A0A158PKN0 · A0A158PKN0_ANGCS

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

    • ORF names
      ACOC_LOCUS10319

Organism names

  • Taxonomic identifier
  • Strain
    • Costa Rica
  • Taxonomic lineage
    Eukaryota > Metazoa > Ecdysozoa > Nematoda > Chromadorea > Rhabditida > Rhabditina > Rhabditomorpha > Strongyloidea > Metastrongylidae > Angiostrongylus

Accessions

  • Primary accession
    A0A158PKN0

Proteomes

Subcellular Location

Keywords

Interaction

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain6-232Thiolase N-terminal
Domain250-352Thiolase C-terminal
Domain381-460SCP2

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    468
  • Mass (Da)
    51,050
  • Last updated
    2016-06-08 v1
  • Checksum
    46EE5A50A3C0EC25
MGNTKVYVIGVGMTKFCKPGSRDWDYPDMVKEAVNLALDDCSLKYSDIEMATVSYLFGGTCCGQRALYELGLTGIPIFNVNNACASGSSGVFLCKQFIESGNADCVLACGFEKMAPGSLDSQAENNDDRILPIDKHIQVIADTYGLFPAPMMAQMFGNAGKEHMEKYGTKREHFAKIAWKNHLHSVHNPNSQFTKEYTLDQVLNAKNIYDFMGLLECSPTSDGSAAAVICSERFLEQHSHLRPQAVEIVETGLTPNDVQVIELHDCFAPNELITYEALGLCDIGKGGTIVDRGDNTYGGKWVINPSGGLISKGHPIGATGVAQVVELSNQLRGKCGKRQVPNCKLALQHNIGIGGAGVVGLYRLGLPSSTSTPVMTTNGDKNLLEKVDSSFKINIIGNNGSTKKWIINAKKPFEIEITIKDNDLMRIAAGKLRPDQAYMQGRMKMKGNVVKSTKLKFLFDPEMLKAKF

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
UYYA01004448
EMBL· GenBank· DDBJ
VDM61904.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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