Q7TQM4 · SOAT2_RAT

  • Protein
    Sterol O-acyltransferase 2
  • Gene
    Soat2
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at transcript level
  • Annotation score
    5/5

Function

function

Catalyzes the formation of fatty acid-cholesterol esters, which are less soluble in membranes than cholesterol. Plays a role in lipoprotein assembly and dietary cholesterol absorption. Utilizes oleoyl-CoA ((9Z)-octadecenoyl-CoA) and linolenoyl-CoA ((9Z,12Z,15Z)-octadecatrienoyl-CoA) as substrates. May provide cholesteryl esters for lipoprotein secretion from hepatocytes and intestinal mucosa.

Catalytic activity

  • a long-chain fatty acyl-CoA + a sterol = a sterol ester + CoA
    This reaction proceeds in the forward direction.
    EC:2.3.1.26 (UniProtKB | ENZYME | Rhea)
  • an acyl-CoA + cholesterol = a cholesterol ester + CoA
    This reaction proceeds in the forward direction.
  • (9Z)-octadecenoyl-CoA + cholesterol = cholesteryl (9Z-octadecenoate) + CoA
    This reaction proceeds in the forward direction.
  • (5Z,8Z,11Z,14Z,17Z)-eicosapentaenoyl-CoA + cholesterol = (5Z,8Z,11Z,14Z,17Z-eicosapentaenoyl)-cholesterol + CoA
    This reaction proceeds in the forward direction.
  • (9Z,12Z,15Z)-octadecatrienoyl-CoA + cholesterol = (9Z,12Z,15Z-octadecatrienoyl)-cholesterol + CoA
    This reaction proceeds in the forward direction.
  • (5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + cholesterol = cholesteryl (5Z,8Z,11Z,14Z)-eicosatetraenoate + CoA
    This reaction proceeds in the forward direction.

Features

Showing features for binding site, active site.

TypeIDPosition(s)Description
Binding site117cholesterol (UniProtKB | ChEBI)
Binding site391an acyl-CoA (UniProtKB | ChEBI)
Binding site394an acyl-CoA (UniProtKB | ChEBI)
Binding site397an acyl-CoA (UniProtKB | ChEBI)
Binding site401an acyl-CoA (UniProtKB | ChEBI)
Binding site409an acyl-CoA (UniProtKB | ChEBI)
Binding site432an acyl-CoA (UniProtKB | ChEBI)
Active site436

GO annotations

AspectTerm
Cellular Componentbrush border
Cellular Componentendoplasmic reticulum
Cellular Componentendoplasmic reticulum membrane
Cellular Componentmembrane
Molecular Functioncholesterol binding
Molecular Functioncholesterol O-acyltransferase activity
Molecular Functionfatty-acyl-CoA binding
Molecular Functionsterol O-acyltransferase activity
Biological Processcholesterol efflux
Biological Processcholesterol homeostasis
Biological Processcholesterol metabolic process
Biological Processcholesterol storage
Biological Processresponse to nutrient
Biological Processvery-low-density lipoprotein particle assembly

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Sterol O-acyltransferase 2
  • EC number
  • Alternative names
    • Acyl-coenzyme A:cholesterol acyltransferase 2 (ACAT-2)
    • Cholesterol acyltransferase 2

Gene names

    • Name
      Soat2
    • Synonyms
      Acat2

Organism names

  • Taxonomic identifier
  • Strain
    • Sprague-Dawley
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Rattus

Accessions

  • Primary accession
    Q7TQM4

Proteomes

Organism-specific databases

Subcellular Location

Features

Showing features for topological domain, transmembrane.

TypeIDPosition(s)Description
Topological domain1-118Cytoplasmic
Transmembrane119-140Helical; Name=1
Topological domain141-160Lumenal
Transmembrane161-186Helical; Name=2
Topological domain187-198Cytoplasmic
Transmembrane199-222Helical; Name=3
Topological domain223-230Lumenal
Transmembrane231-254Helical; Name=4
Topological domain255-295Cytoplasmic
Transmembrane296-328Helical; Name=5
Topological domain329-345Lumenal
Transmembrane346-371Helical; Name=6
Topological domain372-419Cytoplasmic
Transmembrane420-444Helical; Name=7
Topological domain445-450Lumenal
Transmembrane451-466Helical; Name=8
Topological domain467-472Cytoplasmic
Transmembrane473-504Helical; Name=9
Topological domain505-524Lumenal

Keywords

Phenotypes & Variants

PTM/Processing

Features

Showing features for chain, modified residue, cross-link.

TypeIDPosition(s)Description
ChainPRO_00002557131-524Sterol O-acyltransferase 2
Modified residue279Cysteine sulfenic acid (-SOH); alternate
Cross-link279Glycyl cysteine thioester (Cys-Gly) (interchain with G-Cter in ubiquitin); alternate

Post-translational modification

Polyubiquitinated by AMFR/gp78 at Cys-279, leading to its degradation when the lipid levels are low. Association with AMFR/gp78 is mediated via interaction with INSIG1. High concentration of cholesterol and fatty acid results in Cys-279 oxidation, preventing ubiquitination at the same site, resulting in protein stabilization.
Oxidized at Cys-279: high concentration of cholesterol and fatty acid induce reactive oxygen species, which oxidizes Cys-279, preventing ubiquitination at the same site, and resulting in protein stabilization.

Keywords

Proteomic databases

PTM databases

Interaction

Subunit

May form homo- or heterodimers (By similarity).
Interacts with INSIG1; the interaction is direct and promotes association with AMFR/gp78 (By similarity).

Protein-protein interaction databases

Chemistry

Structure

Family & Domains

Features

Showing features for compositional bias, region, motif.

TypeIDPosition(s)Description
Compositional bias1-19Basic and acidic residues
Region1-31Disordered
Motif379-385FYXDWWN motif

Domain

Each protomer consists of 9 transmembrane segments, which enclose a cytosolic tunnel and a transmembrane tunnel that converge at the predicted catalytic site: acyl-CoA enters the active site through the cytosolic tunnel, whereas cholesterol enters from the side through the transmembrane tunnel.

Sequence similarities

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    524
  • Mass (Da)
    60,498
  • Last updated
    2003-10-01 v1
  • Checksum
    75CE7DE53F03C88A
MEPKAPQLRRRERQGEEQENGACGEGNTRTHRAPDLVQWTRHMEAVKTQCLEQAQRELAELMDRAIWEAVQAYPKQDRPLPSTASDSTRKTQELHPGKRKVFITRKSLLDELMGVQHFRTIYHMFIAGLCVLIISTLAIDFIDEGRLMLEFDLLLFSFGQLPLALMMWVPMFLSTLLLPYQTLRLWARPRSGGAWTLGASLGCVLLAAHAAVLCVLPVHVSVKHELPPASRCVLVFEQVRFLMKSYSFLRETVPGIFCVRGGKGICTPSFSSYLYFLFCPTLIYRETYPRTPSIRWNYVAKNFAQALGCLLYACFILGRLCVPVFANMSREPFSTRALLLSILHATGPGIFMLLLIFFAFLHCWLNAFAEMLRFGDRMFYRDWWNSTSFSNYYRTWNVVVHDWLYSYVYQDGLWLLGRQGRGAAMLGVFLVSALVHEYIFCFVLGFFYPVMLILFLVVGGLLNFTMNDRHTGPAWNILMWTFLFLGQGIQVSLYCQEWYARRHCPLPQPTFWELVTPRSWSCHP

Computationally mapped potential isoform sequences

There is 1 potential isoform mapped to this entry

View all
EntryEntry nameGene nameLength
G3V7I6G3V7I6_RATSoat2524

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias1-19Basic and acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AB101480
EMBL· GenBank· DDBJ
BAC78210.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

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