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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: -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

Miscellaneous

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

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

    GO - Biological processi

    Keywordsi

    Molecular functionTransferase
    Biological processFatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism

    Enzyme and pathway databases

    BioCyciYEAST:G3O-31627-MONOMER
    ReactomeiR-SCE-2046105 Linoleic acid (LA) metabolism
    R-SCE-2046106 alpha-linolenic acid (ALA) metabolism
    R-SCE-75876 Synthesis of very long-chain fatty acyl-CoAs

    Chemistry databases

    SwissLipidsiSLP:000000576
    SLP:000000876

    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
    Proteomesi
    • UP000002311 Componenti: Chromosome X

    Organism-specific databases

    EuPathDBiFungiDB:YJL196C
    SGDiS000003732 ELO1

    Subcellular locationi

    Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

    Topology

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Topological domaini1 – 63Lumenal1 PublicationAdd BLAST63
    Transmembranei64 – 84Helical; Name=1Sequence analysisAdd BLAST21
    Topological domaini85 – 100Cytoplasmic1 PublicationAdd BLAST16
    Transmembranei101 – 121Helical; Name=2Sequence analysisAdd BLAST21
    Topological domaini122 – 141Lumenal1 PublicationAdd BLAST20
    Transmembranei142 – 163Helical; Name=3Sequence analysisAdd BLAST22
    Topological domaini164 – 174Cytoplasmic1 PublicationAdd BLAST11
    Transmembranei175 – 196Helical; Name=4Sequence analysisAdd BLAST22
    Topological domaini197 – 201Lumenal1 Publication5
    Transmembranei202 – 223Helical; Name=5Sequence analysisAdd BLAST22
    Topological domaini224 – 234Cytoplasmic1 PublicationAdd BLAST11
    Transmembranei235 – 255Helical; Name=6Sequence analysisAdd BLAST21
    Topological domaini256 – 271Lumenal1 PublicationAdd BLAST16
    Transmembranei272 – 292Helical; Name=7Sequence analysisAdd BLAST21
    Topological domaini293 – 310Cytoplasmic1 PublicationAdd BLAST18

    Keywords - Cellular componenti

    Endoplasmic reticulum, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00002075481 – 310Elongation of fatty acids protein 1Add BLAST310

    Proteomic databases

    MaxQBiP39540
    PaxDbiP39540
    PRIDEiP39540

    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, 99 interactors
    DIPiDIP-8755N
    IntActiP39540, 5 interactors
    MINTiP39540
    STRINGi4932.YJL196C

    Structurei

    3D structure databases

    ProteinModelPortaliP39540
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Motif

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Motifi304 – 307Di-lysine motif1 Publication4

    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

    GeneTreeiENSGT00760000119122
    HOGENOMiHOG000160635
    InParanoidiP39540
    KOiK10245
    OMAiFGYKNKV
    OrthoDBiEOG092C47LF

    Family and domain databases

    InterProiView protein in InterPro
    IPR030457 ELO_CS
    IPR002076 ELO_fam
    PANTHERiPTHR11157 PTHR11157, 1 hit
    PfamiView protein in Pfam
    PF01151 ELO, 1 hit
    PROSITEiView protein in PROSITE
    PS01188 ELO, 1 hit

    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

    Similar proteinsi

    Entry informationi

    Entry nameiELO1_YEAST
    AccessioniPrimary (citable) accession number: P39540
    Secondary accession number(s): D6VVZ6
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1995
    Last sequence update: February 1, 1995
    Last modified: March 28, 2018
    This is version 127 of the entry and version 1 of the sequence. See complete history.
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    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

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