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Protein

Elongation of very long chain fatty acids protein 3

Gene

ELOVL3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -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 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.UniRule annotation1 Publication

Catalytic activityi

A very-long-chain acyl-CoA + malonyl-CoA = CoA + a very-long-chain 3-oxoacyl-CoA + CO2.UniRule annotation1 Publication

Pathwayi: polyunsaturated fatty acid biosynthesis

This protein is involved in the pathway polyunsaturated fatty acid biosynthesis, which is part of Lipid metabolism.UniRule annotation1 Publication
View 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

GO - Biological processi

Keywordsi

Molecular functionTransferase
Biological processFatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism

Enzyme and pathway databases

BioCyciMetaCyc:ENSG00000119915-MONOMER
BRENDAi2.3.1.119 2681
ReactomeiR-HSA-2046105 Linoleic acid (LA) metabolism
R-HSA-2046106 alpha-linolenic acid (ALA) metabolism
R-HSA-75876 Synthesis of very long-chain fatty acyl-CoAs
UniPathwayiUPA00658

Chemistry databases

SwissLipidsiSLP:000000248

Names & Taxonomyi

Protein namesi
Recommended name:
Elongation of very long chain fatty acids protein 3UniRule annotationCurated (EC:2.3.1.199UniRule annotation1 Publication)
Alternative name(s):
3-keto acyl-CoA synthase ELOVL3UniRule annotation
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
Name:ELOVL3UniRule annotation
Synonyms:CIG30
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 10

Organism-specific databases

EuPathDBiHostDB:ENSG00000119915.4
HGNCiHGNC:18047 ELOVL3
MIMi611815 gene
neXtProtiNX_Q9HB03

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transmembranei29 – 49HelicalUniRule annotationAdd BLAST21
Transmembranei63 – 83HelicalUniRule annotationAdd BLAST21
Transmembranei115 – 135HelicalUniRule annotationAdd BLAST21
Transmembranei140 – 160HelicalUniRule annotationAdd BLAST21
Transmembranei164 – 184HelicalUniRule annotationAdd BLAST21
Transmembranei198 – 218HelicalUniRule annotationAdd BLAST21
Transmembranei235 – 255HelicalUniRule annotationAdd BLAST21

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Organism-specific databases

DisGeNETi83401
OpenTargetsiENSG00000119915
PharmGKBiPA27762

Chemistry databases

ChEMBLiCHEMBL5791

Polymorphism and mutation databases

BioMutaiELOVL3
DMDMi26006738

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002075401 – 270Elongation of very long chain fatty acids protein 3Add BLAST270

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi6N-linked (GlcNAc...) asparagineUniRule annotation1
Glycosylationi110N-linked (GlcNAc...) asparagineUniRule annotation1

Post-translational modificationi

N-Glycosylated.UniRule annotation1 Publication

Keywords - PTMi

Glycoprotein

Proteomic databases

PaxDbiQ9HB03
PRIDEiQ9HB03

PTM databases

iPTMnetiQ9HB03
PhosphoSitePlusiQ9HB03

Expressioni

Tissue specificityi

Testis.1 Publication

Gene expression databases

BgeeiENSG00000119915
CleanExiHS_ELOVL3
GenevisibleiQ9HB03 HS

Organism-specific databases

HPAiHPA036236

Interactioni

Protein-protein interaction databases

BioGridi123637, 2 interactors
IntActiQ9HB03, 1 interactor
STRINGi9606.ENSP00000359022

Chemistry databases

BindingDBiQ9HB03

Structurei

3D structure databases

ProteinModelPortaliQ9HB03
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi266 – 270Di-lysine motifUniRule annotation5

Domaini

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

Sequence similaritiesi

Belongs to the ELO family. ELOVL3 subfamily.UniRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3072 Eukaryota
ENOG410Z3FZ LUCA
GeneTreeiENSGT00760000119122
HOGENOMiHOG000038943
HOVERGENiHBG099423
InParanoidiQ9HB03
KOiK10248
OMAiFGYKNKV
OrthoDBiEOG091G0EKU
PhylomeDBiQ9HB03
TreeFamiTF106467

Family and domain databases

HAMAPiMF_03203 VLCF_elongase_3, 1 hit
InterProiView protein in InterPro
IPR030457 ELO_CS
IPR002076 ELO_fam
IPR033679 ELOVL3
PANTHERiPTHR11157 PTHR11157, 1 hit
PTHR11157:SF68 PTHR11157:SF68, 1 hit
PfamiView protein in Pfam
PF01151 ELO, 1 hit
PROSITEiView protein in PROSITE
PS01188 ELO, 1 hit

Sequencei

Sequence statusi: Complete.

Q9HB03-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVTAMNVSHE VNQLFQPYNF ELSKDMRPFF EEYWATSFPI ALIYLVLIAV
60 70 80 90 100
GQNYMKERKG FNLQGPLILW SFCLAIFSIL GAVRMWGIMG TVLLTGGLKQ
110 120 130 140 150
TVCFINFIDN STVKFWSWVF LLSKVIELGD TAFIILRKRP LIFIHWYHHS
160 170 180 190 200
TVLVYTSFGY KNKVPAGGWF VTMNFGVHAI MYTYYTLKAA NVKPPKMLPM
210 220 230 240 250
LITSLQILQM FVGAIVSILT YIWRQDQGCH TTMEHLFWSF ILYMTYFILF
260 270
AHFFCQTYIR PKVKAKTKSQ
Length:270
Mass (Da):31,500
Last modified:November 28, 2002 - v2
Checksum:i0C6C8F1E7B5DE8B1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL160011 Genomic DNA No translation available.
CH471066 Genomic DNA Translation: EAW49711.1
BC034344 mRNA Translation: AAH34344.1
AF292387 Genomic DNA Translation: AAG17875.1
CCDSiCCDS7531.1
RefSeqiNP_689523.1, NM_152310.2
XP_011538547.1, XM_011540245.2
UniGeneiHs.302130

Genome annotation databases

EnsembliENST00000370005; ENSP00000359022; ENSG00000119915
GeneIDi83401
KEGGihsa:83401
UCSCiuc001kut.5 human

Similar proteinsi

Entry informationi

Entry nameiELOV3_HUMAN
AccessioniPrimary (citable) accession number: Q9HB03
Secondary accession number(s): Q5VZL3, Q8N180
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 23, 2002
Last sequence update: November 28, 2002
Last modified: March 28, 2018
This is version 131 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome
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Main funding by: National Institutes of Health