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P25358 (ELO2_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 125. 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·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:FEN1
Synonyms:ELO2, GNS1, VBM2
Ordered Locus Names:YCR034W
ORF Names:YCR34W, YCR521
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces ›

Protein attributes

Sequence length347 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 activity

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

Subcellular location

Membrane; Multi-pass membrane protein.

Miscellaneous

Present with 3510 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the ELO family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 347347Elongation of fatty acids protein 2
PRO_0000207549

Regions

Topological domain1 – 6262Extracellular Potential
Transmembrane63 – 8321Helical; Potential
Topological domain84 – 10724Cytoplasmic Potential
Transmembrane108 – 12821Helical; Potential
Topological domain129 – 20072Extracellular Potential
Transmembrane201 – 22121Helical; Potential
Topological domain222 – 24423Cytoplasmic Potential
Transmembrane245 – 26521Helical; Potential
Topological domain266 – 27510Extracellular Potential
Transmembrane276 – 29621Helical; Potential
Topological domain297 – 34751Cytoplasmic Potential
Compositional bias333 – 3419Pro-rich

Amino acid modifications

Modified residue3341Phosphothreonine Ref.8 Ref.11 Ref.12 Ref.13 Ref.14
Modified residue3361Phosphoserine Ref.8 Ref.11 Ref.12 Ref.13 Ref.14
Modified residue3381Phosphoserine Ref.8 Ref.11 Ref.12 Ref.13 Ref.14

Sequences

Sequence LengthMass (Da)Tools
P25358 [UniParc].

Last modified May 1, 1992. Version 1.
Checksum: 24225E49A43A1003

FASTA34740,002
        10         20         30         40         50         60 
MNSLVTQYAA PLFERYPQLH DYLPTLERPF FNISLWEHFD DVVTRVTNGR FVPSEFQFIA 

        70         80         90        100        110        120 
GELPLSTLPP VLYAITAYYV IIFGGRFLLS KSKPFKLNGL FQLHNLVLTS LSLTLLLLMV 

       130        140        150        160        170        180 
EQLVPIIVQH GLYFAICNIG AWTQPLVTLY YMNYIVKFIE FIDTFFLVLK HKKLTFLHTY 

       190        200        210        220        230        240 
HHGATALLCY TQLMGTTSIS WVPISLNLGV HVVMYWYYFL AARGIRVWWK EWVTRFQIIQ 

       250        260        270        280        290        300 
FVLDIGFIYF AVYQKAVHLY FPILPHCGDC VGSTTATFAG CAIISSYLVL FISFYINVYK 

       310        320        330        340 
RKGTKTSRVV KRAHGGVAAK VNEYVNVDLK NVPTPSPSPK PQHRRKR

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
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]"Phosphoproteome analysis by mass spectrometry and its application to Saccharomyces cerevisiae."
Ficarro S.B., McCleland M.L., Stukenberg P.T., Burke D.J., Ross M.M., Shabanowitz J., Hunt D.F., White F.M.
Nat. Biotechnol. 20:301-305(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-334; SER-336 AND SER-338, MASS SPECTROMETRY.
Strain: 2124.
[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]"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.
[11]"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, MASS SPECTROMETRY.
Strain: ADR376.
[12]"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, MASS SPECTROMETRY.
[13]"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases."
Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.
Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-334; SER-336 AND SER-338, MASS SPECTROMETRY.
[14]"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 THR-334; SER-336 AND SER-338, MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		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.
PIRS12916.
RefSeqNP_009963.1. NM_001178748.1.

3D structure databases

ProteinModelPortalP25358.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-4176N.
MINTMINT-547542.
STRING4932.YCR034W.

Proteomic databases

PaxDbP25358.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYCR034W; YCR034W; YCR034W.
GeneID850400.
KEGGsce:YCR034W.

Organism-specific databases

CYGDYCR034w.
SGDS000000630. FEN1.

Phylogenomic databases

eggNOGNOG305096.
GeneTreeENSGT00690000101823.
HOGENOMHOG000160635.
KOK10245.
OMAGTTSISW.
OrthoDBEOG4HQHT1.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-17330.

Gene expression databases

GenevestigatorP25358.
GermOnlineYCR034W. Saccharomyces cerevisiae.

Family and domain databases

InterProIPR002076. GNS1_SUR4.
[Graphical view]
PANTHERPTHR11157. PTHR11157. 1 hit.
PfamPF01151. ELO. 1 hit.
[Graphical view]
PROSITEPS01188. ELO. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio965935.

Entry information

Entry nameELO2_YEAST
AccessionPrimary (citable) accession number: P25358
Secondary accession number(s): D6VR44
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: May 1, 1992
Last modified: April 3, 2013
This is version 125 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast

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

Yeast chromosome III

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

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents