Q7TQM4 · SOAT2_RAT
- ProteinSterol O-acyltransferase 2
- GeneSoat2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids524 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score5/5
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 + CoAThis reaction proceeds in the forward direction.
- an acyl-CoA + cholesterol = a cholesterol ester + CoAThis reaction proceeds in the forward direction.
- (9Z)-octadecenoyl-CoA + cholesterol = cholesteryl (9Z-octadecenoate) + CoAThis reaction proceeds in the forward direction.
- (5Z,8Z,11Z,14Z,17Z)-eicosapentaenoyl-CoA + cholesterol = (5Z,8Z,11Z,14Z,17Z-eicosapentaenoyl)-cholesterol + CoAThis reaction proceeds in the forward direction.
- (9Z,12Z,15Z)-octadecatrienoyl-CoA + cholesterol = (9Z,12Z,15Z-octadecatrienoyl)-cholesterol + CoAThis reaction proceeds in the forward direction.
- (5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + cholesterol = cholesteryl (5Z,8Z,11Z,14Z)-eicosatetraenoate + CoAThis reaction proceeds in the forward direction.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 117 | cholesterol (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 391 | an acyl-CoA (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 394 | an acyl-CoA (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 397 | an acyl-CoA (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 401 | an acyl-CoA (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 409 | an acyl-CoA (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 432 | an acyl-CoA (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Active site | 436 | |||||
Sequence: H |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | brush border | |
Cellular Component | endoplasmic reticulum | |
Cellular Component | endoplasmic reticulum membrane | |
Cellular Component | membrane | |
Molecular Function | cholesterol binding | |
Molecular Function | cholesterol O-acyltransferase activity | |
Molecular Function | fatty-acyl-CoA binding | |
Molecular Function | sterol O-acyltransferase activity | |
Biological Process | cholesterol efflux | |
Biological Process | cholesterol homeostasis | |
Biological Process | cholesterol metabolic process | |
Biological Process | cholesterol storage | |
Biological Process | response to nutrient | |
Biological Process | very-low-density lipoprotein particle assembly |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameSterol O-acyltransferase 2
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Rattus
Accessions
- Primary accessionQ7TQM4
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Endoplasmic reticulum membrane ; Multi-pass membrane protein
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-118 | Cytoplasmic | ||||
Sequence: MEPKAPQLRRRERQGEEQENGACGEGNTRTHRAPDLVQWTRHMEAVKTQCLEQAQRELAELMDRAIWEAVQAYPKQDRPLPSTASDSTRKTQELHPGKRKVFITRKSLLDELMGVQHF | ||||||
Transmembrane | 119-140 | Helical; Name=1 | ||||
Sequence: RTIYHMFIAGLCVLIISTLAID | ||||||
Topological domain | 141-160 | Lumenal | ||||
Sequence: FIDEGRLMLEFDLLLFSFGQ | ||||||
Transmembrane | 161-186 | Helical; Name=2 | ||||
Sequence: LPLALMMWVPMFLSTLLLPYQTLRLW | ||||||
Topological domain | 187-198 | Cytoplasmic | ||||
Sequence: ARPRSGGAWTLG | ||||||
Transmembrane | 199-222 | Helical; Name=3 | ||||
Sequence: ASLGCVLLAAHAAVLCVLPVHVSV | ||||||
Topological domain | 223-230 | Lumenal | ||||
Sequence: KHELPPAS | ||||||
Transmembrane | 231-254 | Helical; Name=4 | ||||
Sequence: RCVLVFEQVRFLMKSYSFLRETVP | ||||||
Topological domain | 255-295 | Cytoplasmic | ||||
Sequence: GIFCVRGGKGICTPSFSSYLYFLFCPTLIYRETYPRTPSIR | ||||||
Transmembrane | 296-328 | Helical; Name=5 | ||||
Sequence: WNYVAKNFAQALGCLLYACFILGRLCVPVFANM | ||||||
Topological domain | 329-345 | Lumenal | ||||
Sequence: SREPFSTRALLLSILHA | ||||||
Transmembrane | 346-371 | Helical; Name=6 | ||||
Sequence: TGPGIFMLLLIFFAFLHCWLNAFAEM | ||||||
Topological domain | 372-419 | Cytoplasmic | ||||
Sequence: LRFGDRMFYRDWWNSTSFSNYYRTWNVVVHDWLYSYVYQDGLWLLGRQ | ||||||
Transmembrane | 420-444 | Helical; Name=7 | ||||
Sequence: GRGAAMLGVFLVSALVHEYIFCFVL | ||||||
Topological domain | 445-450 | Lumenal | ||||
Sequence: GFFYPV | ||||||
Transmembrane | 451-466 | Helical; Name=8 | ||||
Sequence: MLILFLVVGGLLNFTM | ||||||
Topological domain | 467-472 | Cytoplasmic | ||||
Sequence: NDRHTG | ||||||
Transmembrane | 473-504 | Helical; Name=9 | ||||
Sequence: PAWNILMWTFLFLGQGIQVSLYCQEWYARRHC | ||||||
Topological domain | 505-524 | Lumenal | ||||
Sequence: PLPQPTFWELVTPRSWSCHP |
Keywords
- Cellular component
Phenotypes & Variants
Chemistry
PTM/Processing
Features
Showing features for chain, modified residue, cross-link.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000255713 | 1-524 | Sterol O-acyltransferase 2 | |||
Sequence: MEPKAPQLRRRERQGEEQENGACGEGNTRTHRAPDLVQWTRHMEAVKTQCLEQAQRELAELMDRAIWEAVQAYPKQDRPLPSTASDSTRKTQELHPGKRKVFITRKSLLDELMGVQHFRTIYHMFIAGLCVLIISTLAIDFIDEGRLMLEFDLLLFSFGQLPLALMMWVPMFLSTLLLPYQTLRLWARPRSGGAWTLGASLGCVLLAAHAAVLCVLPVHVSVKHELPPASRCVLVFEQVRFLMKSYSFLRETVPGIFCVRGGKGICTPSFSSYLYFLFCPTLIYRETYPRTPSIRWNYVAKNFAQALGCLLYACFILGRLCVPVFANMSREPFSTRALLLSILHATGPGIFMLLLIFFAFLHCWLNAFAEMLRFGDRMFYRDWWNSTSFSNYYRTWNVVVHDWLYSYVYQDGLWLLGRQGRGAAMLGVFLVSALVHEYIFCFVLGFFYPVMLILFLVVGGLLNFTMNDRHTGPAWNILMWTFLFLGQGIQVSLYCQEWYARRHCPLPQPTFWELVTPRSWSCHP | ||||||
Modified residue | 279 | Cysteine sulfenic acid (-SOH); alternate | ||||
Sequence: C | ||||||
Cross-link | 279 | Glycyl cysteine thioester (Cys-Gly) (interchain with G-Cter in ubiquitin); alternate | ||||
Sequence: C |
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
- PTM
Proteomic databases
PTM databases
Structure
Family & Domains
Features
Showing features for compositional bias, region, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-19 | Basic and acidic residues | ||||
Sequence: MEPKAPQLRRRERQGEEQE | ||||||
Region | 1-31 | Disordered | ||||
Sequence: MEPKAPQLRRRERQGEEQENGACGEGNTRTH | ||||||
Motif | 379-385 | FYXDWWN motif | ||||
Sequence: FYRDWWN |
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
Belongs to the membrane-bound acyltransferase family. Sterol o-acyltransferase subfamily.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length524
- Mass (Da)60,498
- Last updated2003-10-01 v1
- Checksum75CE7DE53F03C88A
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
G3V7I6 | G3V7I6_RAT | Soat2 | 524 |
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-19 | Basic and acidic residues | ||||
Sequence: MEPKAPQLRRRERQGEEQE |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AB101480 EMBL· GenBank· DDBJ | BAC78210.1 EMBL· GenBank· DDBJ | mRNA |