V5I962 · V5I962_ANOGL

Function

function

Mediates the transfer of all common phospholipids, cholesterol and gangliosides from the endoplasmic reticulum to the plasma membrane. May play a role in regulating steroidogenesis. Stimulates the microsomal conversion of 7-dehydrocholesterol to cholesterol. Also binds fatty acids and fatty acyl Coenzyme A (CoA) such as phytanoyl-CoA. Involved in the regulation phospholipid synthesis in endoplasmic reticulum enhancing the incorporation of exogenous fatty acid into glycerides. Seems to stimulate the rate-limiting step in phosphatidic acid formation mediated by GPAT3. Isoforms SCP2 and SCPx cooperate in peroxisomal oxidation of certain naturally occurring tetramethyl-branched fatty acyl-CoAs.
Plays a crucial role in the peroxisomal oxidation of branched-chain fatty acids. Catalyzes the last step of the peroxisomal beta-oxidation of branched chain fatty acids and the side chain of the bile acid intermediates di- and trihydroxycoprostanic acids (DHCA and THCA). Also active with medium and long straight chain 3-oxoacyl-CoAs. Stimulates the microsomal conversion of 7-dehydrocholesterol to cholesterol and transfers phosphatidylcholine and 7-dehydrocholesterol between membrances, in vitro. Isoforms SCP2 and SCPx cooperate in peroxisomal oxidation of certain naturally occurring tetramethyl-branched fatty acyl-CoAs.

Catalytic activity

  • 3-oxo-(9Z-octadecenoyl)-CoA + CoA = (7Z)-hexadecenoyl-CoA + acetyl-CoA
    This reaction proceeds in the forward direction.
  • 3-oxohexadecanedioyl-CoA + CoA = tetradecanedioyl-CoA + acetyl-CoA
    This reaction proceeds in the forward direction.
  • 7-dehydrocholesterol(in) = 7-dehydrocholesterol(out)
  • an acyl-CoA + acetyl-CoA = a 3-oxoacyl-CoA + CoA
    This reaction proceeds in the backward direction.
    EC:2.3.1.16 (UniProtKB | ENZYME | Rhea)
  • butanoyl-CoA + acetyl-CoA = 3-oxohexanoyl-CoA + CoA
    This reaction proceeds in the backward direction.
  • decanoyl-CoA + acetyl-CoA = 3-oxododecanoyl-CoA + CoA
    This reaction proceeds in the backward direction.
  • dodecanoyl-CoA + acetyl-CoA = 3-oxotetradecanoyl-CoA + CoA
    This reaction proceeds in the backward direction.
  • hexadecanoyl-CoA + acetyl-CoA = 3-oxooctadecanoyl-CoA + CoA
    This reaction proceeds in the backward direction.
  • hexanoyl-CoA + acetyl-CoA = 3-oxooctanoyl-CoA + CoA
    This reaction proceeds in the backward direction.
  • octanoyl-CoA + acetyl-CoA = 3-oxodecanoyl-CoA + CoA
    This reaction proceeds in the backward direction.
  • tetradecanoyl-CoA + acetyl-CoA = 3-oxohexadecanoyl-CoA + CoA
    This reaction proceeds in the backward direction.
    EC:2.3.1.155 (UniProtKB | ENZYME | Rhea)
  • choloyl-CoA + propanoyl-CoA = 3alpha,7alpha,12alpha-trihydroxy-24-oxo-5beta-cholestan-26-oyl-CoA + CoA
    This reaction proceeds in the backward direction.
    EC:2.3.1.176 (UniProtKB | ENZYME | Rhea)
  • propanoyl-CoA + tetradecanoyl-CoA = 3-oxo-2-methylhexadecanoyl-CoA + CoA
    This reaction proceeds in the backward direction.

GO annotations

AspectTerm
Cellular Componentmitochondrion
Cellular Componentperoxisome
Molecular Functionacetyl-CoA C-acyltransferase activity
Molecular Functionacetyl-CoA C-myristoyltransferase activity
Molecular Functionlipid binding
Molecular Functionpropanoyl-CoA C-acyltransferase activity
Molecular Functionpropionyl-CoA C2-trimethyltridecanoyltransferase activity
Biological Processlipid transport

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Sterol carrier protein 2
  • EC number
  • Alternative names
    • Acetyl-CoA C-myristoyltransferase
    • Non-specific lipid-transfer protein
    • Propanoyl-CoA C-acyltransferase
    • SCP-2/3-oxoacyl-CoA thiolase
    • SCP-2/thiolase

Gene names

    • Name
      NLTP

Organism names

Accessions

  • Primary accession
    V5I962

Subcellular Location

Keywords

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain4-227Thiolase N-terminal
Domain264-382Thiolase C-terminal
Domain425-524SCP2

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    538
  • Mass (Da)
    58,794
  • Last updated
    2014-01-22 v1
  • Checksum
    2AEB7ECAB5E4D923
MGRVFVIGVGMTKFEKPGKRTDDYPQWGKQAITAALTDANIHMSEVELATAGYVYGDSTSGQRVIYEVGMTGIPIFNVNNNCSTGSSALMLAKELVESGKYNCALALGFEKMERGSLSSKFMDRSNPMEKHIEAMSNLADIDGSPITAQMFGNAAIEHMKRYGTKAEHFAKIAYKNHKHSINNPYSQFQDEYTLDQILKSPKIYGPLTKLQCCPTSDGAAAAILASETFVRRHGLERQAVEILAMEMVTDLPSTFLDNSHMKIVGYDMSKTAAERVFRKTNKDPSDVQVVELHDCFSANELITYEALGLCPPGRAGEFIDRGDNTYGGKFVVNPSGGLISKGHPLGATGLAQCSELCWQLRGEAERRQVANAKLALQHNIGLGGAVVVALYQLGFPEYANRNVGIRRTAAAVSDSGFIVTPYMKILQQAMEDDEEGLIENHRGIYALKVAKANGDTGTWVINCKTGKGKIEFNGKDKPDVTFIVKDSDVIELLTGKIPPQKAFFQGKVKIQGNIGLAVKLTELQRTAAKKIEDLRAKL

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
GALX01003490
EMBL· GenBank· DDBJ
JAB64976.1
EMBL· GenBank· DDBJ
Transcribed RNA

Genome annotation databases

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