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Protein

Elongation of very long chain fatty acids protein 1

Gene

Elovl1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the first and rate-limiting reaction of the four that constitute the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process, allows the addition of 2 carbons to the chain of long- and very long-chain fatty acids/VLCFAs per cycle. Condensing enzyme that exhibits activity toward saturated C18 to C26 acyl-CoA substrates, with the highest activity towards C22:0 acyl-CoA. May participate in the production of both saturated and monounsaturated VLCFAs of different chain lengths that are involved in multiple biological processes as precursors of membrane lipids and lipid mediators. Important for saturated C24:0 and monounsaturated C24:1 sphingolipid synthesis. Indirectly inhibits RPE65 via production of VLCFAs.UniRule annotation2 Publications

Catalytic activityi

A very-long-chain acyl-CoA + malonyl-CoA = CoA + a very-long-chain 3-oxoacyl-CoA + CO2.UniRule annotation

Pathwayi: fatty acid biosynthesis

This protein is involved in the pathway fatty acid biosynthesis, which is part of Lipid metabolism.UniRule annotation
View all proteins of this organism that are known to be involved in the pathway fatty acid biosynthesis and in Lipid metabolism.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism

Enzyme and pathway databases

ReactomeiR-MMU-2046105. Linoleic acid (LA) metabolism.
R-MMU-2046106. alpha-linolenic acid (ALA) metabolism.
R-MMU-75876. Synthesis of very long-chain fatty acyl-CoAs.
UniPathwayiUPA00094.

Chemistry databases

SwissLipidsiSLP:000000257.

Names & Taxonomyi

Protein namesi
Recommended name:
Elongation of very long chain fatty acids protein 1UniRule annotationCurated (EC:2.3.1.199UniRule annotationBy similarity)
Alternative name(s):
3-keto acyl-CoA synthase Elovl1UniRule annotation
ELOVL fatty acid elongase 1UniRule annotation
Short name:
ELOVL FA elongase 1UniRule annotation
Very long chain 3-ketoacyl-CoA synthase 1UniRule annotation
Very long chain 3-oxoacyl-CoA synthase 1UniRule annotation
Gene namesi
Name:Elovl1UniRule annotation
Synonyms:Ssc1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 4

Organism-specific databases

MGIiMGI:1858959. Elovl1.

Subcellular locationi

  • Endoplasmic reticulum membrane UniRule annotation; Multi-pass membrane protein UniRule annotation

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transmembranei23 – 43HelicalUniRule annotationAdd BLAST21
Transmembranei61 – 81HelicalUniRule annotationAdd BLAST21
Transmembranei110 – 130HelicalUniRule annotationAdd BLAST21
Transmembranei137 – 154HelicalUniRule annotationAdd BLAST18
Transmembranei176 – 196HelicalUniRule annotationAdd BLAST21
Transmembranei203 – 223HelicalUniRule annotationAdd BLAST21
Transmembranei231 – 251HelicalUniRule annotationAdd BLAST21

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002075371 – 279Elongation of very long chain fatty acids protein 1Add BLAST279

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineBy similarity1

Keywords - PTMi

Acetylation

Proteomic databases

EPDiQ9JLJ5.
MaxQBiQ9JLJ5.
PaxDbiQ9JLJ5.
PRIDEiQ9JLJ5.

PTM databases

PhosphoSitePlusiQ9JLJ5.
SwissPalmiQ9JLJ5.

Expressioni

Tissue specificityi

Expressed in a broad variety of tissues. Highly expressed in stomach, lung, kidney, skin and intestine. Moderately expressed in white adipose tissue, liver, spleen, brain, brown adipose tissue, heart and muscle. Weakly expressed in testis.1 Publication

Gene expression databases

BgeeiENSMUSG00000006390.
ExpressionAtlasiQ9JLJ5. baseline and differential.
GenevisibleiQ9JLJ5. MM.

Interactioni

Subunit structurei

Interacts with LASS2, TECR and HSD17B12.UniRule annotation

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000006557.

Structurei

3D structure databases

ProteinModelPortaliQ9JLJ5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi275 – 279Di-lysine motifUniRule annotation5

Domaini

The C-terminal di-lysine motif may confer endoplasmic reticulum localization.UniRule annotation

Sequence similaritiesi

Belongs to the ELO family. ELOVL1 subfamily.UniRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3071. Eukaryota.
ENOG410XRWT. LUCA.
GeneTreeiENSGT00760000119122.
HOGENOMiHOG000038120.
HOVERGENiHBG051468.
InParanoidiQ9JLJ5.
KOiK10247.
OMAiLYQEMMK.
OrthoDBiEOG091G0N2V.
PhylomeDBiQ9JLJ5.
TreeFamiTF323454.

Family and domain databases

HAMAPiMF_03201. VLCF_elongase_1. 1 hit.
InterProiIPR030457. ELO_CS.
IPR002076. ELO_fam.
IPR033681. ELOVL1.
[Graphical view]
PANTHERiPTHR11157. PTHR11157. 1 hit.
PfamiPF01151. ELO. 1 hit.
[Graphical view]
PROSITEiPS01188. ELO. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9JLJ5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEAVVNLYHE LMKHADPRIQ SYPLMGSPLL ITSILLTYVY FILSLGPRIM
60 70 80 90 100
ANRKPFQLRG FMIVYNFSLV ILSLYIVYEF LMSGWLSTYT WRCDPIDFSN
110 120 130 140 150
SPEALRMVRV AWLFMLSKVI ELMDTVIFIL RKKDGQVTFL HVFHHSVLPW
160 170 180 190 200
SWWWGIKIAP GGMGSFHAMI NSSVHVVMYL YYGLSALGPV AQPYLWWKKH
210 220 230 240 250
MTAIQLIQFV LVSLHISQYY FMPSCNYQYP IIIHLIWMYG TIFFILFSNF
260 270
WYHSYTKGKR LPRAVQQNGA PATTKVKAN
Length:279
Mass (Da):32,678
Last modified:October 1, 2000 - v1
Checksum:iCA5A1CF55FDB2F76
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti78 – 79YE → MR in BAB22975 (PubMed:16141072).Curated2

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF170907 mRNA. Translation: AAF72572.1.
BC006735 mRNA. Translation: AAH06735.1.
AK003743 mRNA. Translation: BAB22975.1.
CCDSiCCDS18549.1.
RefSeqiNP_001034264.1. NM_001039175.2.
NP_001034265.1. NM_001039176.2.
NP_062295.1. NM_019422.3.
XP_006503296.1. XM_006503233.2.
UniGeneiMm.282096.

Genome annotation databases

EnsembliENSMUST00000006557; ENSMUSP00000006557; ENSMUSG00000006390.
ENSMUST00000067896; ENSMUSP00000064816; ENSMUSG00000006390.
ENSMUST00000167636; ENSMUSP00000126685; ENSMUSG00000006390.
GeneIDi54325.
KEGGimmu:54325.
UCSCiuc008ujz.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF170907 mRNA. Translation: AAF72572.1.
BC006735 mRNA. Translation: AAH06735.1.
AK003743 mRNA. Translation: BAB22975.1.
CCDSiCCDS18549.1.
RefSeqiNP_001034264.1. NM_001039175.2.
NP_001034265.1. NM_001039176.2.
NP_062295.1. NM_019422.3.
XP_006503296.1. XM_006503233.2.
UniGeneiMm.282096.

3D structure databases

ProteinModelPortaliQ9JLJ5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000006557.

Chemistry databases

SwissLipidsiSLP:000000257.

PTM databases

PhosphoSitePlusiQ9JLJ5.
SwissPalmiQ9JLJ5.

Proteomic databases

EPDiQ9JLJ5.
MaxQBiQ9JLJ5.
PaxDbiQ9JLJ5.
PRIDEiQ9JLJ5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000006557; ENSMUSP00000006557; ENSMUSG00000006390.
ENSMUST00000067896; ENSMUSP00000064816; ENSMUSG00000006390.
ENSMUST00000167636; ENSMUSP00000126685; ENSMUSG00000006390.
GeneIDi54325.
KEGGimmu:54325.
UCSCiuc008ujz.2. mouse.

Organism-specific databases

CTDi64834.
MGIiMGI:1858959. Elovl1.

Phylogenomic databases

eggNOGiKOG3071. Eukaryota.
ENOG410XRWT. LUCA.
GeneTreeiENSGT00760000119122.
HOGENOMiHOG000038120.
HOVERGENiHBG051468.
InParanoidiQ9JLJ5.
KOiK10247.
OMAiLYQEMMK.
OrthoDBiEOG091G0N2V.
PhylomeDBiQ9JLJ5.
TreeFamiTF323454.

Enzyme and pathway databases

UniPathwayiUPA00094.
ReactomeiR-MMU-2046105. Linoleic acid (LA) metabolism.
R-MMU-2046106. alpha-linolenic acid (ALA) metabolism.
R-MMU-75876. Synthesis of very long-chain fatty acyl-CoAs.

Miscellaneous databases

PROiQ9JLJ5.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000006390.
ExpressionAtlasiQ9JLJ5. baseline and differential.
GenevisibleiQ9JLJ5. MM.

Family and domain databases

HAMAPiMF_03201. VLCF_elongase_1. 1 hit.
InterProiIPR030457. ELO_CS.
IPR002076. ELO_fam.
IPR033681. ELOVL1.
[Graphical view]
PANTHERiPTHR11157. PTHR11157. 1 hit.
PfamiPF01151. ELO. 1 hit.
[Graphical view]
PROSITEiPS01188. ELO. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiELOV1_MOUSE
AccessioniPrimary (citable) accession number: Q9JLJ5
Secondary accession number(s): Q9D1B2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 23, 2002
Last sequence update: October 1, 2000
Last modified: November 2, 2016
This is version 123 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

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.