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Protein

Elongation of very long chain fatty acids protein 7

Gene

Elovl7

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Protein inferred from homologyi

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 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

UniPathwayiUPA00094.

Names & Taxonomyi

Protein namesi
Recommended name:
Elongation of very long chain fatty acids protein 7UniRule annotationCurated (EC:2.3.1.199UniRule annotationBy similarity)
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
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi1310560. Elovl7.

Subcellular locationi

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

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transmembranei28 – 48HelicalUniRule annotationAdd BLAST21
Transmembranei73 – 93HelicalUniRule annotationAdd BLAST21
Transmembranei116 – 136HelicalUniRule annotationAdd BLAST21
Transmembranei143 – 162HelicalUniRule annotationAdd BLAST20
Transmembranei177 – 197HelicalUniRule annotationAdd BLAST21
Transmembranei207 – 227HelicalUniRule annotationAdd BLAST21
Transmembranei237 – 257HelicalUniRule annotationAdd BLAST21

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004166921 – 281Elongation of very long chain fatty acids protein 7Add BLAST281

Proteomic databases

PaxDbiD4ADY9.
PRIDEiD4ADY9.

Interactioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000014074.

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.
InParanoidiD4ADY9.
KOiK10250.
PhylomeDBiD4ADY9.
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.

D4ADY9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAFSDLTSRT VRFYDNWIKD ADPRVENWLL MSSPLPQTII LGLYVYFVTS
60 70 80 90 100
LGPKLMENRK PFELKKAMIT YNFFIVLFSV YMCYEFVMSG WGTGYSFRCD
110 120 130 140 150
IVDYSQSPRA MRMVHTCWLY YFSKFIELFD TIFFVLRKKN SQVTFLHVFH
160 170 180 190 200
HTIMPWTWWF GVKFAAGGLG TFHALLNTAV HVVMYFYYGL CAMGPAYQKY
210 220 230 240 250
LWWKKHLTSL QLVQFVLVTV HIGQIFFMED CNYQYPVFLY IIMSYGCIFL
260 270 280
LLFLHFWYRA YTKGQRLPKT MENGNCKSKH H
Length:281
Mass (Da):33,547
Last modified:April 20, 2010 - v1
Checksum:iA9314D85BF04B80C
GO

Sequence databases

RefSeqiNP_001178773.1. NM_001191844.1.
UniGeneiRn.105650.

Genome annotation databases

GeneIDi361895.
KEGGirno:361895.

Cross-referencesi

Sequence databases

RefSeqiNP_001178773.1. NM_001191844.1.
UniGeneiRn.105650.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000014074.

Proteomic databases

PaxDbiD4ADY9.
PRIDEiD4ADY9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi361895.
KEGGirno:361895.

Organism-specific databases

CTDi79993.
RGDi1310560. Elovl7.

Phylogenomic databases

eggNOGiKOG3071. Eukaryota.
ENOG410XRWT. LUCA.
InParanoidiD4ADY9.
KOiK10250.
PhylomeDBiD4ADY9.
TreeFamiTF323454.

Enzyme and pathway databases

UniPathwayiUPA00094.

Miscellaneous databases

PROiD4ADY9.

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_RAT
AccessioniPrimary (citable) accession number: D4ADY9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 18, 2012
Last sequence update: April 20, 2010
Last modified: November 2, 2016
This is version 47 of the entry and version 1 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. 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.