Elongation of fatty acids protein 3 - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Contribute

Send feedback

Read comments (?) or add your own

P40319 (ELO3_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 108. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

text xml rdf/xml gff fasta

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

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 names

Name:	SUR4
Synonyms:	APA1, ELO3, SRE1, VBM1
Ordered Locus Names:	YLR372W
ORF Names:	L8039.2

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces ›

Protein attributes

Sequence length	345 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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 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 Probable.
Sequence similarities	Belongs to the ELO family.

Ontologies

Keywords
Biological process	Fatty acid biosynthesis Fatty acid metabolism Lipid biosynthesis Lipid metabolism
Cellular component	Membrane
Domain	Transmembrane Transmembrane helix
Molecular function	Transferase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	fatty acid elongation Inferred from mutant phenotype Ref.7. Source: SGD post-Golgi vesicle-mediated transport Inferred from genetic interaction Ref.6. Source: SGD sphingolipid biosynthetic process Inferred from mutant phenotype Ref.7. Source: SGD
Cellular_component	endoplasmic reticulum Inferred from direct assay PubMed 12087109. Source: SGD integral to membrane Inferred from sequence model PubMed 12192589. Source: SGD
Molecular_function	fatty acid elongase activity Inferred from mutant phenotype PubMed 12684876. Source: SGD
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 345

345

Elongation of fatty acids protein 3

PRO_0000207550

Regions

Topological domain

1 – 73

Extracellular Potential

Transmembrane

74 – 94

Helical; Potential

Topological domain

95 – 105

Cytoplasmic Potential

Transmembrane

106 – 126

Helical; Potential

Topological domain

127 – 207

Extracellular Potential

Transmembrane

208 – 228

Helical; Potential

Topological domain

229 – 242

Cytoplasmic Potential

Transmembrane

243 – 263

Helical; Potential

Topological domain

264 – 283

Extracellular Potential

Transmembrane

284 – 304

Helical; Potential

Topological domain

305 – 345

Cytoplasmic Potential

Amino acid modifications

Modified residue

327

Phosphoserine Ref.9

Experimental info

Sequence conflict

E → D in CAA55129. Ref.3

Sequence conflict

208

W → R in CAA55129. Ref.3

Sequence conflict

330 – 331

ST → FY in CAA55129. Ref.3

Sequences

Sequence

Length

Mass (Da)

Tools

P40319 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: 1303A9AC54BFFCC5
Show »

FASTA

345

39,465

        10         20         30         40         50         60 
MNTTTSTVIA AVADQFQSLN SSSSCFLKVH VPSIENPFGI ELWPIFSKVF EYFSGYPAEQ 

        70         80         90        100        110        120 
FEFIHNKTFL ANGYHAVSII IVYYIIIFGG QAILRALNAS PLKFKLLFEI HNLFLTSISL 

       130        140        150        160        170        180 
VLWLLMLEQL VPMVYHNGLF WSICSKEAFA PKLVTLYYLN YLTKFVELID TVFLVLRRKK 

       190        200        210        220        230        240 
LLFLHTYHHG ATALLCYTQL IGRTSVEWVV ILLNLGVHVI MYWYYFLSSC GIRVWWKQWV 

       250        260        270        280        290        300 
TRFQIIQFLI DLVFVYFATY TFYAHKYLDG ILPNKGTCYG TQAAAAYGYL ILTSYLLLFI 

       310        320        330        340 
SFYIQSYKKG GKKTVKKESE VSGSVASGSS TGVKTSNTKV SSRKA

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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. Hoheisel J.D. Nature 387:87-90(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[5]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases 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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-327, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	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.
PIR	S48517.
RefSeq	NP_013476.3. NM_001182261.3.
3D structure databases
ProteinModelPortal	P40319.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-4024N.
IntAct	P40319. 29 interactions.
MINT	MINT-505805.
STRING	4932.YLR372W.
Proteomic databases
PaxDb	P40319.
PeptideAtlas	P40319.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YLR372W; YLR372W; YLR372W.
GeneID	851087.
KEGG	sce:YLR372W. sce:YLR375W.
Organism-specific databases
CYGD	YLR372w.
SGD	S000004364. SUR4.
Phylogenomic databases
eggNOG	NOG305096.
GeneTree	ENSGT00690000101823.
HOGENOM	HOG000160635.
KO	K10246.
OMA	AFAPKLV.
OrthoDB	EOG4HQHT1.
Enzyme and pathway databases
BioCyc	MetaCyc:MONOMER-17331.
Gene expression databases
Genevestigator	P40319.
GermOnline	YLR372W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR002076. GNS1_SUR4. [Graphical view]
PANTHER	PTHR11157. PTHR11157. 1 hit.
Pfam	PF01151. ELO. 1 hit. [Graphical view]
PROSITE	PS01188. ELO. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	967756.

Entry information

Entry name

ELO3_YEAST

Accession

Primary (citable) accession number: P40319
Secondary accession number(s): D6VZ09

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	February 1, 1995
Last modified:	April 3, 2013
This is version 108 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

Yeast

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

Yeast chromosome XII

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

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents