneous	Present with 1560 molecules/cell in log phase SD medium.
Sequence similarities	Belongs to the zinc-containing alcohol dehydrogenase family. Quinone oxidoreductase subfamily.
Caution	Was originally (Ref.1) thought to be a nuclear protein involved in transcriptional regulation of genes required for the functional assembly of mitochondrial respiratory proteins. This was later proven not to be the case (Ref.6).

Ontologies

Keywords
Biological process	Fatty acid biosynthesis Lipid synthesis
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	DNA-binding NADP
Molecular function	Oxidoreductase
PTM	Phosphoprotein
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	aerobic respiration Ref.6 Inferred from mutant phenotype. Source: SGD fatty acid biosynthetic process Ref.6 Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	DNA binding Inferred from electronic annotation. Source: UniProtKB-KW enoyl-[acyl-carrier-protein] reductase (NADPH, B-specific) activity Inferred from electronic annotation. Source: EC trans-2-enoyl-CoA reductase (NADPH) activity Inferred from electronic annotation. Source: EC zinc ion binding 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 – 9	9	Mitochondrion
	Chain	10 – 380	371	Enoyl-[acyl-carrier protein] reductase [NADPH, B-specific], mitochondrial		PRO_0000160924
Amino acid modifications
	Modified residue	135	1	Phosphoserine
	Modified residue	339	1	Phosphoserine
Experimental info
	Mutagenesis	73	1	Y → N: 0.1% of catalytic activity. No specific ARS1 binding
	Sequence conflict	24	1	I → T in AAS56198. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	P38071-1 [UniParc]. Last modified October 17, 2006. Version 3. Checksum: 9795013283C3E9F8	FASTA	380	42,067
	10 20 30 40 50 60 MLPTFKRYMS SSAHQIPKHF KSLIYSTHEV EDCTKVLSVK NYTPKQDLSQ SIVLKTLAFP 70 80 90 100 110 120 INPSDINQLQ GVYPSRPEKT YDYSTDEPAA IAGNEGVFEV VSLPSGSSKG DLKLGDRVIP 130 140 150 160 170 180 LQANQGTWSN YRVFSSSSDL IKVNDLDLFS AATVSVNGCT GFQLVSDYID WNSNGNEWII 190 200 210 220 230 240 QNAGTSSVSK IVTQVAKAKG IKTLSVIRDR DNFDEVAKVL EDKYGATKVI SESQNNDKTF 250 260 270 280 290 300 AKEVLSKILG ENARVRLALN SVGGKSSASI ARKLENNALM LTYGGMSKQP VTLPTSLHIF 310 320 330 340 350 360 KGLTSKGYWV TEKNKKNPQS KIDTISDFIK MYNYGHIISP RDEIETLTWN TNTTTDEQLL 370 380 ELVKKGITGK GKKKMVVLEW

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A protein which binds preferentially to single-stranded core sequence of autonomously replicating sequence is essential for respiratory function in mitochondrial of Saccharomyces cerevisiae." Yamazoe M., Shirahige K., Rashid M.B., Kaneko Y., Nakayama T., Ogasawara N., Yoshikawa H. J. Biol. Chem. 269:15244-15252(1994) [PubMed: 8195160] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 10-25. Strain: ATCC 26786 / X2180-1A.
[2]	"The complete sequence of a 33 kb fragment on the right arm of chromosome II from Saccharomyces cerevisiae reveals 16 open reading frames, including ten new open reading frames, five previously identified genes and a homologue of the SCO1 gene." Smits P.H.M., de Haan M., Maat C., Grivell L.A. Yeast 10:S75-S80(1994) [PubMed: 8091864] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[3]	"Complete DNA sequence of yeast chromosome II." Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C., Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M., Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M., Cziepluch C. , Demolis N., Delaveau T., Doignon F., Domdey H., Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D., Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N., Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J., Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C., Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P., Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y., Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F., Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E., Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M., Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B., Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L., Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M., Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S., Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K., Mewes H.-W., Kleine K. EMBO J. 13:5795-5809(1994) [PubMed: 7813418] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[4]	"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae." Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J. Genome Res. 17:536-543(2007) [PubMed: 17322287] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[5]	"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: SUBCELLULAR LOCATION.
[6]	"Candida tropicalis Etr1p and Saccharomyces cerevisiae Ybr026p (Mrf1'p), 2-enoyl thioester reductases essential for mitochondrial respiratory competence." Torkko J.M., Koivuranta K.T., Miinalainen I.J., Yagi A.I., Schmitz W., Kastaniotis A.J., Airenne T.T., Gurvitz A., Hiltunen K.J. Mol. Cell. Biol. 21:6243-6253(2001) [PubMed: 11509667] [Abstract] Cited for: FUNCTION, SUBUNIT, SUBCELLULAR LOCATION.
[7]	"Structure-function analysis of enoyl thioester reductase involved in mitochondrial maintenance." Airenne T.T., Torkko J.M., Van den plas S., Sormunen R.T., Kastaniotis A.J., Wierenga R.K., Hiltunen J.K. J. Mol. Biol. 327:47-59(2003) [PubMed: 12614607] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF TYR-73.
[8]	"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].
[9]	"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.
[10]	"A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-135 AND SER-339, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	D26606 Genomic DNA. Translation: BAA05651.1. Z35895 Genomic DNA. Translation: CAA84968.1. X76078 Genomic DNA. Translation: CAA53683.1. AY557872 Genomic DNA. Translation: AAS56198.1.
RefSeq	NP_009582.1.
3D structure databases
HSSP	HSSP built from PDB template 1GYR based on UniProtKB Q8WZM3.
ModBase	Search...
Protein-protein interaction databases
IntAct	P38071.
Proteomic databases
PeptideAtlas	P38071.
Genome annotation databases
Ensembl	YBR026C. Saccharomyces cerevisiae. [Contig view]
GeneID	852314.
GenomeReviews	Gene locus YBR026C in contig Y13134_GR.
KEGG	sce:YBR026C.
NMPDR	fig|4932.3.peg.277.
Organism-specific databases
CYGD	YBR026c.
SGD	S000000230. ETR1.
Yeast-GFP	Search...
Phylogenomic databases
HOGENOM	P38071.
Gene expression databases
GermOnline	YBR026C. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR013154. AlcDHase_GroES-like. IPR002085. AlcDHase_SF_Zn. IPR016040. NAD(P)-bd. [Graphical view]
Gene3D	G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
PANTHER	PTHR11695. ADH_Sf_Zn. 1 hit.
Pfam	PF08240. ADH_N. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
LinkHub	P38071.
NextBio	971002.

Entry information

Entry name

ETR1_YEAST

Accession

Primary (citable) accession number: P38071
Secondary accession number(s): Q6Q5P2

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1994
Last sequence update:	October 17, 2006
Last modified:	November 25, 2008
This is version 76 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)