A0AAD6BPB3 · A0AAD6BPB3_9TELE

  • Protein
    Elongation of very long chain fatty acids protein 5
  • Gene
    ELOVL5
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    5/5

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 in 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. In conditions where the essential linoleic and alpha linoleic fatty acids are lacking it is also involved in the synthesis of Mead acid from oleic acid.
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.
The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

Catalytic activity

  • (11Z)-octadecenoyl-CoA + malonyl-CoA + H+ = 3-oxo-(13Z)-eicosenoyl-CoA + CO2 + CoA
    This reaction proceeds in the forward direction.
  • (5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + malonyl-CoA + H+ = (7Z,10Z,13Z,16Z)-3-oxodocosatetraenoyl-CoA + CO2 + CoA
    This reaction proceeds in the forward direction.
  • (6Z,9Z,12Z)-octadecatrienoyl-CoA + malonyl-CoA + H+ = (8Z,11Z,14Z)-3-oxoeicosatrienoyl-CoA + CO2 + CoA
    This reaction proceeds in the forward direction.
  • (6Z,9Z,12Z,15Z)-octadecatetraenoyl-CoA + malonyl-CoA + H+ = (8Z,11Z,14Z,17Z)-3-oxoicosatetraenoyl-CoA + CO2 + CoA
    This reaction proceeds in the forward direction.
  • (9Z)-hexadecenoyl-CoA + malonyl-CoA + H+ = 3-oxo-(11Z)-octadecenoyl-CoA + CO2 + CoA
    This reaction proceeds in the forward direction.
  • (9Z)-octadecenoyl-CoA + malonyl-CoA + H+ = (11Z)-3-oxoicosenoyl-CoA + CO2 + CoA
    This reaction proceeds in the forward direction.
  • (9Z,12Z)-octadecadienoyl-CoA + malonyl-CoA + H+ = (11Z,14Z)-3-oxoicosa-11,14-dienoyl-CoA + CO2 + CoA
    This reaction proceeds in the forward direction.
  • (9Z,12Z,15Z)-octadecatrienoyl-CoA + malonyl-CoA + H+ = (11Z,14Z,17Z)-3-oxoeicosatrienoyl-CoA + CO2 + CoA
    This reaction proceeds in the forward direction.
  • a very-long-chain acyl-CoA + malonyl-CoA + H+ = 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 Processsphingolipid 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
    • ORF names
      JOQ06_020114

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • SGF0006
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Actinopterygii > Neopterygii > Teleostei > Neoteleostei > Acanthomorphata > Eupercaria > Perciformes > Notothenioidei > Pogonophryne

Accessions

  • Primary accession
    A0AAD6BPB3

Proteomes

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
Transmembrane32-50Helical
Transmembrane62-81Helical
Transmembrane114-132Helical
Transmembrane144-161Helical
Transmembrane207-224Helical
Transmembrane230-251Helical

Keywords

Family & Domains

Features

Showing features for compositional bias, region.

Type
IDPosition(s)Description
Compositional bias265-286Polar residues
Region265-294Disordered

Sequence similarities

Belongs to the ELO family. ELOVL5 subfamily.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    294
  • Mass (Da)
    35,018
  • Last updated
    2024-05-29 v1
  • Checksum
    479E4DDE6CD66E35
METFNHKLNTYLESWMGPRDQRVQGWLLLDNYPPTFAFTVMYLLIVWMGPKYMKHRQPYSSRGLLVLYNLGLTLLSFYMLYELVTAVWHGGYNFYCQDTHSAQEVDNKIIKVLWWYYFSKLIEFMDTFFFILRKNNHQITFLHIYHHASMLNIWWFVMNWVPCGHSYFGASLNSFVHVGMYSYYGLSAIPAMRPYLWWKKYITKLQLIQFFLTMSQTMCAVIWPCGFPKGWLYFQISYMVVLIVLFSNFYIQTYKKHSGSLKKEHQNGSLLSTNGHVNGTPSTKSTEHNKLRVD

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias265-286Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JAPTMU010000001
EMBL· GenBank· DDBJ
KAJ4948581.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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