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UniProtKB/Swiss-Prot entry P38071


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name ETR1_YEAST
Primary accession number P38071
Secondary accession number Q6Q5P2
Integrated into Swiss-Prot on October 1, 1994
Sequence was last modified on October 17, 2006 (Sequence version 3)
Annotations were last modified on    July 22, 2008 (Entry version 73)
Name and origin of the protein
Protein name Enoyl-[acyl-carrier protein] reductase [NADPH, B-specific], mitochondrial [Precursor]
Synonyms EC 1.3.1.10
Trans-2-enoyl-CoA reductase
EC 1.3.1.38
Mitochondrial respiratory function protein 1
Gene name
Name: ETR1
Synonyms: MRF1, MRF1'
OrderedLocusNames: YBR026C
ORFNames: YBR0310
From
Saccharomyces cerevisiae (Baker's yeast) [TaxID: 4932] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 10-25.
STRAIN=ATCC 26786 / X2180-1A;
PubMed=8195160 [NCBI, ExPASy, EBI, Israel, Japan]
Yamazoe M., Shirahige K., Rashid M.B., Kaneko Y., Nakayama T., Ogasawara N., Yoshikawa H.;
"A protein which binds preferentially to single-stranded core sequence of autonomously replicating sequence is essential for respiratory function in mitochondrial of Saccharomyces cerevisiae.";
J. Biol. Chem. 269:15244-15252(1994).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
DOI=10.1002/yea.320100010; PubMed=8091864 [NCBI, ExPASy, EBI, Israel, Japan]
Smits P.H.M., de Haan M., Maat C., Grivell L.A.;
"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.";
Yeast 10:S75-S80(1994).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=7813418 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Complete DNA sequence of yeast chromosome II.";
EMBO J. 13:5795-5809(1994).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
DOI=10.1101/gr.6037607; PubMed=17322287 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae.";
Genome Res. 17:536-543(2007).
[5]
SUBCELLULAR LOCATION.
DOI=10.1021/bi010277r; PubMed=11502169 [NCBI, ExPASy, EBI, Israel, Japan]
Grandier-Vazeille X., Bathany K., Chaignepain S., Camougrand N., Manon S., Schmitter J.-M.;
"Yeast mitochondrial dehydrogenases are associated in a supramolecular complex.";
Biochemistry 40:9758-9769(2001).
[6]
FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
DOI=10.1128/MCB.21.18.6243-6253.2001; PubMed=11509667 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Candida tropicalis Etr1p and Saccharomyces cerevisiae Ybr026p (Mrf1'p), 2-enoyl thioester reductases essential for mitochondrial respiratory competence.";
Mol. Cell. Biol. 21:6243-6253(2001).
[7]
FUNCTION, AND MUTAGENESIS OF TYR-73.
DOI=10.1016/S0022-2836(03)00038-X; PubMed=12614607 [NCBI, ExPASy, EBI, Israel, Japan]
Airenne T.T., Torkko J.M., Van den plas S., Sormunen R.T., Kastaniotis A.J., Wierenga R.K., Hiltunen J.K.;
"Structure-function analysis of enoyl thioester reductase involved in mitochondrial maintenance.";
J. Mol. Biol. 327:47-59(2003).
[8]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
DOI=10.1038/nature02046; PubMed=14562106 [NCBI, ExPASy, EBI, Israel, Japan]
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[9]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
DOI=10.1073/pnas.2135385100; PubMed=14576278 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The proteome of Saccharomyces cerevisiae mitochondria.";
Proc. Natl. Acad. Sci. U.S.A. 100:13207-13212(2003).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-135 AND SER-339, AND MASS SPECTROMETRY.
DOI=10.1074/mcp.M700468-MCP200; PubMed=18407956 [NCBI, ExPASy, EBI, Israel, Japan]
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth phosphoproteome analysis.";
Mol. Cell. Proteomics 0:0-0(2008).
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.
  • CATALYTIC ACTIVITY: Acyl-CoA + NADP+ = trans-2,3-dehydroacyl-CoA + NADPH.
  • SUBUNIT: 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.
  • SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase family. Quinone oxidoreductase subfamily.
  • CAUTION: Was originally (PubMed:8195160) 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 (PubMed:11509667).
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
D26606; BAA05651.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z35895; CAA84968.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X76078; CAA53683.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY557872; AAS56198.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_009582.1; -.
3D structure databases
HSSP Q8WZM3; 1GYR. [HSSP ENTRY / PDB]
ModBase P38071.
Organism-specific databases
CYGD YBR026c; -.
SGD S000000230; ETR1.
Yeast-GFP YBR026C.
Gene expression databases
GermOnline YBR026C; Saccharomyces cerevisiae.
Ontologies
GO
GO:0005739; Cellular component: mitochondrion (inferred from direct assay from SGD).
GO:0016631; Molecular function: enoyl-[acyl-carrier-protein] reductase activity (inferred from direct assay from SGD).
GO:0009060; Biological process: aerobic respiration (inferred from mutant phenotype from SGD).
GO:0006633; Biological process: fatty acid biosynthetic process (inferred from mutant phenotype from SGD).
QuickGo view.
Family and domain databases
InterPro IPR013154; AlcDHase_GroES-like.
IPR002085; AlcDHase_SF_Zn.
IPR016040; NAD(P)-bd.
Graphical view of domain structure.
Gene3D G3DSA:3.40.50.720; NAD(P)-bd; 1.
PANTHER PTHR11695; ADH_Sf_Zn; 1.
Pfam PF08240; ADH_N; 1.
Pfam graphical view of domain structure.
BLOCKS P38071.
Proteomic databases
PeptideAtlas P38071; -.
Genome annotation databases
Ensembl YBR026C; Saccharomyces cerevisiae. [Contig view]
GeneID 852314; -.
GenomeReviews Y13134_GR; YBR026C.
KEGG sce:YBR026C; -.
NMPDR fig|4932.3.peg.277; -.
Phylogenomic databases
HOGENOM P38071; -.
Other
LinkHub P38071; -.
ProtoNet P38071.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Direct protein sequencing; DNA-binding; Fatty acid biosynthesis; Lipid synthesis; Mitochondrion; NADP; Oxidoreductase; Phosphoprotein; Transit peptide.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
TRANSIT   1     9  9     Mitochondrion. 
CHAIN   10   380  371     Enoyl-[acyl-carrier protein] reductase [NADPH, B-specific], mitochondrial. PRO_0000160924
MOD_RES   135   135        Phosphoserine. 
MOD_RES   339   339        Phosphoserine. 
MUTAGEN   73    73        Y->N: 0.1% of catalytic activity. No specific ARS1 binding. 
CONFLICT   24    24        I -> T (in Ref. 4; AAS56198). 
Sequence information
Length: 380 AA [This is the length of the unprocessed precursor] Molecular weight: 42067 Da [This is the MW of the unprocessed precursor] CRC64: 9795013283C3E9F8 [This is a checksum on the sequence]
        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 

P38071 in FASTA format

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