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P40319

- ELO3_YEAST

UniProt

P40319 - ELO3_YEAST

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Protein

Elongation of fatty acids protein 3

Gene

ELO3

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - 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 III, which synthesizes 20-26-carbon fatty acids from 18-carbon-fatty acyl-CoA primers such as stearoyl-CoA by incorporation of malonyl-CoA (PubMed:9211877, PubMed:12684876). Affects plasma membrane H+-ATPase activity. May act on a glucose-signaling pathway that controls the expression of several genes that are transcriptionally regulated by glucose such as PMA1, HXT3 and SNF3 (PubMed:8027068).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 biosynthetic process Source: SGD
  2. fatty acid elongation Source: SGD
  3. post-Golgi vesicle-mediated transport Source: SGD
  4. sphingolipid biosynthetic process 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-17331.
YEAST:G3O-32441-MONOMER.
YEAST:MONOMER3O-70.
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 31 Publication (EC:2.3.1.1991 Publication)
Alternative name(s):
3-keto acyl-CoA synthase ELO3Curated
Affecting plasma membrane ATPase activity protein 11 Publication
Suppressor of RAD3 essential function protein 11 Publication
Suppressor of Rvs161 and Rvs167 mutations protein 41 Publication
Very-long-chain 3-oxoacyl-CoA synthase 3Curated
v-SNARE bypass mutant gene 1 protein1 Publication
Gene namesi
Name:ELO31 Publication
Synonyms:APA11 Publication, SRE11 Publication, SUR41 Publication, VBM11 Publication
Ordered Locus Names:YLR372WImported
ORF Names:L8039.2
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome XII

Organism-specific databases

CYGDiYLR372w.
SGDiS000004364. ELO3.

Subcellular locationi

Endoplasmic reticulum membrane 3 Publications; Multi-pass membrane protein Curated

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 7373Extracellular1 PublicationAdd
BLAST
Transmembranei74 – 9421Helical; Name=1Sequence AnalysisAdd
BLAST
Topological domaini95 – 10511Cytoplasmic1 PublicationAdd
BLAST
Transmembranei106 – 12621Helical; Name=2Sequence AnalysisAdd
BLAST
Topological domaini127 – 15529Extracellular1 PublicationAdd
BLAST
Transmembranei156 – 17621Helical; Name=3Sequence AnalysisAdd
BLAST
Topological domaini177 – 1804Cytoplasmic1 Publication
Transmembranei181 – 20121Helical; Name=4Sequence AnalysisAdd
BLAST
Topological domaini202 – 2076Extracellular1 Publication
Transmembranei208 – 22821Helical; Name=5Sequence AnalysisAdd
BLAST
Topological domaini229 – 24214Cytoplasmic1 PublicationAdd
BLAST
Transmembranei243 – 26321Helical; Name=6Sequence AnalysisAdd
BLAST
Topological domaini264 – 28320Extracellular1 PublicationAdd
BLAST
Transmembranei284 – 30421Helical; Name=7Sequence AnalysisAdd
BLAST
Topological domaini305 – 34541Cytoplasmic1 PublicationAdd
BLAST

GO - Cellular componenti

  1. endoplasmic reticulum Source: SGD
  2. 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 – 345345Elongation of fatty acids protein 3PRO_0000207550Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi2 – 21N-linked (GlcNAc...)PROSITE-ProRule annotation
Glycosylationi20 – 201N-linked (GlcNAc...)PROSITE-ProRule annotation
Glycosylationi66 – 661N-linked (GlcNAc...)PROSITE-ProRule annotation

Keywords - PTMi

Glycoprotein

Proteomic databases

MaxQBiP40319.
PaxDbiP40319.
PeptideAtlasiP40319.

Expressioni

Gene expression databases

GenevestigatoriP40319.

Interactioni

Protein-protein interaction databases

BioGridi31632. 436 interactions.
DIPiDIP-4024N.
IntActiP40319. 55 interactions.
MINTiMINT-505805.
STRINGi4932.YLR372W.

Structurei

3D structure databases

ProteinModelPortaliP40319.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi308 – 3114Di-lysine motif 11 Publication
Motifi312 – 3154Di-lysine motif 21 Publication
Motifi316 – 3194Di-lysine motif 31 Publication

Domaini

The C-terminal di-lysine motifs 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.
InParanoidiP40319.
KOiK10246.
OMAiLIVLYYM.
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.

P40319-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MNTTTSTVIA AVADQFQSLN SSSSCFLKVH VPSIENPFGI ELWPIFSKVF
60 70 80 90 100
EYFSGYPAEQ FEFIHNKTFL ANGYHAVSII IVYYIIIFGG QAILRALNAS
110 120 130 140 150
PLKFKLLFEI HNLFLTSISL VLWLLMLEQL VPMVYHNGLF WSICSKEAFA
160 170 180 190 200
PKLVTLYYLN YLTKFVELID TVFLVLRRKK LLFLHTYHHG ATALLCYTQL
210 220 230 240 250
IGRTSVEWVV ILLNLGVHVI MYWYYFLSSC GIRVWWKQWV TRFQIIQFLI
260 270 280 290 300
DLVFVYFATY TFYAHKYLDG ILPNKGTCYG TQAAAAYGYL ILTSYLLLFI
310 320 330 340
SFYIQSYKKG GKKTVKKESE VSGSVASGSS TGVKTSNTKV SSRKA
Length:345
Mass (Da):39,465
Last modified:February 1, 1995 - v1
Checksum:i1303A9AC54BFFCC5
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti35 – 351E → D in CAA55129. (PubMed:8027068)Curated
Sequence conflicti208 – 2081W → R in CAA55129. (PubMed:8027068)Curated
Sequence conflicti330 – 3312ST → FY in CAA55129. (PubMed:8027068)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L28723 Genomic DNA. Translation: AAA35134.1.
X78326 Genomic DNA. Translation: CAA55129.1.
X82033 Genomic DNA. Translation: CAA57553.1.
U19103 Genomic DNA. Translation: AAB67563.1.
AF011409 Genomic DNA. Translation: AAC28398.1.
BK006945 Genomic DNA. Translation: DAA09675.1.
PIRiS48517.
RefSeqiNP_013476.3. NM_001182261.3.

Genome annotation databases

EnsemblFungiiYLR372W; YLR372W; YLR372W.
GeneIDi851087.
KEGGisce:YLR372W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L28723 Genomic DNA. Translation: AAA35134.1 .
X78326 Genomic DNA. Translation: CAA55129.1 .
X82033 Genomic DNA. Translation: CAA57553.1 .
U19103 Genomic DNA. Translation: AAB67563.1 .
AF011409 Genomic DNA. Translation: AAC28398.1 .
BK006945 Genomic DNA. Translation: DAA09675.1 .
PIRi S48517.
RefSeqi NP_013476.3. NM_001182261.3.

3D structure databases

ProteinModelPortali P40319.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 31632. 436 interactions.
DIPi DIP-4024N.
IntActi P40319. 55 interactions.
MINTi MINT-505805.
STRINGi 4932.YLR372W.

Proteomic databases

MaxQBi P40319.
PaxDbi P40319.
PeptideAtlasi P40319.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YLR372W ; YLR372W ; YLR372W .
GeneIDi 851087.
KEGGi sce:YLR372W.

Organism-specific databases

CYGDi YLR372w.
SGDi S000004364. ELO3.

Phylogenomic databases

eggNOGi NOG305096.
GeneTreei ENSGT00760000119122.
HOGENOMi HOG000160635.
InParanoidi P40319.
KOi K10246.
OMAi LIVLYYM.
OrthoDBi EOG7F51CG.

Enzyme and pathway databases

BioCyci MetaCyc:MONOMER-17331.
YEAST:G3O-32441-MONOMER.
YEAST:MONOMER3O-70.
Reactomei REACT_188942. Linoleic acid (LA) metabolism.
REACT_188947. alpha-linolenic acid (ALA) metabolism.
REACT_239919. Synthesis of very long-chain fatty acyl-CoAs.

Miscellaneous databases

NextBioi 967756.
PROi P40319.

Gene expression databases

Genevestigatori P40319.

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

« Hide 'large scale' publications
  1. Revardel E.
    Thesis (1994), University of Bordeaux II, France
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 44827 / SKQ2N.
  2. "Transcriptional control of yeast plasma membrane H(+)-ATPase by glucose. Cloning and characterization of a new gene involved in this regulation."
    Garcia-Arranz M., Maldonado A.M., Mazon M.J., Portillo F.
    J. Biol. Chem. 269:18076-18082(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
  3. "The immunosuppressant SR 31747 blocks cell proliferation by inhibiting a steroid isomerase in Saccharomyces cerevisiae."
    Silve S., Leplatois P., Josse A., Dupuy P.-H., Lanau C., Kaghad M., Dhers C., Picard C., Rahier A., Taton M., Le Fur G., Caput D., Ferrara P., Loison G.
    Mol. Cell. Biol. 16:2719-2727(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "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.
  5. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII."
    Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W., Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K., Heuss-Neitzel D., Hilbert H.
    , Hilger F., Kleine K., Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A., Hani J., Hoheisel J.D.
    Nature 387:87-90(1997) [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. "The RAD3 gene of Saccharomyces cerevisiae: isolation and characterization of a temperature-sensitive mutant in the essential function and of extragenic suppressors of this mutant."
    Naumovski L., Friedberg E.C.
    Mol. Gen. Genet. 209:458-466(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: GENE NAME.
  8. "Yeast mutants affected in viability upon starvation have a modified phospholipid composition."
    Desfarges L., Durrens P., Juguelin H., Cassagne C., Bonneu M., Aigle M.
    Yeast 9:267-277(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION.
  9. "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.
  10. "The Saccharomyces cerevisiae YBR159w gene encodes the 3-ketoreductase of the microsomal fatty acid elongase."
    Han G., Gable K., Kohlwein S.D., Beaudoin F., Napier J.A., Dunn T.M.
    J. Biol. Chem. 277:35440-35449(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  11. "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.
  12. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  13. "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.
  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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiELO3_YEAST
AccessioniPrimary (citable) accession number: P40319
Secondary accession number(s): D6VZ09
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: November 26, 2014
This is version 120 of the entry and version 1 of the sequence. [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 XII
    Yeast (Saccharomyces cerevisiae) chromosome XII: entries and gene names

External Data

Dasty 3