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Protein

Elongation of fatty acids protein 1

Gene

ELO1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Component of a microsomal membrane bound medium-chain fatty acid elongation system, which extends medium-chain-length fatty acids to long-chain fatty acids. Component of elongase I, which extends 12-16-carbon fatty acyl-CoAs such as lauroyl-CoA to 14-18-carbon fatty acids by incorporation of malonyl-CoA.4 Publications

Catalytic activityi

A very-long-chain acyl-CoA + malonyl-CoA = CoA + a very-long-chain 3-oxoacyl-CoA + CO2.1 Publication

Kineticsi

  1. KM=0.33 mM for octanoyl-CoA1 Publication
  2. KM=0.83 mM for decanoyl-CoA1 Publication
  3. KM=0.05 mM for lauroyl-CoA1 Publication
  4. KM=0.4 mM for myristoyl-CoA1 Publication
  5. KM=0.13 mM for palmitoyl-CoA1 Publication

    GO - Molecular functioni

    • fatty acid elongase activity Source: SGD

    GO - Biological processi

    • fatty acid elongation, unsaturated fatty acid Source: SGD
    Complete GO annotation...

    Keywords - Molecular functioni

    Transferase

    Keywords - Biological processi

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

    Enzyme and pathway databases

    BioCyciYEAST:G3O-31627-MONOMER.
    ReactomeiREACT_297847. Linoleic acid (LA) metabolism.
    REACT_306569. alpha-linolenic acid (ALA) metabolism.
    REACT_308531. Synthesis of very long-chain fatty acyl-CoAs.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Elongation of fatty acids protein 11 Publication (EC:2.3.1.1991 Publication)
    Alternative name(s):
    3-keto acyl-CoA synthase ELO1Curated
    Very-long-chain 3-oxoacyl-CoA synthase 1Curated
    Gene namesi
    Name:ELO11 Publication
    Ordered Locus Names:YJL196CImported
    ORF Names:J0343
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311 Componenti: Chromosome X

    Organism-specific databases

    CYGDiYJL196c.
    EuPathDBiFungiDB:YJL196C.
    SGDiS000003732. ELO1.

    Subcellular locationi

    Topology

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 6363Lumenal1 PublicationAdd
    BLAST
    Transmembranei64 – 8421Helical; Name=1Sequence AnalysisAdd
    BLAST
    Topological domaini85 – 10016Cytoplasmic1 PublicationAdd
    BLAST
    Transmembranei101 – 12121Helical; Name=2Sequence AnalysisAdd
    BLAST
    Topological domaini122 – 14120Lumenal1 PublicationAdd
    BLAST
    Transmembranei142 – 16322Helical; Name=3Sequence AnalysisAdd
    BLAST
    Topological domaini164 – 17411Cytoplasmic1 PublicationAdd
    BLAST
    Transmembranei175 – 19622Helical; Name=4Sequence AnalysisAdd
    BLAST
    Topological domaini197 – 2015Lumenal1 Publication
    Transmembranei202 – 22322Helical; Name=5Sequence AnalysisAdd
    BLAST
    Topological domaini224 – 23411Cytoplasmic1 PublicationAdd
    BLAST
    Transmembranei235 – 25521Helical; Name=6Sequence AnalysisAdd
    BLAST
    Topological domaini256 – 27116Lumenal1 PublicationAdd
    BLAST
    Transmembranei272 – 29221Helical; Name=7Sequence AnalysisAdd
    BLAST
    Topological domaini293 – 31018Cytoplasmic1 PublicationAdd
    BLAST

    GO - Cellular componenti

    • endoplasmic reticulum membrane Source: UniProtKB-SubCell
    • integral component of membrane Source: UniProtKB-KW
    • membrane Source: SGD
    Complete GO annotation...

    Keywords - Cellular componenti

    Endoplasmic reticulum, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 310310Elongation of fatty acids protein 1PRO_0000207548Add
    BLAST

    Proteomic databases

    MaxQBiP39540.
    PaxDbiP39540.

    Expressioni

    Inductioni

    Induced in wild-type cells supplemented with 14:0 fatty acids and repressed when cells are supplied with 16- and 18-carbon fatty acids.

    Interactioni

    Protein-protein interaction databases

    BioGridi33568. 73 interactions.
    DIPiDIP-8755N.
    IntActiP39540. 5 interactions.
    MINTiMINT-1357650.
    STRINGi4932.YJL196C.

    Structurei

    3D structure databases

    ProteinModelPortaliP39540.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi304 – 3074Di-lysine motif1 Publication

    Domaini

    The C-terminal di-lysine motif may confer endoplasmic reticulum localization.1 Publication

    Sequence similaritiesi

    Belongs to the ELO family.Curated

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG305096.
    GeneTreeiENSGT00760000119122.
    HOGENOMiHOG000160635.
    InParanoidiP39540.
    KOiK10245.
    OMAiWATAGRF.
    OrthoDBiEOG7F51CG.

    Family and domain databases

    InterProiIPR002076. ELO_fam.
    [Graphical view]
    PANTHERiPTHR11157. PTHR11157. 1 hit.
    PfamiPF01151. ELO. 1 hit.
    [Graphical view]
    PROSITEiPS01188. ELO. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P39540-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MVSDWKNFCL EKASRFRPTI DRPFFNIYLW DYFNRAVGWA TAGRFQPKDF
    60 70 80 90 100
    EFTVGKQPLS EPRPVLLFIA MYYVVIFGGR SLVKSCKPLK LRFISQVHNL
    110 120 130 140 150
    MLTSVSFLWL ILMVEQMLPI VYRHGLYFAV CNVESWTQPM ETLYYLNYMT
    160 170 180 190 200
    KFVEFADTVL MVLKHRKLTF LHTYHHGATA LLCYNQLVGY TAVTWVPVTL
    210 220 230 240 250
    NLAVHVLMYW YYFLSASGIR VWWKAWVTRL QIVQFMLDLI VVYYVLYQKI
    260 270 280 290 300
    VAAYFKNACT PQCEDCLGSM TAIAAGAAIL TSYLFLFISF YIEVYKRGSA
    310
    SGKKKINKNN
    Length:310
    Mass (Da):36,234
    Last modified:February 1, 1995 - v1
    Checksum:i051D5369976BF48F
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    X77688 Genomic DNA. Translation: CAA54764.1.
    Z49471 Genomic DNA. Translation: CAA89491.1.
    BK006943 Genomic DNA. Translation: DAA08612.1.
    PIRiS46638.
    RefSeqiNP_012339.1. NM_001181629.1.

    Genome annotation databases

    EnsemblFungiiYJL196C; YJL196C; YJL196C.
    GeneIDi853243.
    KEGGisce:YJL196C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    X77688 Genomic DNA. Translation: CAA54764.1.
    Z49471 Genomic DNA. Translation: CAA89491.1.
    BK006943 Genomic DNA. Translation: DAA08612.1.
    PIRiS46638.
    RefSeqiNP_012339.1. NM_001181629.1.

    3D structure databases

    ProteinModelPortaliP39540.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi33568. 73 interactions.
    DIPiDIP-8755N.
    IntActiP39540. 5 interactions.
    MINTiMINT-1357650.
    STRINGi4932.YJL196C.

    Proteomic databases

    MaxQBiP39540.
    PaxDbiP39540.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblFungiiYJL196C; YJL196C; YJL196C.
    GeneIDi853243.
    KEGGisce:YJL196C.

    Organism-specific databases

    CYGDiYJL196c.
    EuPathDBiFungiDB:YJL196C.
    SGDiS000003732. ELO1.

    Phylogenomic databases

    eggNOGiNOG305096.
    GeneTreeiENSGT00760000119122.
    HOGENOMiHOG000160635.
    InParanoidiP39540.
    KOiK10245.
    OMAiWATAGRF.
    OrthoDBiEOG7F51CG.

    Enzyme and pathway databases

    BioCyciYEAST:G3O-31627-MONOMER.
    ReactomeiREACT_297847. Linoleic acid (LA) metabolism.
    REACT_306569. alpha-linolenic acid (ALA) metabolism.
    REACT_308531. Synthesis of very long-chain fatty acyl-CoAs.

    Miscellaneous databases

    NextBioi973475.
    PROiP39540.

    Family and domain databases

    InterProiIPR002076. ELO_fam.
    [Graphical view]
    PANTHERiPTHR11157. PTHR11157. 1 hit.
    PfamiPF01151. ELO. 1 hit.
    [Graphical view]
    PROSITEiPS01188. ELO. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Isolation and characterization of a gene affecting fatty acid elongation in Saccharomyces cerevisiae."
      Toke D.A., Martin C.E.
      J. Biol. Chem. 271:18413-18422(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
    2. "The sequence of a 36 kb segment on the left arm of yeast chromosome X identifies 24 open reading frames including NUC1, PRP21 (SPP91), CDC6, CRY2, the gene for S24, a homologue to the aconitase gene ACO1 and two homologues to chromosome III genes."
      Purnelle B., Coster F., Goffeau A.
      Yeast 10:1235-1249(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    3. "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X."
      Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C., Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D., Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J., Heumann K.
      , Hilger F., Hollenberg C.P., Huang M.-E., Jacq C., Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E., Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T., Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R., Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N., To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H., von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.
      EMBO J. 15:2031-2049(1996) [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. "Fatty acid elongation in yeast--biochemical characteristics of the enzyme system and isolation of elongation-defective mutants."
      Dittrich F., Zajonc D., Huhne K., Hoja U., Ekici A., Greiner E., Klein H., Hofmann J., Bessoule J.J., Sperling P., Schweizer E.
      Eur. J. Biochem. 252:477-485(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
    6. "Elo1p-dependent carboxy-terminal elongation of C14:1Delta(9) to C16:1Delta(11) fatty acids in Saccharomyces cerevisiae."
      Schneiter R., Tatzer V., Gogg G., Leitner E., Kohlwein S.D.
      J. Bacteriol. 182:3655-3660(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    7. "Functional differentiation and selective inactivation of multiple Saccharomyces cerevisiae genes involved in very-long-chain fatty acid synthesis."
      Roessler H., Rieck C., Delong T., Hoja U., Schweizer E.
      Mol. Genet. Genomics 269:290-298(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    8. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    9. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    10. "A global topology map of the Saccharomyces cerevisiae membrane proteome."
      Kim H., Melen K., Oesterberg M., von Heijne G.
      Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: TOPOLOGY [LARGE SCALE ANALYSIS].
      Strain: ATCC 208353 / W303-1A.

    Entry informationi

    Entry nameiELO1_YEAST
    AccessioniPrimary (citable) accession number: P39540
    Secondary accession number(s): D6VVZ6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1995
    Last sequence update: February 1, 1995
    Last modified: June 24, 2015
    This is version 109 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 937 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    Complete proteome, 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 X
      Yeast (Saccharomyces cerevisiae) chromosome X: entries and gene names

    External Data

    Dasty 3

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.