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Protein

Elongation of very long chain fatty acids protein 7

Gene

ELOVL7

Organism
Homo sapiens (Human)
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 with higher activity toward C18 acyl-CoAs, especially C18:3(n-3) acyl-CoAs and C18:3(n-6)-CoAs. Also active toward C20:4-, C18:0-, C18:1-, C18:2- and C16:0-CoAs, and weakly toward C20:0-CoA. Little or no activity toward C22:0-, C24:0-, or C26:0-CoAs. May participate in the production of saturated and polyunsaturated VLCFAs of different chain lengths that are involved in multiple biological processes as precursors of membrane lipids and lipid mediators.UniRule annotation3 Publications

Catalytic activityi

A very-long-chain acyl-CoA + malonyl-CoA = CoA + a very-long-chain 3-oxoacyl-CoA + CO2.UniRule annotation2 Publications

Kineticsi

  1. KM=2.6 µM for C18:3(n-3)-CoA1 Publication
  2. KM=11.7 µM for malonyl-CoA1 Publication
  1. Vmax=0.33 pmol/min/µg enzyme toward C18:3(n-3)-CoA1 Publication
  2. Vmax=0.31 pmol/min/µg enzyme toward malonyl-CoA1 Publication

Pathwayi: fatty acid biosynthesis

This protein is involved in the pathway fatty acid biosynthesis, which is part of Lipid metabolism.UniRule annotation2 Publications
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-HSA-75876. Synthesis of very long-chain fatty acyl-CoAs.
UniPathwayiUPA00094.

Chemistry databases

SwissLipidsiSLP:000000250.

Names & Taxonomyi

Protein namesi
Recommended name:
Elongation of very long chain fatty acids protein 7UniRule annotationCurated (EC:2.3.1.199UniRule annotation2 Publications)
Alternative name(s):
3-keto acyl-CoA synthase ELOVL7UniRule annotation
ELOVL fatty acid elongase 7UniRule annotation
Short name:
ELOVL FA elongase 7UniRule annotation
Very long chain 3-ketoacyl-CoA synthase 7UniRule annotation
Very long chain 3-oxoacyl-CoA synthase 7UniRule annotation
Gene namesi
Name:ELOVL7UniRule annotation
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 5

Organism-specific databases

HGNCiHGNC:26292. ELOVL7.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transmembranei28 – 48HelicalUniRule annotationAdd BLAST21
Transmembranei73 – 93HelicalUniRule annotationAdd BLAST21
Transmembranei116 – 136HelicalUniRule annotationAdd BLAST21
Transmembranei143 – 162HelicalUniRule annotationAdd BLAST20
Transmembranei172 – 194HelicalUniRule annotationAdd BLAST23
Transmembranei207 – 227HelicalUniRule annotationAdd BLAST21
Transmembranei237 – 257HelicalUniRule annotationAdd BLAST21

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi150H → A: Loss of activity; when associated with A-151. 1 Publication1
Mutagenesisi151H → A: Loss of activity; when associated with A-150. 1 Publication1

Organism-specific databases

DisGeNETi79993.
OpenTargetsiENSG00000164181.
PharmGKBiPA134934034.

Polymorphism and mutation databases

BioMutaiELOVL7.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003119881 – 281Elongation of very long chain fatty acids protein 7Add BLAST281

Proteomic databases

EPDiA1L3X0.
MaxQBiA1L3X0.
PaxDbiA1L3X0.
PRIDEiA1L3X0.

PTM databases

iPTMnetiA1L3X0.
PhosphoSitePlusiA1L3X0.

Expressioni

Tissue specificityi

Expressed in most tissues except heart and skeletal muscle.1 Publication

Gene expression databases

BgeeiENSG00000164181.
CleanExiHS_ELOVL7.
ExpressionAtlasiA1L3X0. baseline and differential.
GenevisibleiA1L3X0. HS.

Organism-specific databases

HPAiHPA036337.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
DTNBP1Q96EV83EBI-10285373,EBI-465804

Protein-protein interaction databases

BioGridi123056. 3 interactors.
IntActiA1L3X0. 1 interactor.
STRINGi9606.ENSP00000402634.

Structurei

3D structure databases

ProteinModelPortaliA1L3X0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi277 – 281Di-lysine motifUniRule annotation5

Domaini

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

Sequence similaritiesi

Belongs to the ELO family. ELOVL7 subfamily.UniRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3071. Eukaryota.
ENOG410XRWT. LUCA.
GeneTreeiENSGT00760000119122.
HOGENOMiHOG000038120.
HOVERGENiHBG051468.
InParanoidiA1L3X0.
KOiK10250.
OMAiSQFFFME.
OrthoDBiEOG091G0N2V.
PhylomeDBiA1L3X0.
TreeFamiTF323454.

Family and domain databases

HAMAPiMF_03207. VLCF_elongase_7. 1 hit.
InterProiIPR030457. ELO_CS.
IPR002076. ELO_fam.
IPR033670. ELOVL7.
[Graphical view]
PANTHERiPTHR11157. PTHR11157. 1 hit.
PfamiPF01151. ELO. 1 hit.
[Graphical view]
PROSITEiPS01188. ELO. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

A1L3X0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAFSDLTSRT VHLYDNWIKD ADPRVEDWLL MSSPLPQTIL LGFYVYFVTS
60 70 80 90 100
LGPKLMENRK PFELKKAMIT YNFFIVLFSV YMCYEFVMSG WGIGYSFRCD
110 120 130 140 150
IVDYSRSPTA LRMARTCWLY YFSKFIELLD TIFFVLRKKN SQVTFLHVFH
160 170 180 190 200
HTIMPWTWWF GVKFAAGGLG TFHALLNTAV HVVMYSYYGL SALGPAYQKY
210 220 230 240 250
LWWKKYLTSL QLVQFVIVAI HISQFFFMED CKYQFPVFAC IIMSYSFMFL
260 270 280
LLFLHFWYRA YTKGQRLPKT VKNGTCKNKD N
Length:281
Mass (Da):33,356
Last modified:February 6, 2007 - v1
Checksum:i33C3DA79704F6E9F
GO

Sequence cautioni

The sequence BAB15697 differs from that shown. Reason: Frameshift at position 138.Curated
The sequence BAB15697 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAB15697 differs from that shown. Reason: Erroneous termination at position 52. Translated as Gly.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti16N → K in BAB15697 (PubMed:14702039).Curated1
Sequence conflicti37Q → H in BAB15697 (PubMed:14702039).Curated1
Sequence conflicti80V → E in BAB15697 (PubMed:14702039).Curated1
Sequence conflicti123S → C in BAB15697 (PubMed:14702039).Curated1
Sequence conflicti250L → P in BAD93238 (Ref. 1) Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB181393 mRNA. Translation: BAD93238.1.
BC130310 mRNA. Translation: AAI30311.1.
BC130312 mRNA. Translation: AAI30313.1.
AK027216 mRNA. Translation: BAB15697.1. Sequence problems.
AL137506 mRNA. Translation: CAB70777.1.
CCDSiCCDS34164.1.
PIRiT46257.
RefSeqiNP_001098028.1. NM_001104558.1.
NP_001284546.1. NM_001297617.1.
NP_001284547.1. NM_001297618.1.
NP_079206.2. NM_024930.2.
XP_005248663.1. XM_005248606.4.
XP_006714758.1. XM_006714695.3.
XP_011541953.1. XM_011543651.2.
XP_016865374.1. XM_017009885.1.
UniGeneiHs.274256.

Genome annotation databases

EnsembliENST00000425382; ENSP00000402634; ENSG00000164181.
ENST00000508821; ENSP00000424123; ENSG00000164181.
GeneIDi79993.
KEGGihsa:79993.
UCSCiuc003jsi.5. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB181393 mRNA. Translation: BAD93238.1.
BC130310 mRNA. Translation: AAI30311.1.
BC130312 mRNA. Translation: AAI30313.1.
AK027216 mRNA. Translation: BAB15697.1. Sequence problems.
AL137506 mRNA. Translation: CAB70777.1.
CCDSiCCDS34164.1.
PIRiT46257.
RefSeqiNP_001098028.1. NM_001104558.1.
NP_001284546.1. NM_001297617.1.
NP_001284547.1. NM_001297618.1.
NP_079206.2. NM_024930.2.
XP_005248663.1. XM_005248606.4.
XP_006714758.1. XM_006714695.3.
XP_011541953.1. XM_011543651.2.
XP_016865374.1. XM_017009885.1.
UniGeneiHs.274256.

3D structure databases

ProteinModelPortaliA1L3X0.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi123056. 3 interactors.
IntActiA1L3X0. 1 interactor.
STRINGi9606.ENSP00000402634.

Chemistry databases

SwissLipidsiSLP:000000250.

PTM databases

iPTMnetiA1L3X0.
PhosphoSitePlusiA1L3X0.

Polymorphism and mutation databases

BioMutaiELOVL7.

Proteomic databases

EPDiA1L3X0.
MaxQBiA1L3X0.
PaxDbiA1L3X0.
PRIDEiA1L3X0.

Protocols and materials databases

DNASUi79993.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000425382; ENSP00000402634; ENSG00000164181.
ENST00000508821; ENSP00000424123; ENSG00000164181.
GeneIDi79993.
KEGGihsa:79993.
UCSCiuc003jsi.5. human.

Organism-specific databases

CTDi79993.
DisGeNETi79993.
GeneCardsiELOVL7.
H-InvDBHIX0004886.
HGNCiHGNC:26292. ELOVL7.
HPAiHPA036337.
MIMi614451. gene.
neXtProtiNX_A1L3X0.
OpenTargetsiENSG00000164181.
PharmGKBiPA134934034.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3071. Eukaryota.
ENOG410XRWT. LUCA.
GeneTreeiENSGT00760000119122.
HOGENOMiHOG000038120.
HOVERGENiHBG051468.
InParanoidiA1L3X0.
KOiK10250.
OMAiSQFFFME.
OrthoDBiEOG091G0N2V.
PhylomeDBiA1L3X0.
TreeFamiTF323454.

Enzyme and pathway databases

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

Miscellaneous databases

ChiTaRSiELOVL7. human.
GenomeRNAii79993.
PROiA1L3X0.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000164181.
CleanExiHS_ELOVL7.
ExpressionAtlasiA1L3X0. baseline and differential.
GenevisibleiA1L3X0. HS.

Family and domain databases

HAMAPiMF_03207. VLCF_elongase_7. 1 hit.
InterProiIPR030457. ELO_CS.
IPR002076. ELO_fam.
IPR033670. ELOVL7.
[Graphical view]
PANTHERiPTHR11157. PTHR11157. 1 hit.
PfamiPF01151. ELO. 1 hit.
[Graphical view]
PROSITEiPS01188. ELO. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiELOV7_HUMAN
AccessioniPrimary (citable) accession number: A1L3X0
Secondary accession number(s): Q589T3, Q9H5D0, Q9NT66
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 4, 2007
Last sequence update: February 6, 2007
Last modified: November 2, 2016
This is version 89 of the entry and version 1 of the sequence. [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

Documents

  1. Human chromosome 5
    Human chromosome 5: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. 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.