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P38071 (ETR1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 124. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Enoyl-[acyl-carrier protein] reductase [NADPH, B-specific], mitochondrial

EC=1.3.1.10
Alternative name(s):
Mitochondrial respiratory function protein 1
Trans-2-enoyl-CoA reductase
EC=1.3.1.38
Gene names
Name:ETR1
Synonyms:MRF1, MRF1'
Ordered Locus Names:YBR026C
ORF Names:YBR0310
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length380 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Required for respiration and the maintenance of the mitochondrial compartment. Oxidoreductase with a preference for short and medium chain substrates, including trans-2-hexenoyl-CoA (C6), trans-2-decenoyl-CoA (C10), and trans-2-hexadecenoyl-CoA (C16). May play a role in mitochondrial fatty acid synthesis. Ref.7 Ref.8

Catalytic activity

An acyl-[acyl-carrier protein] + NADP+ = a 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. Ref.7

Subcellular location

Mitochondrion matrix Ref.6 Ref.7 Ref.10.

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.7).

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 99Mitochondrion Ref.1
Chain10 – 380371Enoyl-[acyl-carrier protein] reductase [NADPH, B-specific], mitochondrial
PRO_0000160924

Regions

Nucleotide binding185 – 1884NADP By similarity
Nucleotide binding208 – 2103NADP By similarity
Nucleotide binding283 – 2864NADP By similarity
Nucleotide binding308 – 3103NADP By similarity

Sites

Binding site1571NADP By similarity
Binding site3731NADP By similarity

Amino acid modifications

Modified residue3391Phosphoserine Ref.11

Experimental info

Mutagenesis731Y → N: 0.1% of catalytic activity. No specific ARS1 binding. Ref.8
Sequence conflict241I → T in AAS56198. Ref.5

Sequences

Sequence LengthMass (Da)Tools
P38071 [UniParc].

Last modified October 17, 2006. Version 3.
Checksum: 9795013283C3E9F8

FASTA38042,067
        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 

« Hide

References

« Hide '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] [Europe PMC] [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] [Europe PMC] [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. expand/collapse author list , 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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[4]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[5]"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. expand/collapse author list , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J.
Genome Res. 17:536-543(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[6]"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] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[7]"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] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBUNIT, SUBCELLULAR LOCATION.
[8]"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] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF TYR-73.
[9]"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] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[10]"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] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
Strain: ATCC 76625 / YPH499.
[11]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-339, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D26606 Genomic DNA. Translation: BAA05651.1.
Z35895 Genomic DNA. Translation: CAA84968.1.
X76078 Genomic DNA. Translation: CAA53683.1.
AY557872 Genomic DNA. Translation: AAS56198.1.
BK006936 Genomic DNA. Translation: DAA07148.1.
RefSeqNP_009582.1. NM_001178374.1.

3D structure databases

ProteinModelPortalP38071.
SMRP38071. Positions 52-377.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid32729. 149 interactions.
IntActP38071. 2 interactions.
MINTMINT-2788988.
STRING4932.YBR026C.

Proteomic databases

PaxDbP38071.
PeptideAtlasP38071.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYBR026C; YBR026C; YBR026C.
GeneID852314.
KEGGsce:YBR026C.

Organism-specific databases

CYGDYBR026c.
SGDS000000230. ETR1.

Phylogenomic databases

eggNOGCOG0604.
GeneTreeENSGT00740000115589.
HOGENOMHOG000294683.
KOK07512.
OMAGSGQWFI.
OrthoDBEOG7PS1RH.

Enzyme and pathway databases

BioCycMetaCyc:G3O-29006-MONOMER.
YEAST:G3O-29006-MONOMER.
BRENDA1.3.1.10. 984.

Gene expression databases

GenevestigatorP38071.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
3.90.180.10. 1 hit.
InterProIPR002085. ADH_SF_Zn-type.
IPR011032. GroES-like.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERPTHR11695. PTHR11695. 1 hit.
SUPFAMSSF50129. SSF50129. 1 hit.
ProtoNetSearch...

Other

NextBio971002.
PROP38071.

Entry information

Entry nameETR1_YEAST
AccessionPrimary (citable) accession number: P38071
Secondary accession number(s): D6VQ28, Q6Q5P2
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 17, 2006
Last modified: March 19, 2014
This is version 124 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome II

Yeast (Saccharomyces cerevisiae) chromosome II: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families