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P38071

- ETR1_YEAST

UniProt

P38071 - ETR1_YEAST

Protein

Enoyl-[acyl-carrier protein] reductase [NADPH, B-specific], mitochondrial

Gene

ETR1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 126 (01 Oct 2014)
      Sequence version 3 (17 Oct 2006)
      Previous versions | rss
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    Functioni

    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.2 Publications

    Catalytic activityi

    An acyl-[acyl-carrier protein] + NADP+ = a trans-2,3-dehydroacyl-[acyl-carrier protein] + NADPH.
    Acyl-CoA + NADP+ = trans-2,3-dehydroacyl-CoA + NADPH.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei157 – 1571NADPBy similarity
    Binding sitei373 – 3731NADPBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi185 – 1884NADPBy similarity
    Nucleotide bindingi208 – 2103NADPBy similarity
    Nucleotide bindingi283 – 2864NADPBy similarity
    Nucleotide bindingi308 – 3103NADPBy similarity

    GO - Molecular functioni

    1. DNA binding Source: UniProtKB-KW
    2. enoyl-[acyl-carrier-protein] reductase (NADPH, B-specific) activity Source: UniProtKB-EC
    3. enoyl-[acyl-carrier-protein] reductase activity Source: SGD
    4. trans-2-enoyl-CoA reductase (NADPH) activity Source: UniProtKB-EC
    5. zinc ion binding Source: InterPro

    GO - Biological processi

    1. aerobic respiration Source: SGD
    2. fatty acid biosynthetic process Source: SGD

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism

    Keywords - Ligandi

    DNA-binding, NADP

    Enzyme and pathway databases

    BioCyciMetaCyc:G3O-29006-MONOMER.
    YEAST:G3O-29006-MONOMER.
    BRENDAi1.3.1.10. 984.

    Names & Taxonomyi

    Protein namesi
    Recommended 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 namesi
    Name:ETR1
    Synonyms:MRF1, MRF1'
    Ordered Locus Names:YBR026C
    ORF Names:YBR0310
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome II

    Organism-specific databases

    CYGDiYBR026c.
    SGDiS000000230. ETR1.

    Subcellular locationi

    Mitochondrion matrix 3 Publications

    GO - Cellular componenti

    1. mitochondrial matrix Source: UniProtKB-SubCell
    2. mitochondrion Source: SGD

    Keywords - Cellular componenti

    Mitochondrion

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi73 – 731Y → N: 0.1% of catalytic activity. No specific ARS1 binding. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 99Mitochondrion1 Publication
    Chaini10 – 380371Enoyl-[acyl-carrier protein] reductase [NADPH, B-specific], mitochondrialPRO_0000160924Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei339 – 3391Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP38071.
    PaxDbiP38071.
    PeptideAtlasiP38071.

    Expressioni

    Gene expression databases

    GenevestigatoriP38071.

    Interactioni

    Subunit structurei

    Homodimer or in a complex with other proteins. Interacts with ARS1.1 Publication

    Protein-protein interaction databases

    BioGridi32729. 149 interactions.
    IntActiP38071. 2 interactions.
    MINTiMINT-2788988.
    STRINGi4932.YBR026C.

    Structurei

    3D structure databases

    ProteinModelPortaliP38071.
    SMRiP38071. Positions 52-377.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG0604.
    GeneTreeiENSGT00740000115589.
    HOGENOMiHOG000294683.
    KOiK07512.
    OMAiGSGQWFI.
    OrthoDBiEOG7PS1RH.

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    3.90.180.10. 1 hit.
    InterProiIPR002085. ADH_SF_Zn-type.
    IPR011032. GroES-like.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view]
    PANTHERiPTHR11695. PTHR11695. 1 hit.
    SUPFAMiSSF50129. SSF50129. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P38071-1 [UniParc]FASTAAdd to Basket

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    MLPTFKRYMS SSAHQIPKHF KSLIYSTHEV EDCTKVLSVK NYTPKQDLSQ    50
    SIVLKTLAFP INPSDINQLQ GVYPSRPEKT YDYSTDEPAA IAGNEGVFEV 100
    VSLPSGSSKG DLKLGDRVIP LQANQGTWSN YRVFSSSSDL IKVNDLDLFS 150
    AATVSVNGCT GFQLVSDYID WNSNGNEWII QNAGTSSVSK IVTQVAKAKG 200
    IKTLSVIRDR DNFDEVAKVL EDKYGATKVI SESQNNDKTF AKEVLSKILG 250
    ENARVRLALN SVGGKSSASI ARKLENNALM LTYGGMSKQP VTLPTSLHIF 300
    KGLTSKGYWV TEKNKKNPQS KIDTISDFIK MYNYGHIISP RDEIETLTWN 350
    TNTTTDEQLL ELVKKGITGK GKKKMVVLEW 380
    Length:380
    Mass (Da):42,067
    Last modified:October 17, 2006 - v3
    Checksum:i9795013283C3E9F8
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti24 – 241I → T in AAS56198. (PubMed:17322287)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    RefSeqiNP_009582.1. NM_001178374.1.

    Genome annotation databases

    EnsemblFungiiYBR026C; YBR026C; YBR026C.
    GeneIDi852314.
    KEGGisce:YBR026C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    RefSeqi NP_009582.1. NM_001178374.1.

    3D structure databases

    ProteinModelPortali P38071.
    SMRi P38071. Positions 52-377.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 32729. 149 interactions.
    IntActi P38071. 2 interactions.
    MINTi MINT-2788988.
    STRINGi 4932.YBR026C.

    Proteomic databases

    MaxQBi P38071.
    PaxDbi P38071.
    PeptideAtlasi P38071.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YBR026C ; YBR026C ; YBR026C .
    GeneIDi 852314.
    KEGGi sce:YBR026C.

    Organism-specific databases

    CYGDi YBR026c.
    SGDi S000000230. ETR1.

    Phylogenomic databases

    eggNOGi COG0604.
    GeneTreei ENSGT00740000115589.
    HOGENOMi HOG000294683.
    KOi K07512.
    OMAi GSGQWFI.
    OrthoDBi EOG7PS1RH.

    Enzyme and pathway databases

    BioCyci MetaCyc:G3O-29006-MONOMER.
    YEAST:G3O-29006-MONOMER.
    BRENDAi 1.3.1.10. 984.

    Miscellaneous databases

    NextBioi 971002.
    PROi P38071.

    Gene expression databases

    Genevestigatori P38071.

    Family and domain databases

    Gene3Di 3.40.50.720. 1 hit.
    3.90.180.10. 1 hit.
    InterProi IPR002085. ADH_SF_Zn-type.
    IPR011032. GroES-like.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view ]
    PANTHERi PTHR11695. PTHR11695. 1 hit.
    SUPFAMi SSF50129. SSF50129. 1 hit.
    ProtoNeti Search...

    Publicationsi

    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.
      , 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. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    5. 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. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    10. 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].

    Entry informationi

    Entry nameiETR1_YEAST
    AccessioniPrimary (citable) accession number: P38071
    Secondary accession number(s): D6VQ28, Q6Q5P2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1994
    Last sequence update: October 17, 2006
    Last modified: October 1, 2014
    This is version 126 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 1560 molecules/cell in log phase SD medium.1 Publication

    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).2 Publications

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families
    2. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    3. Yeast chromosome II
      Yeast (Saccharomyces cerevisiae) chromosome II: entries and gene names

    External Data

    Dasty 3