UniProtKB - Q9JLJ5 (ELOV1_MOUSE)
Protein
Elongation of very long chain fatty acids protein 1
Gene
Elovl1
Organism
Mus musculus (Mouse)
Status
Functioni
Catalyzes the first and rate-limiting reaction of the four reactions 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 and monounsaturated 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 annotation4 Publications
Caution
The substrate specificity could be slightly different compared to human ELOVL1, AC Q9BW60. No activity toward octadecanoyl-CoA, for instance, is observed in vivo (PubMed:23689133).1 Publication1 Publication
Catalytic activityi
- a very-long-chain acyl-CoA + H+ + malonyl-CoA = a very-long-chain 3-oxoacyl-CoA + CO2 + CoAUniRule annotation2 PublicationsEC:2.3.1.199UniRule annotation2 PublicationsThis reaction proceeds in the forward1 Publication direction.
- This reaction proceeds in the forward1 Publication direction.
- This reaction proceeds in the forward1 Publication direction.
- This reaction proceeds in the forward1 Publication direction.
: fatty acid biosynthesis Pathwayi
This protein is involved in the pathway fatty acid biosynthesis, which is part of Lipid metabolism.UniRule annotation1 PublicationView all proteins of this organism that are known to be involved in the pathway fatty acid biosynthesis and in Lipid metabolism.
GO - Molecular functioni
- 3-oxo-arachidoyl-CoA synthase activity Source: UniProtKB-EC
- 3-oxo-cerotoyl-CoA synthase activity Source: UniProtKB-EC
- 3-oxo-lignoceronyl-CoA synthase activity Source: UniProtKB-EC
- fatty acid elongase activity Source: MGI
- very-long-chain 3-ketoacyl-CoA synthase activity Source: UniProtKB-EC
GO - Biological processi
- ceramide biosynthetic process Source: UniProtKB
- establishment of skin barrier Source: UniProtKB
- fatty acid elongation, monounsaturated fatty acid Source: UniProtKB
- fatty acid elongation, polyunsaturated fatty acid Source: GO_Central
- fatty acid elongation, saturated fatty acid Source: UniProtKB
- long-chain fatty-acyl-CoA biosynthetic process Source: UniProtKB-UniRule
- sphingolipid biosynthetic process Source: UniProtKB
- unsaturated fatty acid biosynthetic process Source: UniProtKB-UniRule
- very long-chain fatty acid biosynthetic process Source: UniProtKB
Keywordsi
Molecular function | Transferase |
Biological process | Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism |
Enzyme and pathway databases
Reactomei | R-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 |
UniPathwayi | UPA00094 |
Chemistry databases
SwissLipidsi | SLP:000000257 |
Names & Taxonomyi
Protein namesi | Recommended name: Elongation of very long chain fatty acids protein 1UniRule annotationCurated (EC:2.3.1.199UniRule annotation2 Publications)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 | |
Organismi | Mus musculus (Mouse) |
Taxonomic identifieri | 10090 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus |
Proteomesi |
|
Organism-specific databases
MGIi | MGI:1858959, Elovl1 |
Subcellular locationi
Endoplasmic reticulum
- Endoplasmic reticulum membrane UniRule annotation; Multi-pass membrane protein UniRule annotation
Endoplasmic reticulum
- endoplasmic reticulum Source: MGI
- integral component of endoplasmic reticulum membrane Source: GO_Central
Topology
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Transmembranei | 23 – 43 | HelicalUniRule annotationAdd BLAST | 21 | |
Transmembranei | 61 – 81 | HelicalUniRule annotationAdd BLAST | 21 | |
Transmembranei | 110 – 130 | HelicalUniRule annotationAdd BLAST | 21 | |
Transmembranei | 137 – 154 | HelicalUniRule annotationAdd BLAST | 18 | |
Transmembranei | 176 – 196 | HelicalUniRule annotationAdd BLAST | 21 | |
Transmembranei | 203 – 223 | HelicalUniRule annotationAdd BLAST | 21 | |
Transmembranei | 231 – 251 | HelicalUniRule annotationAdd BLAST | 21 |
Keywords - Cellular componenti
Endoplasmic reticulum, MembranePathology & Biotechi
Disruption phenotypei
Homozygous knockout mice die within one day after birth (PubMed:23689133). Death is caused by a skin barrier deficiency and excessive water loss that are associated with impaired formation of lipid lamellae in the stratum corneum (PubMed:23689133). In the epidermis, the levels of ceramides with fatty acid chains containing more than 26 carbons are decreased, while the levels of ceramides with less than 24 carbons are increased (PubMed:23689133).1 Publication
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000207537 | 1 – 279 | Elongation of very long chain fatty acids protein 1Add BLAST | 279 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 1 | N-acetylmethionineBy similarity | 1 |
Keywords - PTMi
AcetylationProteomic databases
EPDi | Q9JLJ5 |
jPOSTi | Q9JLJ5 |
MaxQBi | Q9JLJ5 |
PaxDbi | Q9JLJ5 |
PRIDEi | Q9JLJ5 |
PTM databases
PhosphoSitePlusi | Q9JLJ5 |
SwissPalmi | Q9JLJ5 |
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
Bgeei | ENSMUSG00000006390, Expressed in skin of back and 279 other tissues |
ExpressionAtlasi | Q9JLJ5, baseline and differential |
Genevisiblei | Q9JLJ5, MM |
Interactioni
Subunit structurei
Interacts with LASS2, TECR and HSD17B12.
UniRule annotationProtein-protein interaction databases
IntActi | Q9JLJ5, 1 interactor |
STRINGi | 10090.ENSMUSP00000006557 |
Miscellaneous databases
RNActi | Q9JLJ5, protein |
Family & Domainsi
Motif
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Motifi | 275 – 279 | Di-lysine motifUniRule annotation | 5 |
Domaini
The C-terminal di-lysine motif may confer endoplasmic reticulum localization.UniRule annotation
Sequence similaritiesi
Keywords - Domaini
Transmembrane, Transmembrane helixPhylogenomic databases
eggNOGi | KOG3071, Eukaryota |
GeneTreei | ENSGT01000000214384 |
HOGENOMi | CLU_048483_0_0_1 |
InParanoidi | Q9JLJ5 |
OMAi | YYLSCAL |
OrthoDBi | 1094172at2759 |
PhylomeDBi | Q9JLJ5 |
TreeFami | TF323454 |
Family and domain databases
HAMAPi | MF_03201, VLCF_elongase_1, 1 hit |
InterProi | View protein in InterPro IPR030457, ELO_CS IPR002076, ELO_fam IPR033681, ELOVL1 |
PANTHERi | PTHR11157, PTHR11157, 1 hit |
Pfami | View protein in Pfam PF01151, ELO, 1 hit |
PROSITEi | View protein in PROSITE PS01188, ELO, 1 hit |
(1+)i Sequence
Sequence statusi: Complete.
This entry has 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All
Q9JLJ5-1 [UniParc]FASTAAdd to basket
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
Computationally mapped potential isoform sequencesi
There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basketQ4V9V3 | Q4V9V3_MOUSE | Elongation of very long chain fatty... | Elovl1 | 202 | Annotation score: |
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 78 – 79 | YE → MR in BAB22975 (PubMed:16141072).Curated | 2 |
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 |
CCDSi | CCDS18549.1 |
RefSeqi | NP_001034264.1, NM_001039175.2 NP_001034265.1, NM_001039176.2 NP_062295.1, NM_019422.3 XP_006503296.1, XM_006503233.2 |
Genome annotation databases
Ensembli | ENSMUST00000006557; ENSMUSP00000006557; ENSMUSG00000006390 ENSMUST00000067896; ENSMUSP00000064816; ENSMUSG00000006390 ENSMUST00000167636; ENSMUSP00000126685; ENSMUSG00000006390 |
GeneIDi | 54325 |
KEGGi | mmu:54325 |
UCSCi | uc008ujz.2, mouse |
Similar proteinsi
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 |
CCDSi | CCDS18549.1 |
RefSeqi | NP_001034264.1, NM_001039175.2 NP_001034265.1, NM_001039176.2 NP_062295.1, NM_019422.3 XP_006503296.1, XM_006503233.2 |
3D structure databases
SMRi | Q9JLJ5 |
ModBasei | Search... |
Protein-protein interaction databases
IntActi | Q9JLJ5, 1 interactor |
STRINGi | 10090.ENSMUSP00000006557 |
Chemistry databases
SwissLipidsi | SLP:000000257 |
PTM databases
PhosphoSitePlusi | Q9JLJ5 |
SwissPalmi | Q9JLJ5 |
Proteomic databases
EPDi | Q9JLJ5 |
jPOSTi | Q9JLJ5 |
MaxQBi | Q9JLJ5 |
PaxDbi | Q9JLJ5 |
PRIDEi | Q9JLJ5 |
Protocols and materials databases
Antibodypediai | 32316, 201 antibodies |
Genome annotation databases
Ensembli | ENSMUST00000006557; ENSMUSP00000006557; ENSMUSG00000006390 ENSMUST00000067896; ENSMUSP00000064816; ENSMUSG00000006390 ENSMUST00000167636; ENSMUSP00000126685; ENSMUSG00000006390 |
GeneIDi | 54325 |
KEGGi | mmu:54325 |
UCSCi | uc008ujz.2, mouse |
Organism-specific databases
CTDi | 64834 |
MGIi | MGI:1858959, Elovl1 |
Phylogenomic databases
eggNOGi | KOG3071, Eukaryota |
GeneTreei | ENSGT01000000214384 |
HOGENOMi | CLU_048483_0_0_1 |
InParanoidi | Q9JLJ5 |
OMAi | YYLSCAL |
OrthoDBi | 1094172at2759 |
PhylomeDBi | Q9JLJ5 |
TreeFami | TF323454 |
Enzyme and pathway databases
UniPathwayi | UPA00094 |
Reactomei | R-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
BioGRID-ORCSi | 54325, 4 hits in 19 CRISPR screens |
ChiTaRSi | Elovl1, mouse |
PROi | PR:Q9JLJ5 |
RNActi | Q9JLJ5, protein |
SOURCEi | Search... |
Gene expression databases
Bgeei | ENSMUSG00000006390, Expressed in skin of back and 279 other tissues |
ExpressionAtlasi | Q9JLJ5, baseline and differential |
Genevisiblei | Q9JLJ5, MM |
Family and domain databases
HAMAPi | MF_03201, VLCF_elongase_1, 1 hit |
InterProi | View protein in InterPro IPR030457, ELO_CS IPR002076, ELO_fam IPR033681, ELOVL1 |
PANTHERi | PTHR11157, PTHR11157, 1 hit |
Pfami | View protein in Pfam PF01151, ELO, 1 hit |
PROSITEi | View protein in PROSITE PS01188, ELO, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | ELOV1_MOUSE | |
Accessioni | Q9JLJ5Primary (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: | December 2, 2020 | |
This is version 151 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
Reference proteomeDocuments
- MGD cross-references
Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot - PATHWAY comments
Index of metabolic and biosynthesis pathways - SIMILARITY comments
Index of protein domains and families