SOAT2
entrez
8435
canonical
uniprot
O75908
canonical
ensembl
ENSG00000167780
resolver
ensp
ENSP00000301466
resolver
ensp
ENSP00000539170
resolver
genesymbol
SOAT2
resolver
genesymbol_syn
ACACT2
resolver
genesymbol_syn
ACAT2
resolver
hgnc
HGNC:11178
resolver
uniprot
F5H7W4
resolver
uniprot
I6L9H9
resolver
uniprot
Q4VB99
resolver
uniprot
Q4VBA1
resolver
uniprot
Q96TD4
resolver
uniprot
Q9UNR2
resolver
uniprot_entry
SOAT2_HUMAN
resolver
uniprot_sec
F5H7W4
resolver
uniprot_sec
I6L9H9
resolver
uniprot_sec
Q4VB99
resolver
uniprot_sec
Q4VBA1
resolver
uniprot_sec
Q96TD4
resolver
uniprot_sec
Q9UNR2
resolver
amino_acid_sequence
MEPGGARLRLQRTEGLGGERERQPCGDGNTETHRAPDLVQWTRHMEAVKAQLLEQAQGQLRELLDRAMREAIQSYPSQDKPLPPPPPGSLSRTQEPSLGKQKVFIIRKSLLDELMEVQHFRTIYHMFIAGLCVFIISTLAIDFIDEGRLLLEFDLLIFSFGQLPLALVTWVPMFLSTLLAPYQALRLWARGTWTQATGLGCALLAAHAVVLCALPVHVAVEHQLPPASRCVLVFEQVRFLMKSYSFLREAVPGTLRARRGEGIQAPSFSSYLYFLFCPTLIYRETYPRTPYVRWNYVAKNFAQALGCVLYACFILGRLCVPVFANMSREPFSTRALVLSILHATLPGIFMLLLIFFAFLHCWLNAFAEMLRFGDRMFYRDWWNSTSFSNYYRTWNVVVHDWLYSYVYQDGLRLLGARARGVAMLGVFLVSAVAHEYIFCFVLGFFYPVMLILFLVIGGMLNFMMHDQRTGPAWNVLMWTMLFLGQGIQVSLYCQEWYARRHCPLPQATFWGLVTPRSWSCHT
uniprot
proteins
ec_number
2.3.1.26
uniprot
proteins
function
FUNCTION: Catalyzes the formation of fatty acid-cholesterol esters, which are less soluble in membranes than cholesterol (PubMed:11294643, PubMed:16647063). Plays a role in lipoprotein assembly and dietary cholesterol absorption (PubMed:11294643). Utilizes oleoyl-CoA ((9Z)-octadecenoyl-CoA) and linolenoyl-CoA ((9Z,12Z,15Z)-octadecatrienoyl-CoA) as substrates (PubMed:11294643). May provide cholesteryl esters for lipoprotein secretion from hepatocytes and intestinal mucosa (PubMed:11294643). {ECO:0000269|PubMed:11294643, ECO:0000269|PubMed:16647063}.; FUNCTION: [Isoform 2]: Has lower enzymatic activity compared to isoform 1. {ECO:0000269|PubMed:16331323}.; FUNCTION: [Isoform 3]: Has lower enzymatic activity compared to isoform 1. {ECO:0000269|PubMed:16331323}.
uniprot
proteins
mass_dalton
59896
uniprot
proteins
mutagenesis
MUTAGEN 49; /note="K->R: In K-null mutant; does not affect ubiquitination and sterol-regulated stabilization; when associated with R-80, R-100, R-102, R-108, R-242 and R-299."; /evidence="ECO:0000269|PubMed:28604676"; MUTAGEN 80; /note="K->R: In K-null mutant; does not affect ubiquitination and sterol-regulated stabilization; when associated with R-49, R-100, R-102, R-108, R-242 and R-299."; /evidence="ECO:0000269|PubMed:28604676"; MUTAGEN 100; /note="K->R: In K-null mutant; does not affect ubiquitination and sterol-regulated stabilization; when associated with R-49, R-80, R-102, R-108, R-242 and R-299."; /evidence="ECO:0000269|PubMed:28604676"; MUTAGEN 102; /note="K->R: In K-null mutant; does not affect ubiquitination and sterol-regulated stabilization; when associated with R-49, R-80, R-100, R-108, R-242 and R-299."; /evidence="ECO:0000269|PubMed:28604676"; MUTAGEN 108; /note="K->R: In K-null mutant; does not affect ubiquitination and sterol-regulated stabilization; when associated with R-49, R-80, R-100, R-102, R-242 and R-299."; /evidence="ECO:0000269|PubMed:28604676"; MUTAGEN 242; /note="K->R: In K-null mutant; does not affect ubiquitination and sterol-regulated stabilization; when associated with R-49, R-80, R-100, R-102, R-108 and R-299."; /evidence="ECO:0000269|PubMed:28604676"; MUTAGEN 254; /note="T->A: Does not affect ubiquitination and sterol-regulated stabilization; when associated with R-279."; /evidence="ECO:0000269|PubMed:28604676"; MUTAGEN 267..270; /note="SFSS->AFAA: Does not affect ubiquitination and sterol-regulated stabilization."; /evidence="ECO:0000269|PubMed:28604676"; MUTAGEN 277; /note="C->A: Abolished ubiquitination and sterol-regulated stabilization."; /evidence="ECO:0000269|PubMed:28604676"; MUTAGEN 279; /note="T->A: Does not affect ubiquitination and sterol-regulated stabilization; when associated with R-54."; /evidence="ECO:0000269|PubMed:28604676"; MUTAGEN 299; /note="K->R: In K-null mutant; does not affect ubiquitination and sterol-regulated stabilization; when associated with R-49, R-80, R-100, R-102, R-108 and R-242."; /evidence="ECO:0000269|PubMed:28604676"; MUTAGEN 360; /note="H->A: Abolished cholesterol O-acyltransferase activity."; /evidence="ECO:0000269|PubMed:16647063"; MUTAGEN 399; /note="H->A: Abolished cholesterol O-acyltransferase activity."; /evidence="ECO:0000269|PubMed:16647063
uniprot
proteins
post_translational_modification
PTM: Polyubiquitinated by AMFR/gp78 at Cys-277, leading to its degradation when the lipid levels are low (PubMed:28604676). Association with AMFR/gp78 is mediated via interaction with INSIG1 (PubMed:28604676). High concentration of cholesterol and fatty acid results in Cys-277 oxidation, preventing ubiquitination at the same site, resulting in protein stabilization (PubMed:28604676). {ECO:0000269|PubMed:28604676}.; PTM: Oxidized at Cys-277: high concentration of cholesterol and fatty acid induce reactive oxygen species, which oxidizes Cys-277, preventing ubiquitination at the same site, and resulting in protein stabilization. {ECO:0000269|PubMed:28604676}.
uniprot
proteins
protein_family
Membrane-bound acyltransferase family
uniprot
proteins
protein_family
Sterol o-acyltransferase subfamily
uniprot
proteins
pubmed
10846185
uniprot
proteins
pubmed
11294643
uniprot
proteins
pubmed
11325614
uniprot
proteins
pubmed
11401500
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16331323
uniprot
proteins
pubmed
16541075
uniprot
proteins
pubmed
16647063
uniprot
proteins
pubmed
28604676
uniprot
proteins
pubmed
29184177
uniprot
proteins
pubmed
9756920
uniprot
proteins
sequence_length
522
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:O88908}; Multi-pass membrane protein {ECO:0000255}.
uniprot
proteins
transmembrane_region
TRANSMEM 121..142; /note="Helical; Name=1"; /evidence="ECO:0000250|UniProtKB:P35610"; TRANSMEM 163..188; /note="Helical; Name=2"; /evidence="ECO:0000250|UniProtKB:P35610"; TRANSMEM 197..220; /note="Helical; Name=3"; /evidence="ECO:0000250|UniProtKB:P35610"; TRANSMEM 229..252; /note="Helical; Name=4"; /evidence="ECO:0000250|UniProtKB:P35610"; TRANSMEM 294..326; /note="Helical; Name=5"; /evidence="ECO:0000250|UniProtKB:P35610"; TRANSMEM 344..369; /note="Helical; Name=6"; /evidence="ECO:0000250|UniProtKB:P35610"; TRANSMEM 418..442; /note="Helical; Name=7"; /evidence="ECO:0000250|UniProtKB:P35610"; TRANSMEM 449..464; /note="Helical; Name=8"; /evidence="ECO:0000250|UniProtKB:P35610"; TRANSMEM 471..502; /note="Helical; Name=9"; /evidence="ECO:0000250|UniProtKB:P35610
uniprot
proteins