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P25358

- ELO2_YEAST

UniProt

P25358 - ELO2_YEAST

Protein

Elongation of fatty acids protein 2

Gene

FEN1

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 134 (01 Oct 2014)
      Sequence version 1 (01 May 1992)
      Previous versions | rss
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    Functioni

    Involved in synthesis of 1,3-beta-glucan. Could be a subunit of 1,3-beta-glucan synthase. Could be also a component of the membrane bound fatty acid elongation systems that produce the 26-carbon very long chain fatty acids that are precursors for ceramide and sphingolipids. Appears to be involved in the elongation of fatty acids up to 24 carbons. Appears to have the highest affinity for substrates with chain length less than 22 carbons.

    Catalytic activityi

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

    GO - Molecular functioni

    1. fatty acid elongase activity Source: SGD

    GO - Biological processi

    1. fatty acid elongation Source: SGD
    2. sphingolipid biosynthetic process Source: SGD
    3. vesicle-mediated transport Source: SGD

    Keywords - Molecular functioni

    Transferase

    Keywords - Biological processi

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

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-17330.
    YEAST:YCR034W-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Elongation of fatty acids protein 2 (EC:2.3.1.199)
    Alternative name(s):
    3-keto acyl-CoA synthase ELO2
    Protein GNS1
    Very-long-chain 3-oxoacyl-CoA synthase 2
    v-SNARE bypass mutant gene 2 protein
    Gene namesi
    Name:FEN1
    Synonyms:ELO2, GNS1, VBM2
    Ordered Locus Names:YCR034W
    ORF Names:YCR34W, YCR521
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome III

    Organism-specific databases

    CYGDiYCR034w.
    SGDiS000000630. FEN1.

    Subcellular locationi

    GO - Cellular componenti

    1. endoplasmic reticulum Source: SGD
    2. integral component of membrane Source: UniProtKB-KW

    Keywords - Cellular componenti

    Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 347347Elongation of fatty acids protein 2PRO_0000207549Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei334 – 3341Phosphothreonine3 Publications
    Modified residuei336 – 3361Phosphoserine3 Publications
    Modified residuei338 – 3381Phosphoserine3 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP25358.
    PaxDbiP25358.

    Expressioni

    Gene expression databases

    GenevestigatoriP25358.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ERP1Q053591EBI-6415,EBI-6581
    ERV25P548371EBI-6415,EBI-6642
    PHO88P382641EBI-6415,EBI-13350
    PIS1P061971EBI-6415,EBI-13458
    SPF1P399861EBI-6415,EBI-3128
    SUR2P389921EBI-6415,EBI-18574
    SWP1Q027951EBI-6415,EBI-12666
    YHR080CP388001EBI-6415,EBI-24597

    Protein-protein interaction databases

    BioGridi31017. 258 interactions.
    DIPiDIP-4176N.
    IntActiP25358. 21 interactions.
    MINTiMINT-547542.
    STRINGi4932.YCR034W.

    Structurei

    3D structure databases

    ProteinModelPortaliP25358.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 6262ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini84 – 10724CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini129 – 20072ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini222 – 24423CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini266 – 27510ExtracellularSequence Analysis
    Topological domaini297 – 34751CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei63 – 8321HelicalSequence AnalysisAdd
    BLAST
    Transmembranei108 – 12821HelicalSequence AnalysisAdd
    BLAST
    Transmembranei201 – 22121HelicalSequence AnalysisAdd
    BLAST
    Transmembranei245 – 26521HelicalSequence AnalysisAdd
    BLAST
    Transmembranei276 – 29621HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi333 – 3419Pro-rich

    Sequence similaritiesi

    Belongs to the ELO family.Curated

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG305096.
    GeneTreeiENSGT00740000115027.
    HOGENOMiHOG000160635.
    KOiK10245.
    OMAiYMNYIVK.
    OrthoDBiEOG7F51CG.

    Family and domain databases

    InterProiIPR002076. GNS1_SUR4.
    [Graphical view]
    PANTHERiPTHR11157. PTHR11157. 1 hit.
    PfamiPF01151. ELO. 1 hit.
    [Graphical view]
    PROSITEiPS01188. ELO. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P25358-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNSLVTQYAA PLFERYPQLH DYLPTLERPF FNISLWEHFD DVVTRVTNGR    50
    FVPSEFQFIA GELPLSTLPP VLYAITAYYV IIFGGRFLLS KSKPFKLNGL 100
    FQLHNLVLTS LSLTLLLLMV EQLVPIIVQH GLYFAICNIG AWTQPLVTLY 150
    YMNYIVKFIE FIDTFFLVLK HKKLTFLHTY HHGATALLCY TQLMGTTSIS 200
    WVPISLNLGV HVVMYWYYFL AARGIRVWWK EWVTRFQIIQ FVLDIGFIYF 250
    AVYQKAVHLY FPILPHCGDC VGSTTATFAG CAIISSYLVL FISFYINVYK 300
    RKGTKTSRVV KRAHGGVAAK VNEYVNVDLK NVPTPSPSPK PQHRRKR 347
    Length:347
    Mass (Da):40,002
    Last modified:May 1, 1992 - v1
    Checksum:i24225E49A43A1003
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    S78624 Genomic DNA. Translation: AAB21260.1.
    X56909 Genomic DNA. Translation: CAA40226.1.
    X59720 Genomic DNA. Translation: CAA42301.1.
    AF012655 Genomic DNA. Translation: AAB87766.1.
    BK006937 Genomic DNA. Translation: DAA07513.1.
    PIRiS12916.
    RefSeqiNP_009963.1. NM_001178748.1.

    Genome annotation databases

    EnsemblFungiiYCR034W; YCR034W; YCR034W.
    GeneIDi850400.
    KEGGisce:YCR034W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    S78624 Genomic DNA. Translation: AAB21260.1 .
    X56909 Genomic DNA. Translation: CAA40226.1 .
    X59720 Genomic DNA. Translation: CAA42301.1 .
    AF012655 Genomic DNA. Translation: AAB87766.1 .
    BK006937 Genomic DNA. Translation: DAA07513.1 .
    PIRi S12916.
    RefSeqi NP_009963.1. NM_001178748.1.

    3D structure databases

    ProteinModelPortali P25358.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 31017. 258 interactions.
    DIPi DIP-4176N.
    IntActi P25358. 21 interactions.
    MINTi MINT-547542.
    STRINGi 4932.YCR034W.

    Proteomic databases

    MaxQBi P25358.
    PaxDbi P25358.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YCR034W ; YCR034W ; YCR034W .
    GeneIDi 850400.
    KEGGi sce:YCR034W.

    Organism-specific databases

    CYGDi YCR034w.
    SGDi S000000630. FEN1.

    Phylogenomic databases

    eggNOGi NOG305096.
    GeneTreei ENSGT00740000115027.
    HOGENOMi HOG000160635.
    KOi K10245.
    OMAi YMNYIVK.
    OrthoDBi EOG7F51CG.

    Enzyme and pathway databases

    BioCyci MetaCyc:MONOMER-17330.
    YEAST:YCR034W-MONOMER.

    Miscellaneous databases

    NextBioi 965935.
    PROi P25358.

    Gene expression databases

    Genevestigatori P25358.

    Family and domain databases

    InterProi IPR002076. GNS1_SUR4.
    [Graphical view ]
    PANTHERi PTHR11157. PTHR11157. 1 hit.
    Pfami PF01151. ELO. 1 hit.
    [Graphical view ]
    PROSITEi PS01188. ELO. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Involvement of long chain fatty acid elongation in the trafficking of secretory vesicles in yeast."
      David D., Sundarababu S., Gerst J.E.
      J. Cell Biol. 143:1167-1182(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "The complete sequence of the 8.2 kb segment left of MAT on chromosome III reveals five ORFs, including a gene for a yeast ribokinase."
      Thierry A., Fairhead C., Dujon B.
      Yeast 6:521-534(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 96604 / S288c / FY1679.
    3. "The complete sequence of a 7.5 kb region of chromosome III from Saccharomyces cerevisiae that lies between CRY1 and MAT."
      Wicksteed B.L., Roberts A.B., Sagliocco F.A., Brown A.J.P.
      Yeast 7:761-772(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    4. "The complete DNA sequence of yeast chromosome III."
      Oliver S.G., van der Aart Q.J.M., Agostoni-Carbone M.L., Aigle M., Alberghina L., Alexandraki D., Antoine G., Anwar R., Ballesta J.P.G., Benit P., Berben G., Bergantino E., Biteau N., Bolle P.-A., Bolotin-Fukuhara M., Brown A., Brown A.J.P., Buhler J.-M.
      , Carcano C., Carignani G., Cederberg H., Chanet R., Contreras R., Crouzet M., Daignan-Fornier B., Defoor E., Delgado M.D., Demolder J., Doira C., Dubois E., Dujon B., Duesterhoeft A., Erdmann D., Esteban M., Fabre F., Fairhead C., Faye G., Feldmann H., Fiers W., Francingues-Gaillard M.-C., Franco L., Frontali L., Fukuhara H., Fuller L.J., Galland P., Gent M.E., Gigot D., Gilliquet V., Glansdorff N., Goffeau A., Grenson M., Grisanti P., Grivell L.A., de Haan M., Haasemann M., Hatat D., Hoenicka J., Hegemann J.H., Herbert C.J., Hilger F., Hohmann S., Hollenberg C.P., Huse K., Iborra F., Indge K.J., Isono K., Jacq C., Jacquet M., James C.M., Jauniaux J.-C., Jia Y., Jimenez A., Kelly A., Kleinhans U., Kreisl P., Lanfranchi G., Lewis C., van der Linden C.G., Lucchini G., Lutzenkirchen K., Maat M.J., Mallet L., Mannhaupt G., Martegani E., Mathieu A., Maurer C.T.C., McConnell D., McKee R.A., Messenguy F., Mewes H.-W., Molemans F., Montague M.A., Muzi Falconi M., Navas L., Newlon C.S., Noone D., Pallier C., Panzeri L., Pearson B.M., Perea J., Philippsen P., Pierard A., Planta R.J., Plevani P., Poetsch B., Pohl F.M., Purnelle B., Ramezani Rad M., Rasmussen S.W., Raynal A., Remacha M.A., Richterich P., Roberts A.B., Rodriguez F., Sanz E., Schaaff-Gerstenschlaeger I., Scherens B., Schweitzer B., Shu Y., Skala J., Slonimski P.P., Sor F., Soustelle C., Spiegelberg R., Stateva L.I., Steensma H.Y., Steiner S., Thierry A., Thireos G., Tzermia M., Urrestarazu L.A., Valle G., Vetter I., van Vliet-Reedijk J.C., Voet M., Volckaert G., Vreken P., Wang H., Warmington J.R., von Wettstein D., Wicksteed B.L., Wilson C., Wurst H., Xu G., Yoshikawa A., Zimmermann F.K., Sgouros J.G.
      Nature 357:38-46(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    5. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    6. "Cloning and characterization of GNS1: a Saccharomyces cerevisiae gene involved in synthesis of 1,3-beta-glucan in vitro."
      El-Sherbeini M., Clemas J.A.
      J. Bacteriol. 177:3227-3234(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.
    7. "ELO2 and ELO3, homologues of the Saccharomyces cerevisiae ELO1 gene, function in fatty acid elongation and are required for sphingolipid formation."
      Oh C.-S., Toke D.A., Mandala S., Martin C.E.
      J. Biol. Chem. 272:17376-17384(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.
    8. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    9. "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.
    10. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
      Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
      J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-334; SER-336 AND SER-338, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: ADR376.
    11. "Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry."
      Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.
      Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-334; SER-336 AND SER-338, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
      Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
      Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-334; SER-336 AND SER-338, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiELO2_YEAST
    AccessioniPrimary (citable) accession number: P25358
    Secondary accession number(s): D6VR44
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 1, 1992
    Last sequence update: May 1, 1992
    Last modified: October 1, 2014
    This is version 134 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 3510 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 III
      Yeast (Saccharomyces cerevisiae) chromosome III: entries and gene names

    External Data

    Dasty 3