A0A6J2R8C5 · A0A6J2R8C5_COTGO

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.

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 acid biosynthetic process
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
    • Synonyms
      ELOVL5

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Actinopterygii > Neopterygii > Teleostei > Neoteleostei > Acanthomorphata > Eupercaria > Perciformes > Notothenioidei > Bovichtidae > Cottoperca

Accessions

  • Primary accession
    A0A6J2R8C5

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 region, compositional bias.

Type
IDPosition(s)Description
Region261-294Disordered
Compositional bias267-283Polar residues
Compositional bias284-294Basic and acidic residues

Sequence similarities

Belongs to the ELO family. ELOVL5 subfamily.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    294
  • Mass (Da)
    35,180
  • Last updated
    2020-10-07 v1
  • MD5 Checksum
    8567691B8304221EEEC79AD37F1FF838
METFNHKLNTFLESWMGPRDQRVRGWLLLDNYPPTFALTVMYLLIVWMGPKYMKHRQPYSSRGLLVLYNLGLTLLSFYMFYELVTAVWHGGYNFYCQDTHSAQEVDNKIINVLWWYYFSKLIEFMDTFFFILRKNNHQITFLHIYHHASMLNIWWFVMNWVPCGHSYFGASLNSFVHVVMYSYYGLSAIPAMRPYLWWKKYITQLQLIQFFLTMSQTMCAVIWPCDFPKGWLYFQISYMVVLVFLFSNFYIQTYKKHSGSLKKEHQNGSPVSTNGHANGTASMERTEHKKLRVD

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias267-283Polar residues
Compositional bias284-294Basic and acidic residues

Keywords

Sequence databases

Genome annotation databases

Similar Proteins

Disclaimer

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