UniProtKB - O35949 (ELOV3_MOUSE)
Protein
Elongation of very long chain fatty acids protein 3
Gene
Elovl3
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 unsaturated acyl-CoA substrates with higher activity toward C18 acyl-CoAs, especially C18:0 acyl-CoAs. May participate in the production of saturated and monounsaturated VLCFAs of different chain lengths that are involved in multiple biological processes as precursors of membrane lipids and lipid mediators. Participates in the formation of certain VLCFA and triglycerides in certain cells of the hair follicles and the sebaceous glands, required for skin barrier function. Critical enzyme for lipid accumulation and metabolic activity in brown adipocytes during the early phase of the tissue recruitment. Plays a role in lipid storage and in resistance to diet-induced obesity.UniRule annotation4 Publications
Catalytic activityi
- a very-long-chain acyl-CoA + H+ + malonyl-CoA = a very-long-chain 3-oxoacyl-CoA + CO2 + CoAUniRule annotationEC:2.3.1.199UniRule annotationThis reaction proceeds in the forwardBy similarity direction.
- This reaction proceeds in the forwardBy similarity direction.
- This reaction proceeds in the forwardBy similarity direction.
- This reaction proceeds in the forwardBy similarity direction.
- This reaction proceeds in the forwardBy similarity direction.
- (9Z,12Z)-octadecadienoyl-CoA + H+ + malonyl-CoA = (11Z,14Z)-3-oxoicosa-11,14-dienoyl-CoA + CO2 + CoABy similarityThis reaction proceeds in the forwardBy similarity direction.
- (9Z,12Z,15Z)-octadecatrienoyl-CoA + H+ + malonyl-CoA = (11Z,14Z,17Z)-3-oxoeicosatrienoyl-CoA + CO2 + CoABy similarityThis reaction proceeds in the forwardBy similarity direction.
- This reaction proceeds in the forwardBy similarity direction.
- This reaction proceeds in the forwardBy similarity direction.
: polyunsaturated fatty acid biosynthesis Pathwayi
This protein is involved in the pathway polyunsaturated fatty acid biosynthesis, which is part of Lipid metabolism.UniRule annotationView all proteins of this organism that are known to be involved in the pathway polyunsaturated 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: GO_Central
- very-long-chain 3-ketoacyl-CoA synthase activity Source: UniProtKB-EC
GO - Biological processi
- fatty acid elongation, monounsaturated fatty acid Source: UniProtKB
- fatty acid elongation, polyunsaturated fatty acid Source: MGI
- fatty acid elongation, saturated fatty acid Source: UniProtKB
- long-chain fatty-acyl-CoA biosynthetic process Source: UniProtKB-UniRule
- positive regulation of cold-induced thermogenesis Source: YuBioLab
- sphingolipid biosynthetic process Source: GO_Central
- 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 | UPA00658 |
Names & Taxonomyi
Protein namesi | Recommended name: Elongation of very long chain fatty acids protein 3UniRule annotationCurated (EC:2.3.1.199UniRule annotationBy similarity)Alternative name(s): 3-keto acyl-CoA synthase Elovl3UniRule annotation CIN-2 Cold-inducible glycoprotein of 30 kDa ELOVL fatty acid elongase 3UniRule annotation Short name: ELOVL FA elongase 3UniRule annotation Very long chain 3-ketoacyl-CoA synthase 3UniRule annotation Very long chain 3-oxoacyl-CoA synthase 3UniRule 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:1195976, Elovl3 |
Subcellular locationi
Endoplasmic reticulum
- Endoplasmic reticulum membrane UniRule annotation1 Publication; Multi-pass membrane protein UniRule annotation
Endoplasmic reticulum
- endoplasmic reticulum Source: UniProtKB
- integral component of endoplasmic reticulum membrane Source: GO_Central
Topology
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Transmembranei | 30 – 50 | HelicalUniRule annotationAdd BLAST | 21 | |
Transmembranei | 67 – 87 | HelicalUniRule annotationAdd BLAST | 21 | |
Transmembranei | 116 – 136 | HelicalUniRule annotationAdd BLAST | 21 | |
Transmembranei | 141 – 161 | HelicalUniRule annotationAdd BLAST | 21 | |
Transmembranei | 165 – 187 | HelicalUniRule annotationAdd BLAST | 23 | |
Transmembranei | 199 – 219 | HelicalUniRule annotationAdd BLAST | 21 | |
Transmembranei | 236 – 256 | HelicalUniRule annotationAdd BLAST | 21 |
Keywords - Cellular componenti
Endoplasmic reticulum, MembranePathology & Biotechi
Disruption phenotypei
Mutant mice grow normally and are fertile. They display a sparse hair coat, a hyperplastic pilosebaceous system and their hair lipid content is disturbed with exceptionally high levels of eicosenoic acid (20:1). In the triglyceride fraction, fatty acids longer than 20 carbon atoms are almost undetectable. As a result, mice exhibited a severe defect in water repulsion and increased trans-epidermal water loss. When exposed to cold stress, mutants exhibit a significantly reduced VLCFA elongation activity in brown adipose tissue, but only during the initial phase. Cold-acclimated mutants are equally efficient as normal mice at elongating fatty acids. Mutant mice are lean and resistant to diet-induced weight gain, they show normal food intake but increased metabolic rate, and show reduced hepatic lipogenesis and triglycerides synthesis.3 Publications
Chemistry databases
ChEMBLi | CHEMBL5775 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000207541 | 1 – 271 | Elongation of very long chain fatty acids protein 3Add BLAST | 271 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Glycosylationi | 6 | N-linked (GlcNAc...) asparagineUniRule annotation2 Publications | 1 |
Post-translational modificationi
N-Glycosylated.UniRule annotation1 Publication
Keywords - PTMi
GlycoproteinProteomic databases
jPOSTi | O35949 |
MaxQBi | O35949 |
PaxDbi | O35949 |
PRIDEi | O35949 |
PTM databases
GlyGeni | O35949, 1 site |
iPTMneti | O35949 |
PhosphoSitePlusi | O35949 |
Expressioni
Tissue specificityi
Expressed in brown adipose tissue and liver. In the skin, strong expressed in the cells of the inner layer of the outer root sheath of the hair follicles and in the sebocytes of the sebaceous glands. Hardly detectable in the epidermis and not at all in fibroblasts.2 Publications
Inductioni
Strongly up-regulated in brown adipose tissue in conditions of brown fat recruitment, such as cold stress, perinatal development and after diet-induced thermogenesis. A synergistic action of both catecholamines and glucocorticoids is required for the induction.
Gene expression databases
Bgeei | ENSMUSG00000038754, Expressed in lip and 82 other tissues |
ExpressionAtlasi | O35949, baseline and differential |
Genevisiblei | O35949, MM |
Interactioni
Protein-protein interaction databases
STRINGi | 10090.ENSMUSP00000036357 |
Chemistry databases
BindingDBi | O35949 |
Miscellaneous databases
RNActi | O35949, protein |
Family & Domainsi
Sequence similaritiesi
Keywords - Domaini
Transmembrane, Transmembrane helixPhylogenomic databases
eggNOGi | KOG3072, Eukaryota |
GeneTreei | ENSGT01000000214384 |
HOGENOMi | CLU_048483_1_1_1 |
InParanoidi | O35949 |
OMAi | QPYNFEL |
OrthoDBi | 1094172at2759 |
PhylomeDBi | O35949 |
TreeFami | TF106467 |
Family and domain databases
HAMAPi | MF_03203, VLCF_elongase_3, 1 hit |
InterProi | View protein in InterPro IPR030457, ELO_CS IPR002076, ELO_fam IPR033679, ELOVL3 |
PANTHERi | PTHR11157, PTHR11157, 1 hit PTHR11157:SF68, PTHR11157:SF68, 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
O35949-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MDTSMNFSRG LKMDLMQPYD FETFQDLRPF LEEYWVSSFL IVVVYLLLIV
60 70 80 90 100
VGQTYMRTRK SFSLQRPLIL WSFFLAIFSI LGTLRMWKFM ATVMFTVGLK
110 120 130 140 150
QTVCFAIYTD DAVVRFWSFL FLLSKVVELG DTAFIILRKR PLIFVHWYHH
160 170 180 190 200
STVLLFTSFG YKNKVPSGGW FMTMNFGVHS VMYTYYTMKA AKLKHPNLLP
210 220 230 240 250
MVITSLQILQ MVLGTIFGIL NYIWRQEKGC HTTTEHFFWS FMLYGTYFIL
260 270
FAHFFHRAYL RPKGKVASKS Q
Computationally mapped potential isoform sequencesi
There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basketA0A498WFQ4 | A0A498WFQ4_MOUSE | Elongation of very long chain fatty... | Elovl3 | 248 | Annotation score: |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | U97107 mRNA Translation: AAC06127.1 AF054504 Genomic DNA Translation: AAD51088.1 BC016468 mRNA Translation: AAH16468.1 |
CCDSi | CCDS29871.1 |
RefSeqi | NP_031729.1, NM_007703.2 |
Genome annotation databases
Ensembli | ENSMUST00000237098; ENSMUSP00000157465; ENSMUSG00000038754 |
GeneIDi | 12686 |
KEGGi | mmu:12686 |
UCSCi | uc008hsk.1, mouse |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | U97107 mRNA Translation: AAC06127.1 AF054504 Genomic DNA Translation: AAD51088.1 BC016468 mRNA Translation: AAH16468.1 |
CCDSi | CCDS29871.1 |
RefSeqi | NP_031729.1, NM_007703.2 |
3D structure databases
ModBasei | Search... |
SWISS-MODEL-Workspacei | Submit a new modelling project... |
Protein-protein interaction databases
STRINGi | 10090.ENSMUSP00000036357 |
Chemistry databases
BindingDBi | O35949 |
ChEMBLi | CHEMBL5775 |
PTM databases
GlyGeni | O35949, 1 site |
iPTMneti | O35949 |
PhosphoSitePlusi | O35949 |
Proteomic databases
jPOSTi | O35949 |
MaxQBi | O35949 |
PaxDbi | O35949 |
PRIDEi | O35949 |
Protocols and materials databases
Antibodypediai | 31401, 176 antibodies |
Genome annotation databases
Ensembli | ENSMUST00000237098; ENSMUSP00000157465; ENSMUSG00000038754 |
GeneIDi | 12686 |
KEGGi | mmu:12686 |
UCSCi | uc008hsk.1, mouse |
Organism-specific databases
CTDi | 83401 |
MGIi | MGI:1195976, Elovl3 |
Phylogenomic databases
eggNOGi | KOG3072, Eukaryota |
GeneTreei | ENSGT01000000214384 |
HOGENOMi | CLU_048483_1_1_1 |
InParanoidi | O35949 |
OMAi | QPYNFEL |
OrthoDBi | 1094172at2759 |
PhylomeDBi | O35949 |
TreeFami | TF106467 |
Enzyme and pathway databases
UniPathwayi | UPA00658 |
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 | 12686, 0 hits in 17 CRISPR screens |
PROi | PR:O35949 |
RNActi | O35949, protein |
SOURCEi | Search... |
Gene expression databases
Bgeei | ENSMUSG00000038754, Expressed in lip and 82 other tissues |
ExpressionAtlasi | O35949, baseline and differential |
Genevisiblei | O35949, MM |
Family and domain databases
HAMAPi | MF_03203, VLCF_elongase_3, 1 hit |
InterProi | View protein in InterPro IPR030457, ELO_CS IPR002076, ELO_fam IPR033679, ELOVL3 |
PANTHERi | PTHR11157, PTHR11157, 1 hit PTHR11157:SF68, PTHR11157:SF68, 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 | ELOV3_MOUSE | |
Accessioni | O35949Primary (citable) accession number: O35949 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | January 23, 2002 |
Last sequence update: | January 1, 1998 | |
Last modified: | December 2, 2020 | |
This is version 154 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