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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: 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

GO - Biological processi

  • fatty acid biosynthetic process Source: SGD
  • fatty acid elongation Source: SGD
  • late endosome to vacuole transport via multivesicular body sorting pathway Source: SGD
  • post-Golgi vesicle-mediated transport Source: SGD
  • sphingolipid biosynthetic process Source: SGD
  • very long-chain fatty acid 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:MONOMER3O-70.
YEAST:G3O-32441-MONOMER.
YEAST:MONOMER3O-70.
ReactomeiR-SCE-2046105. Linoleic acid (LA) metabolism.
R-SCE-2046106. alpha-linolenic acid (ALA) metabolism.
R-SCE-75876. Synthesis of very long-chain fatty acyl-CoAs.

Chemistry databases

SwissLipidsiSLP:000000494.

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
Proteomesi
  • UP000002311 Componenti: Chromosome XII

Organism-specific databases

EuPathDBiFungiDB:YLR372W.
SGDiS000004364. ELO3.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 73Extracellular1 PublicationAdd BLAST73
Transmembranei74 – 94Helical; Name=1Sequence analysisAdd BLAST21
Topological domaini95 – 105Cytoplasmic1 PublicationAdd BLAST11
Transmembranei106 – 126Helical; Name=2Sequence analysisAdd BLAST21
Topological domaini127 – 155Extracellular1 PublicationAdd BLAST29
Transmembranei156 – 176Helical; Name=3Sequence analysisAdd BLAST21
Topological domaini177 – 180Cytoplasmic1 Publication4
Transmembranei181 – 201Helical; Name=4Sequence analysisAdd BLAST21
Topological domaini202 – 207Extracellular1 Publication6
Transmembranei208 – 228Helical; Name=5Sequence analysisAdd BLAST21
Topological domaini229 – 242Cytoplasmic1 PublicationAdd BLAST14
Transmembranei243 – 263Helical; Name=6Sequence analysisAdd BLAST21
Topological domaini264 – 283Extracellular1 PublicationAdd BLAST20
Transmembranei284 – 304Helical; Name=7Sequence analysisAdd BLAST21
Topological domaini305 – 345Cytoplasmic1 PublicationAdd BLAST41

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002075501 – 345Elongation of fatty acids protein 3Add BLAST345

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi2N-linked (GlcNAc...)PROSITE-ProRule annotation1
Glycosylationi20N-linked (GlcNAc...)PROSITE-ProRule annotation1
Glycosylationi66N-linked (GlcNAc...)PROSITE-ProRule annotation1

Keywords - PTMi

Glycoprotein

Proteomic databases

MaxQBiP40319.
PRIDEiP40319.

PTM databases

iPTMnetiP40319.

Interactioni

Protein-protein interaction databases

BioGridi31632. 438 interactors.
DIPiDIP-4024N.
IntActiP40319. 55 interactors.
MINTiMINT-505805.

Structurei

3D structure databases

ProteinModelPortaliP40319.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi308 – 311Di-lysine motif 11 Publication4
Motifi312 – 315Di-lysine motif 21 Publication4
Motifi316 – 319Di-lysine motif 31 Publication4

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

GeneTreeiENSGT00760000119122.
HOGENOMiHOG000160635.
InParanoidiP40319.
KOiK10246.
OMAiICHKNAF.
OrthoDBiEOG092C47LF.

Family and domain databases

InterProiIPR030457. ELO_CS.
IPR002076. ELO_fam.
[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)DescriptionActionsGraphical viewLength
Sequence conflicti35E → D in CAA55129 (PubMed:8027068).Curated1
Sequence conflicti208W → R in CAA55129 (PubMed:8027068).Curated1
Sequence conflicti330 – 331ST → FY in CAA55129 (PubMed:8027068).Curated2

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.
PIRiS48517.
RefSeqiNP_013476.3. NM_001182261.3.

3D structure databases

ProteinModelPortaliP40319.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31632. 438 interactors.
DIPiDIP-4024N.
IntActiP40319. 55 interactors.
MINTiMINT-505805.

Chemistry databases

SwissLipidsiSLP:000000494.

PTM databases

iPTMnetiP40319.

Proteomic databases

MaxQBiP40319.
PRIDEiP40319.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

EuPathDBiFungiDB:YLR372W.
SGDiS000004364. ELO3.

Phylogenomic databases

GeneTreeiENSGT00760000119122.
HOGENOMiHOG000160635.
InParanoidiP40319.
KOiK10246.
OMAiICHKNAF.
OrthoDBiEOG092C47LF.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER3O-70.
YEAST:G3O-32441-MONOMER.
YEAST:MONOMER3O-70.
ReactomeiR-SCE-2046105. Linoleic acid (LA) metabolism.
R-SCE-2046106. alpha-linolenic acid (ALA) metabolism.
R-SCE-75876. Synthesis of very long-chain fatty acyl-CoAs.

Miscellaneous databases

PROiP40319.

Family and domain databases

InterProiIPR030457. ELO_CS.
IPR002076. ELO_fam.
[Graphical view]
PANTHERiPTHR11157. PTHR11157. 1 hit.
PfamiPF01151. ELO. 1 hit.
[Graphical view]
PROSITEiPS01188. ELO. 1 hit.
[Graphical view]
ProtoNetiSearch...

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 2, 2016
This is version 139 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

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 one 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.