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Protein

Elongation of very long chain fatty acids protein 4

Gene

Elovl4

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 specifically elongates C24:0 and C26:0 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. May play a critical role in early brain and skin development.UniRule annotation

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-75876. Synthesis of very long-chain fatty acyl-CoAs.
UniPathwayiUPA00094.

Chemistry databases

SwissLipidsiSLP:000000264.

Names & Taxonomyi

Protein namesi
Recommended name:
Elongation of very long chain fatty acids protein 4UniRule annotationCurated (EC:2.3.1.199UniRule annotationBy similarity)
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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 9

Organism-specific databases

MGIiMGI:1933331. Elovl4.

Subcellular locationi

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

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transmembranei42 – 62HelicalUniRule annotationAdd BLAST21
Transmembranei78 – 98HelicalUniRule annotationAdd BLAST21
Transmembranei127 – 147HelicalUniRule annotationAdd BLAST21
Transmembranei165 – 185HelicalUniRule annotationAdd BLAST21
Transmembranei188 – 208HelicalUniRule annotationAdd BLAST21
Transmembranei217 – 237HelicalUniRule annotationAdd BLAST21
Transmembranei246 – 266HelicalUniRule annotationAdd BLAST21

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002075451 – 312Elongation of very long chain fatty acids protein 4Add BLAST312

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi20N-linked (GlcNAc...)UniRule annotation1
Glycosylationi292N-linked (GlcNAc...)UniRule annotation1

Keywords - PTMi

Glycoprotein

Proteomic databases

PaxDbiQ9EQC4.
PRIDEiQ9EQC4.

PTM databases

PhosphoSitePlusiQ9EQC4.

Expressioni

Tissue specificityi

Expressed in the retina, exclusively in photoreceptor cells and in the brain, skin, testis and lens.1 Publication

Developmental stagei

Expressed in the ocular tissues of the retina at 10.5 dpc and becomes restricted predominantly to the photoreceptor layer in the mature retina (at protein level). Expressed in the embryo at 7 dpc.1 Publication

Gene expression databases

BgeeiENSMUSG00000032262.
ExpressionAtlasiQ9EQC4. baseline and differential.
GenevisibleiQ9EQC4. MM.

Interactioni

Subunit structurei

Oligomer.UniRule annotation

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000034796.

Structurei

3D structure databases

ProteinModelPortaliQ9EQC4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi308 – 312Di-lysine motifUniRule annotation5

Domaini

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

Sequence similaritiesi

Belongs to the ELO family. ELOVL4 subfamily.UniRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3071. Eukaryota.
ENOG410XRWT. LUCA.
GeneTreeiENSGT00760000119122.
HOGENOMiHOG000038120.
HOVERGENiHBG051468.
InParanoidiQ9EQC4.
KOiK10249.
OMAiFYVRTYK.
OrthoDBiEOG091G0N2V.
TreeFamiTF323454.

Family and domain databases

HAMAPiMF_03204. VLCF_elongase_4. 1 hit.
InterProiIPR030457. ELO_CS.
IPR002076. ELO_fam.
IPR033678. ELOVL4.
[Graphical view]
PANTHERiPTHR11157. PTHR11157. 1 hit.
PfamiPF01151. ELO. 1 hit.
[Graphical view]
PROSITEiPS01188. ELO. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9EQC4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGLLDSEPGS VLNAMSTAFN DTVEFYRWTW TIADKRVADW PLMQSPWPTI
60 70 80 90 100
SISTLYLLFV WLGPKWMKDR EPFQMRLVLI IYNFGMVLLN LFIFRELFMG
110 120 130 140 150
SYNAGYSYIC QSVDYSNDVN EVRIAGALWW YFVSKGVEYL DTVFFILRKK
160 170 180 190 200
NNQVSFLHVY HHCTMFTLWW IGIKWVAGGQ AFFGAQMNSF IHVIMYSYYG
210 220 230 240 250
LTAFGPWIQK YLWWKRYLTM LQLVQFHVTI GHTALSLYTD CPFPKWMHWA
260 270 280 290 300
LIAYAISFIF LFLNFYTRTY NEPKQSKTGK TATNGISSNG VNKSEKALEN
310
GKPQKNGKPK GE
Length:312
Mass (Da):36,506
Last modified:July 27, 2011 - v2
Checksum:iB049772627D28294
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti126G → A in AAG47667 (PubMed:11138005).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF277093 mRNA. Translation: AAG47667.1.
AJ550628
, AJ550629, AJ550630, AJ550631, AJ550632, AJ550633 Genomic DNA. Translation: CAD80158.4.
AK029065 mRNA. Translation: BAC26274.1.
CH466522 Genomic DNA. Translation: EDL26470.1.
BC037030 mRNA. Translation: AAH37030.1.
CCDSiCCDS23376.1.
RefSeqiNP_683743.2. NM_148941.2.
UniGeneiMm.83949.

Genome annotation databases

EnsembliENSMUST00000034796; ENSMUSP00000034796; ENSMUSG00000032262.
GeneIDi83603.
KEGGimmu:83603.
UCSCiuc012gxk.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF277093 mRNA. Translation: AAG47667.1.
AJ550628
, AJ550629, AJ550630, AJ550631, AJ550632, AJ550633 Genomic DNA. Translation: CAD80158.4.
AK029065 mRNA. Translation: BAC26274.1.
CH466522 Genomic DNA. Translation: EDL26470.1.
BC037030 mRNA. Translation: AAH37030.1.
CCDSiCCDS23376.1.
RefSeqiNP_683743.2. NM_148941.2.
UniGeneiMm.83949.

3D structure databases

ProteinModelPortaliQ9EQC4.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000034796.

Chemistry databases

SwissLipidsiSLP:000000264.

PTM databases

PhosphoSitePlusiQ9EQC4.

Proteomic databases

PaxDbiQ9EQC4.
PRIDEiQ9EQC4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000034796; ENSMUSP00000034796; ENSMUSG00000032262.
GeneIDi83603.
KEGGimmu:83603.
UCSCiuc012gxk.1. mouse.

Organism-specific databases

CTDi6785.
MGIiMGI:1933331. Elovl4.

Phylogenomic databases

eggNOGiKOG3071. Eukaryota.
ENOG410XRWT. LUCA.
GeneTreeiENSGT00760000119122.
HOGENOMiHOG000038120.
HOVERGENiHBG051468.
InParanoidiQ9EQC4.
KOiK10249.
OMAiFYVRTYK.
OrthoDBiEOG091G0N2V.
TreeFamiTF323454.

Enzyme and pathway databases

UniPathwayiUPA00094.
ReactomeiR-MMU-75876. Synthesis of very long-chain fatty acyl-CoAs.

Miscellaneous databases

PROiQ9EQC4.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000032262.
ExpressionAtlasiQ9EQC4. baseline and differential.
GenevisibleiQ9EQC4. MM.

Family and domain databases

HAMAPiMF_03204. VLCF_elongase_4. 1 hit.
InterProiIPR030457. ELO_CS.
IPR002076. ELO_fam.
IPR033678. ELOVL4.
[Graphical view]
PANTHERiPTHR11157. PTHR11157. 1 hit.
PfamiPF01151. ELO. 1 hit.
[Graphical view]
PROSITEiPS01188. ELO. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiELOV4_MOUSE
AccessioniPrimary (citable) accession number: Q9EQC4
Secondary accession number(s): Q8JZV3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 23, 2002
Last sequence update: July 27, 2011
Last modified: November 2, 2016
This is version 105 of the entry and version 2 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.