G8IIS1 · G8IIS1_SOLSE

Function

function

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 acts specifically toward polyunsaturated acyl-CoA with the higher activity toward C18:3(n-6) acyl-CoA. May participate to the production of monounsaturated and of polyunsaturated VLCFAs of different chain lengths that are involved in multiple biological processes as precursors of membrane lipids and lipid mediators.

Caution

Lacks conserved residue(s) required for the propagation of feature annotation.

Catalytic activity

  • (11Z)-octadecenoyl-CoA + H+ + malonyl-CoA = 3-oxo-(13Z)-eicosenoyl-CoA + CO2 + CoA
    This reaction proceeds in the forward direction.
  • (5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + H+ + malonyl-CoA = (7Z,10Z,13Z,16Z)-3-oxodocosatetraenoyl-CoA + CO2 + CoA
    This reaction proceeds in the forward direction.
  • (6Z,9Z,12Z)-octadecatrienoyl-CoA + H+ + malonyl-CoA = (8Z,11Z,14Z)-3-oxoeicosatrienoyl-CoA + CO2 + CoA
    This reaction proceeds in the forward direction.
  • (6Z,9Z,12Z,15Z)-octadecatetraenoyl-CoA + H+ + malonyl-CoA = (8Z,11Z,14Z,17Z)-3-oxoicosatetraenoyl-CoA + CO2 + CoA
    This reaction proceeds in the forward direction.
  • (9Z)-hexadecenoyl-CoA + H+ + malonyl-CoA = 3-oxo-(11Z)-octadecenoyl-CoA + CO2 + CoA
    This reaction proceeds in the forward direction.
  • (9Z)-octadecenoyl-CoA + H+ + malonyl-CoA = (11Z)-3-oxoicosenoyl-CoA + CO2 + CoA
    This reaction proceeds in the forward direction.
  • (9Z,12Z)-octadecadienoyl-CoA + H+ + malonyl-CoA = (11Z,14Z)-3-oxoicosa-11,14-dienoyl-CoA + CO2 + CoA
    This reaction proceeds in the forward direction.
  • (9Z,12Z,15Z)-octadecatrienoyl-CoA + H+ + malonyl-CoA = (11Z,14Z,17Z)-3-oxoeicosatrienoyl-CoA + CO2 + CoA
    This reaction proceeds in the forward direction.
  • a very-long-chain acyl-CoA + H+ + malonyl-CoA = a very-long-chain 3-oxoacyl-CoA + CO2 + CoA
    EC:2.3.1.199 (UniProtKB | ENZYME | Rhea)

Pathway

Lipid metabolism; polyunsaturated fatty acid biosynthesis.

GO annotations

AspectTerm
Cellular Componentdendrite
Cellular Componentendoplasmic reticulum membrane
Molecular Functionfatty acid elongase activity
Biological Processfatty acid elongation, monounsaturated fatty acid
Biological Processfatty acid elongation, polyunsaturated fatty acid
Biological Processfatty acid elongation, saturated fatty acid
Biological Processlong-chain fatty-acyl-CoA biosynthetic process
Biological Processunsaturated fatty acid biosynthetic process
Biological Processvery long-chain fatty acid biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Elongation of very long chain fatty acids protein 5
  • EC number
  • Alternative names
    • 3-keto acyl-CoA synthase ELOVL5
    • ELOVL fatty acid elongase 5
      (ELOVL FA elongase 5
      )
    • Very long chain 3-ketoacyl-CoA synthase 5
    • Very long chain 3-oxoacyl-CoA synthase 5

Gene names

    • Name
      ELOVL5

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Actinopterygii > Neopterygii > Teleostei > Neoteleostei > Acanthomorphata > Carangaria > Pleuronectiformes > Pleuronectoidei > Soleidae > Solea

Accessions

  • Primary accession
    G8IIS1

Subcellular Location

Endoplasmic reticulum membrane
; Multi-pass membrane protein
Cell projection, dendrite
Membrane
; Multi-pass membrane protein
Note: In Purkinje cells, the protein localizes to the soma and proximal portion of the dendritic tree.

Features

Showing features for transmembrane.

TypeIDPosition(s)Description
Transmembrane32-49Helical
Transmembrane61-81Helical
Transmembrane114-132Helical
Transmembrane144-161Helical
Transmembrane207-225Helical
Transmembrane231-251Helical

Keywords

Family & Domains

Features

Showing features for compositional bias, region.

TypeIDPosition(s)Description
Compositional bias259-276Polar residues
Region259-288Disordered

Sequence similarities

Belongs to the ELO family. ELOVL5 subfamily.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    288
  • Mass (Da)
    34,460
  • Last updated
    2012-01-25 v1
  • Checksum
    68B87096516E87AA
METFNHKLNTHIDSWLGPRDQRVRGWLLLDDYPPTFALTVMYLLIVWMGPKYMQHRQPYSCRGLLVLYNLGLTLLSFYMFYELVSAVWHGGYNFYCQDIHSAPEVDKKVIKVLWWYYFSKVIEFMDTFFFILRKNNHQITFLHIYHHASMLNIWWFVMNWIPCGHSYFGASINSFVHVVMYSYYGLSAIPAVRPYLWWKRYITQLQLIQFFLTVFHTMSAVIWPCGFPMRWLYFQISYMVTLIILFANFYIQTYKKRSGSQQKGSPAHGHTNGTPSMEHSAHKKLRVD

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias259-276Polar residues

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JN793448
EMBL· GenBank· DDBJ
AER58183.1
EMBL· GenBank· DDBJ
mRNA

Similar Proteins

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