UniProtKB - Q3S8M4 (ELOV4_MACMU)
Protein
Elongation of very long chain fatty acids protein 4
Gene
ELOVL4
Organism
Macaca mulatta (Rhesus macaque)
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 catalyzes the synthesis of very long chain saturated (VLC-SFA) and polyunsaturated (PUFA) fatty acids that are involved in multiple biological processes as precursors of membrane lipids and lipid mediators. May play a critical role in early brain and skin development.UniRule annotation
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.
- (19Z,22Z,25Z,28Z,31Z)-tetratriacontapentaenoyl-CoA + H+ + malonyl-CoA = 3-oxo-(21Z,24Z,27Z,30Z,33Z)-hexatriacontapentaenoyl-CoA + CO2 + CoABy similarityThis reaction proceeds in the forwardBy similarity direction.
- (4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoyl-CoA + H+ + malonyl-CoA = 3-oxo-(6Z,9Z,12Z,15Z,18Z,21Z)-tetracosahexaenoyl-CoA + CO2 + CoABy similarityThis reaction proceeds in the forwardBy similarity direction.
- (7Z,10Z,13Z,16Z)-docosatetraenoyl-CoA + H+ + malonyl-CoA = (9Z,12Z,15Z,18Z)-3-oxotetracosatetraenoyl-CoA + CO2 + CoABy similarityThis reaction proceeds in the forwardBy similarity direction.
- (11Z,14Z,17Z,20Z,23Z)-hexacosapentaenoyl-CoA + H+ + malonyl-CoA = 3-oxo-(13Z,16Z,19Z,22Z,25Z)-octacosapentaenoyl-CoA + CO2 + CoABy similarityThis reaction proceeds in the forwardBy similarity direction.
- (13Z,16Z,19Z,22Z,25Z)-octacosapentaenoyl-CoA + H+ + malonyl-CoA = 3-oxo-(15Z,18Z,21Z,24Z,27Z)-triacontapentaenoyl-CoA + CO2 + CoABy similarityThis reaction proceeds in the forwardBy similarity direction.
- (15Z,18Z,21Z,24Z,27Z)-triacontapentaenoyl-CoA + H+ + malonyl-CoA = 3-oxo-(17Z,20Z,23Z,26Z,29Z)-dotriacontapentaenoyl-CoA + CO2 + CoABy similarityThis reaction proceeds in the forwardBy similarity direction.
- (17Z,20Z,23Z,26Z,29Z)-dotriacontapentaenoyl-CoA + H+ + malonyl-CoA = 3-oxo-(19Z,22Z,25Z,28Z,31Z)-tetratriacontapentaenoyl-CoA + CO2 + CoABy similarityThis reaction proceeds in the forwardBy similarity direction.
- (21Z,24Z,27Z,30Z,33Z)-hexatriacontapentaenoyl-CoA + H+ + malonyl-CoA = 3-oxo-(23Z,26Z,29Z,32Z,35Z)-octatriacontapentaenoyl-CoA + CO2 + CoABy similarityThis reaction proceeds in the forwardBy similarity direction.
- (11Z,14Z,17Z,20Z)-hexacosatetraenoyl-CoA + H+ + malonyl-CoA = (13Z,16Z,19Z,22Z)-3-oxooctacosatetraenoyl-CoA + CO2 + CoABy similarityThis reaction proceeds in the forwardBy similarity direction.
- (13Z,16Z,19Z,22Z)-octacosatetraenoyl-CoA + H+ + malonyl-CoA = 3-oxo-(15Z,18Z,21Z,24Z)-triacontatetraenoyl-CoA + CO2 + CoABy similarityThis reaction proceeds in the forwardBy similarity direction.
- (15Z,18Z,21Z,24Z)-triacontatetraenoyl-CoA + H+ + malonyl-CoA = 3-oxo-(17Z,20Z,23Z,26Z)-dotriacontatetraenoyl-CoA + CO2 + CoABy similarityThis reaction proceeds in the forwardBy similarity direction.
- (17Z,20Z,23Z,26Z)-dotriacontatetraenoyl-CoA + H+ + malonyl-CoA = 3-oxo-(19Z,22Z,25Z,28Z)-tetratriacontatetraenoyl-CoA + CO2 + CoABy similarityThis reaction proceeds in the forwardBy similarity direction.
- (19Z,22Z,25Z,28Z)-tetratriacontatetraenoyl-CoA + H+ + malonyl-CoA = 3-oxo-(21Z,24Z,27Z,30Z)-hexatriacontatetraenoyl-CoA + CO2 + CoABy similarityThis reaction proceeds in the forwardBy similarity direction.
- (21Z,24Z,27Z,30Z)-hexatriacontatetraenoyl-CoA + H+ + malonyl-CoA = 3-oxo-(23Z,26Z,29Z,32Z)-octatriacontatetraenoyl-CoA + CO2 + CoABy similarityThis reaction proceeds in the forwardBy similarity direction.
- (6Z,9Z,12Z,15Z,18Z,21Z)-tetracosahexaenoyl-CoA + H+ + malonyl-CoA = 3-oxo-(8Z,11Z,14Z,17Z,20Z,23Z)-hexacosahexaenoyl-CoA + CO2 + CoABy similarityThis reaction proceeds in the forwardBy similarity direction.
- (8Z,11Z,14Z,17Z,20Z,23Z)-hexacosahexaenoyl-CoA + H+ + malonyl-CoA = 3-oxo-(10Z,13Z,16Z,19Z,22Z,25Z)-octacosahexaenoyl-CoA + CO2 + CoABy similarityThis reaction proceeds in the forwardBy similarity direction.
- (10Z,13Z,16Z,19Z,22Z,25Z)-octacosahexaenoyl-CoA + H+ + malonyl-CoA = 3-oxo-(12Z,15Z,18Z,21Z,24Z,27Z)-triacontahexaenoyl-CoA + CO2 + CoABy similarityThis reaction proceeds in the forwardBy similarity direction.
- (12Z,15Z,18Z,21Z,24Z,27Z)-triacontahexaenoyl-CoA + H+ + malonyl-CoA = 3-oxo-(14Z,17Z,20Z,23Z,26Z,29Z)-dotriacontahexaenoyl-CoA + CO2 + CoABy similarityThis reaction proceeds in the forwardBy similarity direction.
- (14Z,17Z,20Z,23Z,26Z,29Z)-dotriacontahexaenoyl-CoA + H+ + malonyl-CoA = 3-oxo-(16Z,19Z,22Z,25Z,28Z,31Z)-tetratriacontahexaenoyl-CoA + CO2 + CoABy similarityThis reaction proceeds in the forwardBy similarity direction.
- (16Z,19Z,22Z,25Z,28Z,31Z)-tetratriacontahexaenoyl-CoA + H+ + malonyl-CoA = 3-oxo-(18Z,21Z,24Z,27Z,30Z,33Z)-hexatriacontahexaenoyl-CoA + CO2 + CoABy similarityThis reaction proceeds in the forwardBy similarity direction.
- (9Z,12Z,15Z,18Z,21Z)-tetracosapentaenoyl-CoA + H+ + malonyl-CoA = 3-oxo-(11Z,14Z,17Z,20Z,23Z)-hexacosapentaenoyl-CoA + CO2 + CoABy similarityThis reaction proceeds in the forwardBy similarity direction.
: fatty acid biosynthesis Pathwayi
This protein is involved in the pathway 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 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: UniProtKB
- very-long-chain 3-ketoacyl-CoA synthase activity Source: UniProtKB-EC
GO - Biological processi
- fatty acid elongation, monounsaturated fatty acid Source: GO_Central
- fatty acid elongation, polyunsaturated fatty acid Source: UniProtKB
- fatty acid elongation, saturated fatty acid Source: UniProtKB
- long-chain fatty-acyl-CoA biosynthetic process Source: UniProtKB-UniRule
- 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
UniPathwayi | UPA00094 |
Names & Taxonomyi
Protein namesi | Recommended name: Elongation of very long chain fatty acids protein 4UniRule annotationCurated (EC:2.3.1.199UniRule annotation)Alternative name(s): 3-keto acyl-CoA synthase ELOVL4UniRule annotation ELOVL fatty acid elongase 4UniRule annotation Short name: ELOVL FA elongase 4UniRule annotation Very long chain 3-ketoacyl-CoA synthase 4UniRule annotation Very long chain 3-oxoacyl-CoA synthase 4UniRule annotation |
Gene namesi | Name:ELOVL4UniRule annotation |
Organismi | Macaca mulatta (Rhesus macaque) |
Taxonomic identifieri | 9544 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Cercopithecidae › Cercopithecinae › Macaca |
Proteomesi |
|
Organism-specific databases
VGNCi | VGNC:72044, ELOVL4 |
Subcellular locationi
Endoplasmic reticulum
- Endoplasmic reticulum membrane UniRule annotation; Multi-pass membrane protein UniRule annotation
Endoplasmic reticulum
- endoplasmic reticulum Source: UniProtKB
- integral component of endoplasmic reticulum membrane Source: UniProtKB
Topology
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Transmembranei | 42 – 62 | HelicalUniRule annotationAdd BLAST | 21 | |
Transmembranei | 78 – 98 | HelicalUniRule annotationAdd BLAST | 21 | |
Transmembranei | 127 – 147 | HelicalUniRule annotationAdd BLAST | 21 | |
Transmembranei | 165 – 185 | HelicalUniRule annotationAdd BLAST | 21 | |
Transmembranei | 188 – 208 | HelicalUniRule annotationAdd BLAST | 21 | |
Transmembranei | 217 – 237 | HelicalUniRule annotationAdd BLAST | 21 | |
Transmembranei | 247 – 267 | HelicalUniRule annotationAdd BLAST | 21 |
Keywords - Cellular componenti
Endoplasmic reticulum, MembranePTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000207544 | 1 – 314 | Elongation of very long chain fatty acids protein 4Add BLAST | 314 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Glycosylationi | 20 | N-linked (GlcNAc...) asparagineUniRule annotation | 1 |
Post-translational modificationi
N-glycosylated.By similarity
Keywords - PTMi
GlycoproteinExpressioni
Gene expression databases
Bgeei | ENSMMUG00000020208, Expressed in primary visual cortex and 19 other tissues |
ExpressionAtlasi | Q3S8M4, baseline |
Interactioni
Subunit structurei
Oligomer.
UniRule annotationProtein-protein interaction databases
STRINGi | 9544.ENSMMUP00000026603 |
Family & Domainsi
Motif
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Motifi | 310 – 314 | Di-lysine motifUniRule annotation | 5 |
Domaini
The C-terminal di-lysine motif confers endoplasmic reticulum localization.UniRule annotation
Sequence similaritiesi
Keywords - Domaini
Transmembrane, Transmembrane helixPhylogenomic databases
eggNOGi | KOG3071, Eukaryota |
GeneTreei | ENSGT01000000214427 |
HOGENOMi | CLU_048483_0_1_1 |
InParanoidi | Q3S8M4 |
OMAi | SIYIDCP |
OrthoDBi | 1094172at2759 |
TreeFami | TF323454 |
Family and domain databases
HAMAPi | MF_03204, VLCF_elongase_4, 1 hit |
InterProi | View protein in InterPro IPR030457, ELO_CS IPR002076, ELO_fam IPR033678, ELOVL4 |
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
Q3S8M4-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MGLLDSEPGS VLNVVSTALN DTVEFYRWTW SIADKRVENW PLMQSPWPTL
60 70 80 90 100
SISTLYLLFV WLGPKWMKDR EPFQMRLVLI IYNFGMVLLN FFIFRELFMG
110 120 130 140 150
SYNAGYSYIC QSVDYSNNVN EVRIAAALWW YFVSKGVEYL DTVFFILRKK
160 170 180 190 200
NNQVSFLHVY HHCTMFTLWW IGIKWVAGGQ AFFGAQMNSF IHVIMYSYYG
210 220 230 240 250
LAAFGPWIQK YLWWKRYLTM LQLVQFHVTI GHTALSLYTD CPFPKWMHWA
260 270 280 290 300
LIAYAISFIF LFLNFYIRTY KEPKKPKTGK TAMNGISANG VSKSEKQLVI
310
ENGKKQKNGK AKGD
Computationally mapped potential isoform sequencesi
There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basketA0A1D5Q1M6 | A0A1D5Q1M6_MACMU | Elongation of very long chain fatty... | ELOVL4 | 381 | Annotation score: |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | DQ147007 , DQ147002, DQ147003, DQ147004, DQ147005, DQ147006 Genomic DNA Translation: AAZ95094.1 |
RefSeqi | NP_001035509.1, NM_001040419.3 |
Genome annotation databases
Ensembli | ENSMMUT00000028429; ENSMMUP00000026603; ENSMMUG00000020208 ENSMMUT00000104786; ENSMMUP00000076993; ENSMMUG00000020208 |
GeneIDi | 692070 |
KEGGi | mcc:692070 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | DQ147007 , DQ147002, DQ147003, DQ147004, DQ147005, DQ147006 Genomic DNA Translation: AAZ95094.1 |
RefSeqi | NP_001035509.1, NM_001040419.3 |
3D structure databases
SMRi | Q3S8M4 |
ModBasei | Search... |
Protein-protein interaction databases
STRINGi | 9544.ENSMMUP00000026603 |
Genome annotation databases
Ensembli | ENSMMUT00000028429; ENSMMUP00000026603; ENSMMUG00000020208 ENSMMUT00000104786; ENSMMUP00000076993; ENSMMUG00000020208 |
GeneIDi | 692070 |
KEGGi | mcc:692070 |
Organism-specific databases
CTDi | 6785 |
VGNCi | VGNC:72044, ELOVL4 |
Phylogenomic databases
eggNOGi | KOG3071, Eukaryota |
GeneTreei | ENSGT01000000214427 |
HOGENOMi | CLU_048483_0_1_1 |
InParanoidi | Q3S8M4 |
OMAi | SIYIDCP |
OrthoDBi | 1094172at2759 |
TreeFami | TF323454 |
Enzyme and pathway databases
UniPathwayi | UPA00094 |
Gene expression databases
Bgeei | ENSMMUG00000020208, Expressed in primary visual cortex and 19 other tissues |
ExpressionAtlasi | Q3S8M4, baseline |
Family and domain databases
HAMAPi | MF_03204, VLCF_elongase_4, 1 hit |
InterProi | View protein in InterPro IPR030457, ELO_CS IPR002076, ELO_fam IPR033678, ELOVL4 |
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 | ELOV4_MACMU | |
Accessioni | Q3S8M4Primary (citable) accession number: Q3S8M4 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | November 22, 2005 |
Last sequence update: | October 11, 2005 | |
Last modified: | December 2, 2020 | |
This is version 99 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
- PATHWAY comments
Index of metabolic and biosynthesis pathways - SIMILARITY comments
Index of protein domains and families