UniProtKB - Q9NXB9 (ELOV2_HUMAN)
Protein
Elongation of very long chain fatty acids protein 2
Gene
ELOVL2
Organism
Homo sapiens (Human)
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 polyunsaturated very long chain fatty acid (C20- and C22-PUFA), acting specifically toward polyunsaturated acyl-CoA with the higher activity toward C20:4(n-6) acyl-CoA. May participate in the production of polyunsaturated VLCFAs of different chain lengths that are involved in multiple biological processes as precursors of membrane lipids and lipid mediators.UniRule annotation4 Publications
Catalytic activityi
- a very-long-chain acyl-CoA + H+ + malonyl-CoA = a very-long-chain 3-oxoacyl-CoA + CO2 + CoAUniRule annotation4 PublicationsEC:2.3.1.199UniRule annotation4 PublicationsThis reaction proceeds in the forward1 Publication direction.
- (5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + H+ + malonyl-CoA = (7Z,10Z,13Z,16Z)-3-oxodocosatetraenoyl-CoA + CO2 + CoA4 PublicationsThis reaction proceeds in the forward1 Publication direction.
- (7Z,10Z,13Z,16Z)-docosatetraenoyl-CoA + H+ + malonyl-CoA = (9Z,12Z,15Z,18Z)-3-oxotetracosatetraenoyl-CoA + CO2 + CoA2 PublicationsThis reaction proceeds in the forward1 Publication direction.
- (5Z,8Z,11Z,14Z,17Z)-eicosapentaenoyl-CoA + H+ + malonyl-CoA = (7Z,10Z,13Z,16Z,19Z)-3-oxodocosapentaenoyl-CoA + CO2 + CoA2 PublicationsThis reaction proceeds in the forward1 Publication direction.
- (7Z,10Z,13Z,16Z,19Z)-docosapentaenoyl-CoA + H+ + malonyl-CoA = (9Z,12Z,15Z,18Z,21Z)-3-oxotetracosapentaenoyl-CoA + CO2 + CoA2 PublicationsThis reaction proceeds in the forward1 Publication direction.
: polyunsaturated fatty acid biosynthesis Pathwayi
This protein is involved in the pathway polyunsaturated fatty acid biosynthesis, which is part of Lipid metabolism.UniRule annotation4 PublicationsView 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: UniProtKB
- very-long-chain 3-ketoacyl-CoA synthase activity Source: UniProtKB-EC
GO - Biological processi
- alpha-linolenic acid metabolic process Source: Reactome
- fatty acid elongation, monounsaturated fatty acid Source: GO_Central
- fatty acid elongation, polyunsaturated fatty acid Source: UniProtKB
- fatty acid elongation, saturated fatty acid Source: GO_Central
- linoleic acid metabolic process Source: Reactome
- long-chain fatty-acyl-CoA biosynthetic process Source: Reactome
- sphingolipid biosynthetic process Source: GO_Central
- unsaturated fatty acid biosynthetic process Source: UniProtKB-UniPathway
- 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
BioCyci | MetaCyc:ENSG00000096256-MONOMER |
BRENDAi | 2.3.1.119, 2681 |
PathwayCommonsi | Q9NXB9 |
Reactomei | R-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 |
UniPathwayi | UPA00658 |
Chemistry databases
SwissLipidsi | SLP:000000245 |
Names & Taxonomyi
Protein namesi | Recommended name: Elongation of very long chain fatty acids protein 2UniRule annotationCurated (EC:2.3.1.199UniRule annotation4 Publications)Alternative name(s): 3-keto acyl-CoA synthase ELOVL2UniRule annotation ELOVL fatty acid elongase 2UniRule annotation Short name: ELOVL FA elongase 2UniRule annotation Very long chain 3-ketoacyl-CoA synthase 2UniRule annotation Very long chain 3-oxoacyl-CoA synthase 2UniRule annotation |
Gene namesi | |
Organismi | Homo sapiens (Human) |
Taxonomic identifieri | 9606 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Proteomesi |
|
Organism-specific databases
EuPathDBi | HostDB:ENSG00000197977.3 |
HGNCi | HGNC:14416, ELOVL2 |
MIMi | 611814, gene |
neXtProti | NX_Q9NXB9 |
Subcellular locationi
Endoplasmic reticulum
- Endoplasmic reticulum membrane UniRule annotation1 Publication; Multi-pass membrane protein UniRule annotation
Endoplasmic reticulum
- endoplasmic reticulum Source: UniProtKB
- endoplasmic reticulum membrane Source: Reactome
- integral component of endoplasmic reticulum membrane Source: GO_Central
Topology
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Transmembranei | 29 – 49 | HelicalUniRule annotationAdd BLAST | 21 | |
Transmembranei | 67 – 87 | HelicalUniRule annotationAdd BLAST | 21 | |
Transmembranei | 115 – 135 | HelicalUniRule annotationAdd BLAST | 21 | |
Transmembranei | 153 – 173 | HelicalUniRule annotationAdd BLAST | 21 | |
Transmembranei | 175 – 195 | HelicalUniRule annotationAdd BLAST | 21 | |
Transmembranei | 208 – 225 | HelicalUniRule annotationAdd BLAST | 18 | |
Transmembranei | 230 – 250 | HelicalUniRule annotationAdd BLAST | 21 |
Keywords - Cellular componenti
Endoplasmic reticulum, MembranePathology & Biotechi
Organism-specific databases
DisGeNETi | 54898 |
OpenTargetsi | ENSG00000197977 |
PharmGKBi | PA27761 |
Miscellaneous databases
Pharosi | Q9NXB9, Tbio |
Chemistry databases
ChEMBLi | CHEMBL5911 |
DrugBanki | DB00132, alpha-Linolenic acid |
Polymorphism and mutation databases
BioMutai | ELOVL2 |
DMDMi | 187472388 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000207538 | 1 – 296 | Elongation of very long chain fatty acids protein 2Add BLAST | 296 |
Proteomic databases
MassIVEi | Q9NXB9 |
MaxQBi | Q9NXB9 |
PaxDbi | Q9NXB9 |
PeptideAtlasi | Q9NXB9 |
PRIDEi | Q9NXB9 |
ProteomicsDBi | 83070 |
PTM databases
iPTMneti | Q9NXB9 |
PhosphoSitePlusi | Q9NXB9 |
SwissPalmi | Q9NXB9 |
Expressioni
Tissue specificityi
Liver and testis.1 Publication
Gene expression databases
Bgeei | ENSG00000197977, Expressed in ventricular zone and 172 other tissues |
ExpressionAtlasi | Q9NXB9, baseline and differential |
Genevisiblei | Q9NXB9, HS |
Organism-specific databases
HPAi | ENSG00000197977, Tissue enhanced (brain, liver, parathyroid gland, placenta) |
Interactioni
Binary interactionsi
Hide detailsQ9NXB9
With | #Exp. | IntAct |
---|---|---|
FXYD6 [Q9H0Q3] | 3 | EBI-17206972,EBI-713304 |
IFITM3 [Q01628] | 3 | EBI-17206972,EBI-7932862 |
MALL [Q13021] | 3 | EBI-17206972,EBI-750078 |
TMEM218 [A2RU14] | 3 | EBI-17206972,EBI-10173151 |
Protein-protein interaction databases
BioGRIDi | 120244, 13 interactors |
IntActi | Q9NXB9, 12 interactors |
STRINGi | 9606.ENSP00000346693 |
Chemistry databases
BindingDBi | Q9NXB9 |
Miscellaneous databases
RNActi | Q9NXB9, protein |
Family & Domainsi
Motif
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Motifi | 293 – 296 | Di-lysine motifUniRule annotation | 4 |
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 | ENSGT01000000214427 |
HOGENOMi | CLU_048483_0_1_1 |
InParanoidi | Q9NXB9 |
OMAi | ATWEGGY |
OrthoDBi | 1094172at2759 |
PhylomeDBi | Q9NXB9 |
TreeFami | TF323454 |
Family and domain databases
HAMAPi | MF_03202, VLCF_elongase_2, 1 hit |
InterProi | View protein in InterPro IPR030457, ELO_CS IPR002076, ELO_fam IPR033680, ELOVL2 |
PANTHERi | PTHR11157, PTHR11157, 1 hit PTHR11157:SF16, PTHR11157:SF16, 1 hit |
Pfami | View protein in Pfam PF01151, ELO, 1 hit |
PROSITEi | View protein in PROSITE PS01188, ELO, 1 hit |
i Sequence
Sequence statusi: Complete.
Q9NXB9-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MEHLKAFDDE INAFLDNMFG PRDSRVRGWF MLDSYLPTFF LTVMYLLSIW
60 70 80 90 100
LGNKYMKNRP ALSLRGILTL YNLGITLLSA YMLAELILST WEGGYNLQCQ
110 120 130 140 150
DLTSAGEADI RVAKVLWWYY FSKSVEFLDT IFFVLRKKTS QITFLHVYHH
160 170 180 190 200
ASMFNIWWCV LNWIPCGQSF FGPTLNSFIH ILMYSYYGLS VFPSMHKYLW
210 220 230 240 250
WKKYLTQAQL VQFVLTITHT MSAVVKPCGF PFGCLIFQSS YMLTLVILFL
260 270 280 290
NFYVQTYRKK PMKKDMQEPP AGKEVKNGFS KAYFTAANGV MNKKAQ
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 31 | M → T in BAA91096 (PubMed:14702039).Curated | 1 | |
Sequence conflicti | 179 | I → V in BAA91096 (PubMed:14702039).Curated | 1 |
Natural variant
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural variantiVAR_039039 | 216 | T → A1 PublicationCorresponds to variant dbSNP:rs17855038Ensembl. | 1 | |
Natural variantiVAR_039040 | 225 | V → M. Corresponds to variant dbSNP:rs6919726Ensembl. | 1 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AK000341 mRNA Translation: BAA91096.1 AL121955 Genomic DNA No translation available. CH471087 Genomic DNA Translation: EAW55291.1 BC050278 mRNA Translation: AAH50278.2 BC060809 mRNA Translation: AAH60809.1 |
CCDSi | CCDS4518.1 |
RefSeqi | NP_060240.3, NM_017770.3 |
Genome annotation databases
Ensembli | ENST00000354666; ENSP00000346693; ENSG00000197977 |
GeneIDi | 54898 |
KEGGi | hsa:54898 |
UCSCi | uc003mzp.5, human |
Keywords - Coding sequence diversityi
PolymorphismSimilar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AK000341 mRNA Translation: BAA91096.1 AL121955 Genomic DNA No translation available. CH471087 Genomic DNA Translation: EAW55291.1 BC050278 mRNA Translation: AAH50278.2 BC060809 mRNA Translation: AAH60809.1 |
CCDSi | CCDS4518.1 |
RefSeqi | NP_060240.3, NM_017770.3 |
3D structure databases
ModBasei | Search... |
SWISS-MODEL-Workspacei | Submit a new modelling project... |
Protein-protein interaction databases
BioGRIDi | 120244, 13 interactors |
IntActi | Q9NXB9, 12 interactors |
STRINGi | 9606.ENSP00000346693 |
Chemistry databases
BindingDBi | Q9NXB9 |
ChEMBLi | CHEMBL5911 |
DrugBanki | DB00132, alpha-Linolenic acid |
SwissLipidsi | SLP:000000245 |
PTM databases
iPTMneti | Q9NXB9 |
PhosphoSitePlusi | Q9NXB9 |
SwissPalmi | Q9NXB9 |
Polymorphism and mutation databases
BioMutai | ELOVL2 |
DMDMi | 187472388 |
Proteomic databases
MassIVEi | Q9NXB9 |
MaxQBi | Q9NXB9 |
PaxDbi | Q9NXB9 |
PeptideAtlasi | Q9NXB9 |
PRIDEi | Q9NXB9 |
ProteomicsDBi | 83070 |
Protocols and materials databases
Antibodypediai | 44274, 159 antibodies |
DNASUi | 54898 |
Genome annotation databases
Ensembli | ENST00000354666; ENSP00000346693; ENSG00000197977 |
GeneIDi | 54898 |
KEGGi | hsa:54898 |
UCSCi | uc003mzp.5, human |
Organism-specific databases
CTDi | 54898 |
DisGeNETi | 54898 |
EuPathDBi | HostDB:ENSG00000197977.3 |
GeneCardsi | ELOVL2 |
HGNCi | HGNC:14416, ELOVL2 |
HPAi | ENSG00000197977, Tissue enhanced (brain, liver, parathyroid gland, placenta) |
MIMi | 611814, gene |
neXtProti | NX_Q9NXB9 |
OpenTargetsi | ENSG00000197977 |
PharmGKBi | PA27761 |
GenAtlasi | Search... |
Phylogenomic databases
eggNOGi | KOG3071, Eukaryota |
GeneTreei | ENSGT01000000214427 |
HOGENOMi | CLU_048483_0_1_1 |
InParanoidi | Q9NXB9 |
OMAi | ATWEGGY |
OrthoDBi | 1094172at2759 |
PhylomeDBi | Q9NXB9 |
TreeFami | TF323454 |
Enzyme and pathway databases
UniPathwayi | UPA00658 |
BioCyci | MetaCyc:ENSG00000096256-MONOMER |
BRENDAi | 2.3.1.119, 2681 |
PathwayCommonsi | Q9NXB9 |
Reactomei | R-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 |
Miscellaneous databases
BioGRID-ORCSi | 54898, 3 hits in 845 CRISPR screens |
ChiTaRSi | ELOVL2, human |
GenomeRNAii | 54898 |
Pharosi | Q9NXB9, Tbio |
PROi | PR:Q9NXB9 |
RNActi | Q9NXB9, protein |
SOURCEi | Search... |
Gene expression databases
Bgeei | ENSG00000197977, Expressed in ventricular zone and 172 other tissues |
ExpressionAtlasi | Q9NXB9, baseline and differential |
Genevisiblei | Q9NXB9, HS |
Family and domain databases
HAMAPi | MF_03202, VLCF_elongase_2, 1 hit |
InterProi | View protein in InterPro IPR030457, ELO_CS IPR002076, ELO_fam IPR033680, ELOVL2 |
PANTHERi | PTHR11157, PTHR11157, 1 hit PTHR11157:SF16, PTHR11157:SF16, 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 | ELOV2_HUMAN | |
Accessioni | Q9NXB9Primary (citable) accession number: Q9NXB9 Secondary accession number(s): Q6P9E1, Q86W94 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | January 23, 2002 |
Last sequence update: | February 26, 2008 | |
Last modified: | December 2, 2020 | |
This is version 148 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program | |
Disclaimer | Any 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
Reference proteomeDocuments
- Human chromosome 6
Human chromosome 6: entries, gene names and cross-references to MIM - Human polymorphisms and disease mutations
Index of human polymorphisms and disease mutations - MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot - PATHWAY comments
Index of metabolic and biosynthesis pathways - SIMILARITY comments
Index of protein domains and families - Human entries with polymorphisms or disease mutations
List of human entries with polymorphisms or disease mutations