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P40319

- ELO3_YEAST

UniProt

P40319 - ELO3_YEAST

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Protein

Elongation of fatty acids protein 3

Gene
SUR4, APA1, ELO3, SRE1, VBM1, YLR372W, L8039.2
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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. 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. Is essential for the conversion of 24-carbon fatty acids to 26 carbon species.

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 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.

Names & Taxonomyi

Protein namesi
Recommended name:
Elongation of fatty acids protein 3 (EC:2.3.1.199)
Alternative name(s):
3-keto acyl-CoA synthase ELO3
Protein SRE1
Protein SUR4
Very-long-chain 3-oxoacyl-CoA synthase 3
v-SNARE bypass mutant gene 1 protein
Gene namesi
Name:SUR4
Synonyms:APA1, ELO3, SRE1, VBM1
Ordered Locus Names:YLR372W
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. SUR4.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 7373Extracellular Reviewed predictionAdd
BLAST
Transmembranei74 – 9421Helical; Reviewed predictionAdd
BLAST
Topological domaini95 – 10511Cytoplasmic Reviewed predictionAdd
BLAST
Transmembranei106 – 12621Helical; Reviewed predictionAdd
BLAST
Topological domaini127 – 20781Extracellular Reviewed predictionAdd
BLAST
Transmembranei208 – 22821Helical; Reviewed predictionAdd
BLAST
Topological domaini229 – 24214Cytoplasmic Reviewed predictionAdd
BLAST
Transmembranei243 – 26321Helical; Reviewed predictionAdd
BLAST
Topological domaini264 – 28320Extracellular Reviewed predictionAdd
BLAST
Transmembranei284 – 30421Helical; Reviewed predictionAdd
BLAST
Topological domaini305 – 34541Cytoplasmic Reviewed predictionAdd
BLAST

GO - Cellular componenti

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

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 345345Elongation of fatty acids protein 3PRO_0000207550Add
BLAST

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.

Family & Domainsi

Sequence similaritiesi

Belongs to the ELO family.

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG305096.
GeneTreeiENSGT00740000115027.
HOGENOMiHOG000160635.
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

MNTTTSTVIA AVADQFQSLN SSSSCFLKVH VPSIENPFGI ELWPIFSKVF    50
EYFSGYPAEQ FEFIHNKTFL ANGYHAVSII IVYYIIIFGG QAILRALNAS 100
PLKFKLLFEI HNLFLTSISL VLWLLMLEQL VPMVYHNGLF WSICSKEAFA 150
PKLVTLYYLN YLTKFVELID TVFLVLRRKK LLFLHTYHHG ATALLCYTQL 200
IGRTSVEWVV ILLNLGVHVI MYWYYFLSSC GIRVWWKQWV TRFQIIQFLI 250
DLVFVYFATY TFYAHKYLDG ILPNKGTCYG TQAAAAYGYL ILTSYLLLFI 300
SFYIQSYKKG GKKTVKKESE VSGSVASGSS TGVKTSNTKV SSRKA 345
Length:345
Mass (Da):39,465
Last modified:February 1, 1995 - v1
Checksum:i1303A9AC54BFFCC5
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti35 – 351E → D in CAA55129. 1 Publication
Sequence conflicti208 – 2081W → R in CAA55129. 1 Publication
Sequence conflicti330 – 3312ST → FY in CAA55129. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L28723 Genomic DNA. Translation: AAA35134.1.
X82033 Genomic DNA. Translation: CAA57553.1.
X78326 Genomic DNA. Translation: CAA55129.1.
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:
EMBL
GenBank
DDBJ
Links Updated
L28723 Genomic DNA. Translation: AAA35134.1 .
X82033 Genomic DNA. Translation: CAA57553.1 .
X78326 Genomic DNA. Translation: CAA55129.1 .
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. SUR4.

Phylogenomic databases

eggNOGi NOG305096.
GeneTreei ENSGT00740000115027.
HOGENOMi HOG000160635.
KOi K10246.
OMAi LIVLYYM.
OrthoDBi EOG7F51CG.

Enzyme and pathway databases

BioCyci MetaCyc:MONOMER-17331.
YEAST:G3O-32441-MONOMER.
YEAST:MONOMER3O-70.

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. "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].
  3. "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].
  4. "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.
  5. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  6. "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].
  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. "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.
  9. "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: September 3, 2014
This is version 117 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

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