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Protein

Elongation of fatty acids protein 2

Gene

ELO2

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 long-chain fatty acid elongation system, which produces the 20-26-carbon very long-chain fatty acids (VLCFA) from long-chain fatty acid precursors and is involved ceramide and inositol sphingolipid biosynthesis. Component of elongase II, which elongates 16-18 carbon fatty acyl-CoAs such as palmitoyl-CoA and stearoyl-CoA to 20-22-carbon fatty acids by incorporation of malonyl-CoA (PubMed:9211877, PubMed:12684876). Involved in the synthesis of 1,3-beta-glucan (PubMed:7768822).3 Publications

Catalytic activityi

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

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
Complete GO annotation...

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.
ReactomeiREACT_188942. Linoleic acid (LA) metabolism.
REACT_188947. alpha-linolenic acid (ALA) metabolism.
REACT_239919. Synthesis of very long-chain fatty acyl-CoAs.

Names & Taxonomyi

Protein namesi
Recommended name:
Elongation of fatty acids protein 21 Publication (EC:2.3.1.1991 Publication)
Alternative name(s):
3-keto acyl-CoA synthase ELO2Curated
Fenpropimorph resistance protein 11 Publication
Glucan synthesis protein 11 Publication
Very-long-chain 3-oxoacyl-CoA synthase 2Curated
v-SNARE bypass mutant gene 2 protein1 Publication
Gene namesi
Name:ELO21 Publication
Synonyms:FEN11 Publication, GNS11 Publication, VBM21 Publication
Ordered Locus Names:YCR034WImported
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. ELO2.

Subcellular locationi

Endoplasmic reticulum membrane 2 Publications; Multi-pass membrane protein Sequence Analysis

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 6262Lumenal1 PublicationAdd
BLAST
Transmembranei63 – 8321Helical; Name=1Sequence AnalysisAdd
BLAST
Topological domaini84 – 9613Cytoplasmic1 PublicationAdd
BLAST
Transmembranei97 – 11923Helical; Name=2Sequence AnalysisAdd
BLAST
Topological domaini120 – 1223Lumenal1 Publication
Transmembranei123 – 14220Helical; Name=3Sequence AnalysisAdd
BLAST
Topological domaini143 – 1464Cytoplasmic1 Publication
Transmembranei147 – 16923Helical; Name=4Sequence AnalysisAdd
BLAST
Topological domaini170 – 20031Lumenal1 PublicationAdd
BLAST
Transmembranei201 – 22121Helical; Name=5Sequence AnalysisAdd
BLAST
Topological domaini222 – 23110Cytoplasmic1 Publication
Transmembranei232 – 25423Helical; Name=6Sequence AnalysisAdd
BLAST
Topological domaini255 – 27521Lumenal1 PublicationAdd
BLAST
Transmembranei276 – 29621Helical; Name=7Sequence AnalysisAdd
BLAST
Topological domaini297 – 34751Cytoplasmic1 PublicationAdd
BLAST

GO - Cellular componenti

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

Keywords - Cellular componenti

Endoplasmic reticulum, 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
Glycosylationi32 – 321N-linked (GlcNAc...)PROSITE-ProRule annotation
Modified residuei334 – 3341Phosphothreonine3 Publications
Modified residuei336 – 3361Phosphoserine3 Publications
Modified residuei338 – 3381Phosphoserine3 Publications

Keywords - PTMi

Glycoprotein, 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...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi344 – 3474Di-lysine-like motif1 Publication

Domaini

The C-terminal di-lysine-like 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.
InParanoidiP25358.
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

        10         20         30         40         50
MNSLVTQYAA PLFERYPQLH DYLPTLERPF FNISLWEHFD DVVTRVTNGR
60 70 80 90 100
FVPSEFQFIA GELPLSTLPP VLYAITAYYV IIFGGRFLLS KSKPFKLNGL
110 120 130 140 150
FQLHNLVLTS LSLTLLLLMV EQLVPIIVQH GLYFAICNIG AWTQPLVTLY
160 170 180 190 200
YMNYIVKFIE FIDTFFLVLK HKKLTFLHTY HHGATALLCY TQLMGTTSIS
210 220 230 240 250
WVPISLNLGV HVVMYWYYFL AARGIRVWWK EWVTRFQIIQ FVLDIGFIYF
260 270 280 290 300
AVYQKAVHLY FPILPHCGDC VGSTTATFAG CAIISSYLVL FISFYINVYK
310 320 330 340
RKGTKTSRVV KRAHGGVAAK VNEYVNVDLK NVPTPSPSPK PQHRRKR
Length:347
Mass (Da):40,002
Last modified:May 1, 1992 - v1
Checksum:i24225E49A43A1003
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

ProteinModelPortaliP25358.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

Proteomic databases

MaxQBiP25358.
PaxDbiP25358.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CYGDiYCR034w.
SGDiS000000630. ELO2.

Phylogenomic databases

eggNOGiNOG305096.
GeneTreeiENSGT00760000119122.
HOGENOMiHOG000160635.
InParanoidiP25358.
KOiK10245.
OMAiYMNYIVK.
OrthoDBiEOG7F51CG.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-17330.
YEAST:YCR034W-MONOMER.
ReactomeiREACT_188942. Linoleic acid (LA) metabolism.
REACT_188947. alpha-linolenic acid (ALA) metabolism.
REACT_239919. Synthesis of very long-chain fatty acyl-CoAs.

Miscellaneous databases

NextBioi965935.
PROiP25358.

Gene expression databases

GenevestigatoriP25358.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
  2. "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], SUBCELLULAR LOCATION.
  3. "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.
  4. "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].
  5. "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.
  6. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  7. "General resistance to sterol biosynthesis inhibitors in Saccharomyces cerevisiae."
    Ladeveze V., Marcireau C., Delourme D., Karst F.
    Lipids 28:907-912(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION.
  8. "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: FUNCTION.
  9. "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, CATALYTIC ACTIVITY.
  10. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  11. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  12. "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.
  13. "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.
  14. "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].
  15. "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].
  16. "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].
  17. 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: January 7, 2015
This is version 137 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

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.