A0A485MVX2 · A0A485MVX2_LYNPA

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 with higher activity toward C18 acyl-CoAs, especially C18:0 acyl-CoAs. May participate to the production of saturated and monounsaturated 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

Pathway

Lipid metabolism; polyunsaturated fatty acid biosynthesis.

GO annotations

AspectTerm
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 3
  • EC number
  • Alternative names
    • 3-keto acyl-CoA synthase ELOVL3
    • ELOVL fatty acid elongase 3
      (ELOVL FA elongase 3
      )
    • Very long chain 3-ketoacyl-CoA synthase 3
    • Very long chain 3-oxoacyl-CoA synthase 3

Gene names

    • Name
      ELOVL3
    • ORF names
      LYPA_23C006656

Organism names

Accessions

  • Primary accession
    A0A485MVX2

Proteomes

Subcellular Location

Endoplasmic reticulum membrane
; Multi-pass membrane protein
Membrane
; Multi-pass membrane protein

Features

Showing features for transmembrane.

TypeIDPosition(s)Description
Transmembrane33-55Helical
Transmembrane67-87Helical
Transmembrane166-185Helical
Transmembrane197-223Helical
Transmembrane235-254Helical

Keywords

PTM/Processing

Post-translational modification

N-Glycosylated.

Keywords

Family & Domains

Features

Showing features for motif.

TypeIDPosition(s)Description
Motif266-270Di-lysine motif

Domain

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

Sequence similarities

Belongs to the ELO family. ELOVL3 subfamily.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    270
  • Mass (Da)
    31,607
  • Last updated
    2019-06-05 v1
  • Checksum
    F39B9B6965B5A94A
MVTAMNVSDEIDQLFQPYNFELFQDMRPFLEEYWATSFPIALVYLLLIFVGQNYMKARKGFNLQGPLILWSFCLAIFSILGAVRTWGYMGTVLLRGSLKHTVCFSDFIQNSVIKFWSCLFLLSKVIELGDTAFIILRKRPLIFVHWYHHSTVLVYTSFGYKNKVAAGGWFMTMNYGVHAIMYIYYTLRAAKVKSPTWLPKLITSLQILQMFMGTIVGILTYIWRQEQGCHTTTEHFFWSLVLYTTYFILFAHYFHHTYITPKAKAKTKSQ

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CAAGRJ010006514
EMBL· GenBank· DDBJ
VFV24437.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

Any 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. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp