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Sterol O-acyltransferase 2 (EC 2.3.1.26) (Acyl-coenzyme A:cholesterol acyltransferase 2) (ACAT-2) (Cholesterol acyltransferase 2)

 SOAT2_HUMAN             Reviewed;         522 AA.
O75908; F5H7W4; I6L9H9; Q4VB99; Q4VBA1; Q96TD4; Q9UNR2;
18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
01-NOV-1998, sequence version 1.
12-AUG-2020, entry version 161.
RecName: Full=Sterol O-acyltransferase 2 {ECO:0000305};
EC=2.3.1.26 {ECO:0000305|PubMed:11294643};
AltName: Full=Acyl-coenzyme A:cholesterol acyltransferase 2;
Short=ACAT-2;
AltName: Full=Cholesterol acyltransferase 2;
Name=SOAT2 {ECO:0000312|HGNC:HGNC:11178}; Synonyms=ACACT2, ACAT2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=9756920; DOI=10.1074/jbc.273.41.26765;
Oelkers P., Behari A., Cromley D., Billheimer J.T., Sturley S.L.;
"Characterization of two human genes encoding acyl coenzyme A:cholesterol
acyltransferase-related enzymes.";
J. Biol. Chem. 273:26765-26771(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT ILE-254.
TISSUE=Intestine;
PubMed=10846185; DOI=10.1074/jbc.m003927200;
Chang C.C.Y., Sakashita N., Ornvold K., Lee O., Chang E.T., Dong R.,
Lin S., Lee C.-Y.G., Strom S.C., Kashyap R., Fung J.J., Farese R.V. Jr.,
Patoiseau J.-F., Delhon A., Chang T.-Y.;
"Immunological quantitation and localization of ACAT-1 and ACAT-2 in human
liver and small intestine.";
J. Biol. Chem. 275:28083-28092(2000).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=11325614; DOI=10.1016/s1388-1981(01)00106-8;
Katsuren K., Tamura T., Arashiro R., Takata K., Matsuura T., Niikawa N.,
Ohta T.;
"Structure of the human acyl-CoA:cholesterol acyltransferase-2 (ACAT-2)
gene and its relation to dyslipidemia.";
Biochim. Biophys. Acta 1531:230-240(2001).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=11401500; DOI=10.1006/bbrc.2001.4612;
Song B.L., Qi W., Yang X.Y., Chang C.C.Y., Zhu J.Q., Chang T.Y., Li B.L.;
"Organization of human ACAT-2 gene and its cell-type-specific promoter
activity.";
Biochem. Biophys. Res. Commun. 282:580-588(2001).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16541075; DOI=10.1038/nature04569;
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
Gibbs R.A.;
"The finished DNA sequence of human chromosome 12.";
Nature 440:346-351(2006).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4), AND VARIANTS
GLY-14 AND ILE-254.
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project:
the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
CATALYTIC ACTIVITY, AND FUNCTION.
PubMed=11294643; DOI=10.1021/bi0022947;
Seo T., Oelkers P.M., Giattina M.R., Worgall T.S., Sturley S.L.,
Deckelbaum R.J.;
"Differential modulation of ACAT1 and ACAT2 transcription and activity by
long chain free fatty acids in cultured cells.";
Biochemistry 40:4756-4762(2001).
[8]
TISSUE SPECIFICITY, FUNCTION (ISOFORMS 2 AND 3), AND ALTERNATIVE SPLICING
(ISOFORMS 2 AND 3).
PubMed=16331323; DOI=10.1111/j.1745-7270.2005.00118.x;
Yao X.M., Wang C.H., Song B.L., Yang X.Y., Wang Z.Z., Qi W., Lin Z.X.,
Chang C.C., Chang T.Y., Li B.L.;
"Two human ACAT2 mRNA variants produced by alternative splicing and coding
for novel isoenzymes.";
Acta Biochim. Biophys. Sin. 37:797-806(2005).
[9]
INTERACTION WITH INSIG1, UBIQUITINATION AT CYS-277, OXIDATION AT CYS-277,
AND MUTAGENESIS OF LYS-49; LYS-80; LYS-100; LYS-102; LYS-108; LYS-242;
THR-254; 267-SER--SER-270; CYS-277; THR-279 AND LYS-299.
PubMed=28604676; DOI=10.1038/ncb3551;
Wang Y.J., Bian Y., Luo J., Lu M., Xiong Y., Guo S.Y., Yin H.Y., Lin X.,
Li Q., Chang C.C.Y., Chang T.Y., Li B.L., Song B.L.;
"Cholesterol and fatty acids regulate cysteine ubiquitylation of ACAT2
through competitive oxidation.";
Nat. Cell Biol. 19:808-819(2017).
[10]
ERRATUM OF PUBMED:28604676.
PubMed=29184177; DOI=10.1038/ncb3651;
Wang Y.J., Bian Y., Luo J., Lu M., Xiong Y., Guo S.Y., Yong H., Lin X.,
Li Q., Chang C.C.Y., Chang T.Y., Li B.L., Song B.L.;
"Corrigendum: Cholesterol and fatty acids regulate cysteine ubiquitylation
of ACAT2 through competitive oxidation.";
Nat. Cell Biol. 19:1441-1441(2017).
-!- FUNCTION: Catalyzes the formation of fatty acid-cholesterol esters,
which are less soluble in membranes than cholesterol (PubMed:11294643).
Plays a role in lipoprotein assembly and dietary cholesterol absorption
(PubMed:11294643). In addition to its acyltransferase activity, it may
act as a ligase (PubMed:11294643). Utilizes oleoyl-CoA and linolenoyl-
CoA as substrates (PubMed:11294643). May provide cholesteryl esters for
lipoprotein secretion from hepatocytes and intestinal mucosa
(PubMed:11294643). {ECO:0000269|PubMed:11294643}.
-!- 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}.
-!- CATALYTIC ACTIVITY:
Reaction=an acyl-CoA + cholesterol = a cholesterol ester + CoA;
Xref=Rhea:RHEA:17729, ChEBI:CHEBI:16113, ChEBI:CHEBI:17002,
ChEBI:CHEBI:57287, ChEBI:CHEBI:58342; EC=2.3.1.26;
Evidence={ECO:0000305|PubMed:11294643};
PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17730;
Evidence={ECO:0000305|PubMed:11294643};
-!- CATALYTIC ACTIVITY:
Reaction=(9Z)-octadecenoyl-CoA + cholesterol = cholesteryl (9Z-
octadecenoate) + CoA; Xref=Rhea:RHEA:41436, ChEBI:CHEBI:16113,
ChEBI:CHEBI:46898, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387;
Evidence={ECO:0000269|PubMed:11294643};
PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41437;
Evidence={ECO:0000305|PubMed:11294643};
-!- CATALYTIC ACTIVITY:
Reaction=(5Z,8Z,11Z,14Z,17Z)-eicosapentaenoyl-CoA + cholesterol =
cholesteryl (5Z,8Z,11Z,14Z,17Z-eicosapentaenoate) + CoA;
Xref=Rhea:RHEA:46612, ChEBI:CHEBI:16113, ChEBI:CHEBI:57287,
ChEBI:CHEBI:73862, ChEBI:CHEBI:84969;
Evidence={ECO:0000269|PubMed:11294643};
PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46613;
Evidence={ECO:0000305|PubMed:11294643};
-!- CATALYTIC ACTIVITY:
Reaction=(9Z,12Z,15Z)-octadecatrienoyl-CoA + cholesterol = cholesteryl
(9Z,12Z,15Z)-octadecatrienoate + CoA; Xref=Rhea:RHEA:46620,
ChEBI:CHEBI:16113, ChEBI:CHEBI:57287, ChEBI:CHEBI:74034,
ChEBI:CHEBI:84341; Evidence={ECO:0000269|PubMed:11294643};
PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46621;
Evidence={ECO:0000305|PubMed:11294643};
-!- CATALYTIC ACTIVITY:
Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + cholesterol =
cholesteryl (5Z,8Z,11Z,14Z)-eicosatetraenoate + CoA;
Xref=Rhea:RHEA:42816, ChEBI:CHEBI:16113, ChEBI:CHEBI:57287,
ChEBI:CHEBI:57368, ChEBI:CHEBI:82751;
Evidence={ECO:0000269|PubMed:11294643};
PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42817;
Evidence={ECO:0000305|PubMed:11294643};
-!- SUBUNIT: May form homo- or heterodimers (By similarity). Interacts with
INSIG1; the interaction is direct and promotes association with
AMFR/gp78 (PubMed:28604676). {ECO:0000250|UniProtKB:P35610,
ECO:0000269|PubMed:28604676}.
-!- INTERACTION:
O75908; P55061: TMBIM6; NbExp=3; IntAct=EBI-9055438, EBI-1045825;
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
{ECO:0000250|UniProtKB:O88908}; Multi-pass membrane protein
{ECO:0000255}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1; Synonyms=ACAD2a;
IsoId=O75908-1; Sequence=Displayed;
Name=2; Synonyms=ACAD2b;
IsoId=O75908-2; Sequence=VSP_057159;
Name=3; Synonyms=ACAD2c;
IsoId=O75908-3; Sequence=VSP_057158, VSP_057160;
Name=4;
IsoId=O75908-4; Sequence=VSP_057161, VSP_057162;
-!- TISSUE SPECIFICITY: Expression seems confined in hepatocytes and
enterocytes. {ECO:0000269|PubMed:16331323}.
-!- 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}.
-!- SIMILARITY: Belongs to the membrane-bound acyltransferase family.
Sterol o-acyltransferase subfamily. {ECO:0000305}.
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EMBL; AF059203; AAC63998.1; -; mRNA.
EMBL; AF099031; AAC78335.2; -; mRNA.
EMBL; AF331516; AAK18275.1; -; Genomic_DNA.
EMBL; AF331502; AAK18275.1; JOINED; Genomic_DNA.
EMBL; AF331503; AAK18275.1; JOINED; Genomic_DNA.
EMBL; AF331504; AAK18275.1; JOINED; Genomic_DNA.
EMBL; AF331505; AAK18275.1; JOINED; Genomic_DNA.
EMBL; AF331506; AAK18275.1; JOINED; Genomic_DNA.
EMBL; AF331507; AAK18275.1; JOINED; Genomic_DNA.
EMBL; AF331508; AAK18275.1; JOINED; Genomic_DNA.
EMBL; AF331509; AAK18275.1; JOINED; Genomic_DNA.
EMBL; AF331510; AAK18275.1; JOINED; Genomic_DNA.
EMBL; AF331511; AAK18275.1; JOINED; Genomic_DNA.
EMBL; AF331512; AAK18275.1; JOINED; Genomic_DNA.
EMBL; AF331513; AAK18275.1; JOINED; Genomic_DNA.
EMBL; AF331514; AAK18275.1; JOINED; Genomic_DNA.
EMBL; AF331515; AAK18275.1; JOINED; Genomic_DNA.
EMBL; AF332858; AAK48829.1; -; Genomic_DNA.
EMBL; AF332857; AAK48829.1; JOINED; Genomic_DNA.
EMBL; AC073573; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC096090; AAH96090.1; -; mRNA.
EMBL; BC096091; AAH96091.1; -; mRNA.
EMBL; BC096092; AAH96092.1; -; mRNA.
EMBL; BC099626; AAH99626.1; -; mRNA.
CCDS; CCDS8847.1; -. [O75908-1]
RefSeq; NP_003569.1; NM_003578.3. [O75908-1]
BioGRID; 114015; 4.
IntAct; O75908; 3.
MINT; O75908; -.
STRING; 9606.ENSP00000301466; -.
BindingDB; O75908; -.
ChEMBL; CHEMBL4465; -.
DrugBank; DB01094; Hesperetin.
SwissLipids; SLP:000001262; -. [O75908-1]
iPTMnet; O75908; -.
PhosphoSitePlus; O75908; -.
SwissPalm; O75908; -.
BioMuta; SOAT2; -.
MassIVE; O75908; -.
PaxDb; O75908; -.
PeptideAtlas; O75908; -.
PRIDE; O75908; -.
ProteomicsDB; 27608; -.
ProteomicsDB; 50258; -. [O75908-1]
Antibodypedia; 43294; 137 antibodies.
Ensembl; ENST00000301466; ENSP00000301466; ENSG00000167780. [O75908-1]
Ensembl; ENST00000542365; ENSP00000442234; ENSG00000167780. [O75908-4]
GeneID; 8435; -.
KEGG; hsa:8435; -.
UCSC; uc001sbv.4; human. [O75908-1]
CTD; 8435; -.
DisGeNET; 8435; -.
EuPathDB; HostDB:ENSG00000167780.11; -.
GeneCards; SOAT2; -.
HGNC; HGNC:11178; SOAT2.
HPA; ENSG00000167780; Tissue enriched (intestine).
MIM; 601311; gene.
neXtProt; NX_O75908; -.
OpenTargets; ENSG00000167780; -.
PharmGKB; PA36016; -.
eggNOG; KOG0380; Eukaryota.
GeneTree; ENSGT00950000183081; -.
HOGENOM; CLU_031845_1_0_1; -.
InParanoid; O75908; -.
KO; K00637; -.
OMA; TMNDRHT; -.
OrthoDB; 1275897at2759; -.
PhylomeDB; O75908; -.
TreeFam; TF315226; -.
BRENDA; 2.3.1.26; 2681.
PathwayCommons; O75908; -.
Reactome; R-HSA-8964038; LDL clearance.
SABIO-RK; O75908; -.
BioGRID-ORCS; 8435; 15 hits in 872 CRISPR screens.
GeneWiki; SOAT2; -.
GenomeRNAi; 8435; -.
Pharos; O75908; Tchem.
PRO; PR:O75908; -.
Proteomes; UP000005640; Chromosome 12.
RNAct; O75908; protein.
Bgee; ENSG00000167780; Expressed in liver and 87 other tissues.
ExpressionAtlas; O75908; baseline and differential.
Genevisible; O75908; HS.
GO; GO:0005903; C:brush border; IDA:BHF-UCL.
GO; GO:0005783; C:endoplasmic reticulum; IDA:BHF-UCL.
GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:BHF-UCL.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0015485; F:cholesterol binding; IDA:BHF-UCL.
GO; GO:0034736; F:cholesterol O-acyltransferase activity; IDA:BHF-UCL.
GO; GO:0000062; F:fatty-acyl-CoA binding; IDA:BHF-UCL.
GO; GO:0008374; F:O-acyltransferase activity; IBA:GO_Central.
GO; GO:0004772; F:sterol O-acyltransferase activity; IDA:UniProtKB.
GO; GO:0016746; F:transferase activity, transferring acyl groups; TAS:ProtInc.
GO; GO:0033344; P:cholesterol efflux; IMP:BHF-UCL.
GO; GO:0034435; P:cholesterol esterification; IDA:UniProtKB.
GO; GO:0042632; P:cholesterol homeostasis; TAS:BHF-UCL.
GO; GO:0008203; P:cholesterol metabolic process; IDA:UniProtKB.
GO; GO:0030299; P:intestinal cholesterol absorption; IC:BHF-UCL.
GO; GO:0034383; P:low-density lipoprotein particle clearance; TAS:Reactome.
GO; GO:0010742; P:macrophage derived foam cell differentiation; TAS:BHF-UCL.
GO; GO:0034379; P:very-low-density lipoprotein particle assembly; IMP:BHF-UCL.
InterPro; IPR004299; MBOAT_fam.
InterPro; IPR014371; Oat_ACAT_DAG_ARE.
InterPro; IPR030687; Sterol_acyltranf_meta.
PANTHER; PTHR10408; PTHR10408; 1.
Pfam; PF03062; MBOAT; 1.
PIRSF; PIRSF000439; Oat_ACAT_DAG_ARE; 1.
PIRSF; PIRSF500230; Sterol_acyltranf_ACAT; 1.
1: Evidence at protein level;
Acyltransferase; Alternative splicing; Cholesterol metabolism;
Endoplasmic reticulum; Lipid metabolism; Membrane; Oxidation; Polymorphism;
Reference proteome; Steroid metabolism; Sterol metabolism; Thioester bond;
Transferase; Transmembrane; Transmembrane helix; Ubl conjugation.
CHAIN 1..522
/note="Sterol O-acyltransferase 2"
/id="PRO_0000207645"
TOPO_DOM 1..122
/note="Cytoplasmic"
/evidence="ECO:0000255"
TRANSMEM 123..141
/note="Helical"
/evidence="ECO:0000255"
TOPO_DOM 142..160
/note="Lumenal"
/evidence="ECO:0000255"
TRANSMEM 161..179
/note="Helical"
/evidence="ECO:0000255"
TOPO_DOM 180..200
/note="Cytoplasmic"
/evidence="ECO:0000255"
TRANSMEM 201..219
/note="Helical"
/evidence="ECO:0000255"
TOPO_DOM 220..340
/note="Lumenal"
/evidence="ECO:0000255"
TRANSMEM 341..363
/note="Helical"
/evidence="ECO:0000255"
TOPO_DOM 364..475
/note="Cytoplasmic"
/evidence="ECO:0000255"
TRANSMEM 476..494
/note="Helical"
/evidence="ECO:0000255"
TOPO_DOM 495..522
/note="Lumenal"
/evidence="ECO:0000255"
ACT_SITE 434
/evidence="ECO:0000255"
MOD_RES 277
/note="Cysteine sulfenic acid (-SOH); alternate"
/evidence="ECO:0000269|PubMed:28604676"
CROSSLNK 277
/note="Glycyl cysteine thioester (Cys-Gly) (interchain with
G-Cter in ubiquitin); alternate"
/evidence="ECO:0000269|PubMed:28604676"
VAR_SEQ 93..148
/note="Missing (in isoform 3)"
/evidence="ECO:0000269|PubMed:16331323"
/id="VSP_057158"
VAR_SEQ 93..112
/note="Missing (in isoform 2)"
/evidence="ECO:0000269|PubMed:16331323"
/id="VSP_057159"
VAR_SEQ 236..261
/note="Missing (in isoform 3)"
/evidence="ECO:0000269|PubMed:16331323"
/id="VSP_057160"
VAR_SEQ 289..310
/note="TPYVRWNYVAKNFAQALGCVLY -> PWDVCSMPASSWAASVFLSLPT (in
isoform 4)"
/evidence="ECO:0000303|PubMed:15489334"
/id="VSP_057161"
VAR_SEQ 311..522
/note="Missing (in isoform 4)"
/evidence="ECO:0000303|PubMed:15489334"
/id="VSP_057162"
VARIANT 14
/note="E -> G (in dbSNP:rs9658625)"
/evidence="ECO:0000269|PubMed:15489334"
/id="VAR_020373"
VARIANT 254
/note="T -> I (in dbSNP:rs2272296)"
/evidence="ECO:0000269|PubMed:10846185,
ECO:0000269|PubMed:15489334"
/id="VAR_020374"
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"
CONFLICT 22
/note="R -> P (in Ref. 4; AAK48829)"
/evidence="ECO:0000305"
SEQUENCE 522 AA; 59896 MW; EEAC2DB569FFE729 CRC64;
MEPGGARLRL QRTEGLGGER ERQPCGDGNT ETHRAPDLVQ WTRHMEAVKA QLLEQAQGQL
RELLDRAMRE AIQSYPSQDK PLPPPPPGSL SRTQEPSLGK QKVFIIRKSL LDELMEVQHF
RTIYHMFIAG LCVFIISTLA IDFIDEGRLL LEFDLLIFSF GQLPLALVTW VPMFLSTLLA
PYQALRLWAR GTWTQATGLG CALLAAHAVV LCALPVHVAV EHQLPPASRC VLVFEQVRFL
MKSYSFLREA VPGTLRARRG EGIQAPSFSS YLYFLFCPTL IYRETYPRTP YVRWNYVAKN
FAQALGCVLY ACFILGRLCV PVFANMSREP FSTRALVLSI LHATLPGIFM LLLIFFAFLH
CWLNAFAEML RFGDRMFYRD WWNSTSFSNY YRTWNVVVHD WLYSYVYQDG LRLLGARARG
VAMLGVFLVS AVAHEYIFCF VLGFFYPVML ILFLVIGGML NFMMHDQRTG PAWNVLMWTM
LFLGQGIQVS LYCQEWYARR HCPLPQATFW GLVTPRSWSC HT


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EIAAB39178 ACACT,ACACT1,ACAT,ACAT1,ACAT-1,Acyl-coenzyme A cholesterol acyltransferase 1,Cholesterol acyltransferase 1,Homo sapiens,Human,SOAT,SOAT1,STAT,Sterol O-acyltransferase 1
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EIAAB39182 Acat2,ACAT-2,Acyl-coenzyme A cholesterol acyltransferase 2,Cholesterol acyltransferase 2,Rat,Rattus norvegicus,Soat2,Sterol O-acyltransferase 2
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E2114Rb ELISA LCAT,Lecithin-cholesterol acyltransferase,Oryctolagus cuniculus,Phosphatidylcholine-sterol acyltransferase,Phospholipid-cholesterol acyltransferase,Rabbit 96T
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E2114h ELISA Homo sapiens,Human,LCAT,Lecithin-cholesterol acyltransferase,Phosphatidylcholine-sterol acyltransferase,Phospholipid-cholesterol acyltransferase 96T
U2114r CLIA kit Lcat,Lecithin-cholesterol acyltransferase,Phosphatidylcholine-sterol acyltransferase,Phospholipid-cholesterol acyltransferase,Rat,Rattus norvegicus 96T
U2114m CLIA kit Lcat,Lecithin-cholesterol acyltransferase,Mouse,Mus musculus,Phosphatidylcholine-sterol acyltransferase,Phospholipid-cholesterol acyltransferase 96T
E2114r ELISA kit Lcat,Lecithin-cholesterol acyltransferase,Phosphatidylcholine-sterol acyltransferase,Phospholipid-cholesterol acyltransferase,Rat,Rattus norvegicus 96T
E2114r ELISA Lcat,Lecithin-cholesterol acyltransferase,Phosphatidylcholine-sterol acyltransferase,Phospholipid-cholesterol acyltransferase,Rat,Rattus norvegicus 96T
U2114m CLIA Lcat,Lecithin-cholesterol acyltransferase,Mouse,Mus musculus,Phosphatidylcholine-sterol acyltransferase,Phospholipid-cholesterol acyltransferase 96T
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Pathways :
WP1668: Lipopolysaccharide biosynthesis
WP1614: 1- and 2-Methylnaphthalene degradation
WP627: Triacylglycerol Biosynthesis
WP1657: Glycerolipid metabolism
WP1714: Tyrosine metabolism
WP1665: Limonene and pinene degradation
WP1686: Phenylalanine metabolism
WP1626: Benzoate degradation via CoA ligation
WP1646: Ethylbenzene degradation
WP1658: Glycerophospholipid metabolism
WP833: Cholesterol Biosynthesis
WP103: Cholesterol Biosynthesis
WP132: Cholesterol Biosynthesis
WP1795: Cholesterol biosynthesis
WP2084: SREBF and miR33 in cholesterol and lipid homeostasis
WP1634: Butanoate metabolism
WP461: Cholesterol Biosynthesis
WP1666: Linoleic acid metabolism
WP1186: Cholesterol Biosynthesis
WP2011: SREBF and miR33 in cholesterol and lipid homeostasis
WP1633: Bisphenol A degradation
WP1652: Fructose and mannose metabolism
WP659: Cholesterol metabolism
WP1070: Cholesterol Biosynthesis
WP952: Cholesterol Biosynthesis

Related Genes :
[SOAT2 ACACT2 ACAT2] Sterol O-acyltransferase 2 (EC 2.3.1.26) (Acyl-coenzyme A:cholesterol acyltransferase 2) (ACAT-2) (Cholesterol acyltransferase 2)
[SOAT1 ACACT ACACT1 ACAT ACAT1 SOAT STAT] Sterol O-acyltransferase 1 (EC 2.3.1.26) (Acyl-coenzyme A:cholesterol acyltransferase 1) (ACAT-1) (Cholesterol acyltransferase 1)
[Soat2 Acat2] Sterol O-acyltransferase 2 (EC 2.3.1.26) (Acyl-coenzyme A:cholesterol acyltransferase 2) (ACAT-2) (Cholesterol acyltransferase 2)
[Soat2 Acact-2 Acat2] Sterol O-acyltransferase 2 (EC 2.3.1.26) (Acyl-coenzyme A:cholesterol acyltransferase 2) (ACAT-2) (Cholesterol acyltransferase 2)
[Soat1 Acact Acat] Sterol O-acyltransferase 1 (EC 2.3.1.26) (Acyl-coenzyme A:cholesterol acyltransferase 1) (ACAT-1) (Cholesterol acyltransferase 1)
[Soat1 Acact] Sterol O-acyltransferase 1 (EC 2.3.1.26) (Acyl-coenzyme A:cholesterol acyltransferase 1) (ACAT-1) (Cholesterol acyltransferase 1)
[SOAT1 ACAT1] Sterol O-acyltransferase 1 (EC 2.3.1.26) (Acyl-coenzyme A:cholesterol acyltransferase 1) (ACAT-1) (Cholesterol acyltransferase 1)
[SOAT1 ACAT ACAT1] Sterol O-acyltransferase 1 (EC 2.3.1.26) (Acyl-coenzyme A:cholesterol acyltransferase 1) (ACAT-1) (Cholesterol acyltransferase 1)
[SOAT2 ACAT2] Sterol O-acyltransferase 2 (EC 2.3.1.26) (Acyl-coenzyme A:cholesterol acyltransferase 2) (ACAT-2) (Cholesterol acyltransferase 2)
[SOAT1 ACAT ACAT1] Sterol O-acyltransferase 1 (EC 2.3.1.26) (Acyl-coenzyme A:cholesterol acyltransferase 1) (ACAT-1) (Cholesterol acyltransferase 1)
[CES1 CES2 SES1] Liver carboxylesterase 1 (Acyl-coenzyme A:cholesterol acyltransferase) (ACAT) (Brain carboxylesterase hBr1) (Carboxylesterase 1) (CE-1) (hCE-1) (EC 3.1.1.1) (Cholesteryl ester hydrolase) (CEH) (EC 3.1.1.13) (Cocaine carboxylesterase) (Egasyn) (HMSE) (Methylumbelliferyl-acetate deacetylase 1) (EC 3.1.1.56) (Monocyte/macrophage serine esterase) (Retinyl ester hydrolase) (REH) (Serine esterase 1) (Triacylglycerol hydrolase) (TGH)
[LCAT] Phosphatidylcholine-sterol acyltransferase (EC 2.3.1.43) (1-alkyl-2-acetylglycerophosphocholine esterase) (EC 3.1.1.47) (Lecithin-cholesterol acyltransferase) (Phospholipid-cholesterol acyltransferase) (Platelet-activating factor acetylhydrolase) (PAF acetylhydrolase)
[DGAT1 AGRP1 DGAT] Diacylglycerol O-acyltransferase 1 (EC 2.3.1.20) (ACAT-related gene product 1) (Acyl-CoA retinol O-fatty-acyltransferase) (ARAT) (Retinol O-fatty-acyltransferase) (EC 2.3.1.76) (Diglyceride acyltransferase)
[Lcat] Phosphatidylcholine-sterol acyltransferase (EC 2.3.1.43) (1-alkyl-2-acetylglycerophosphocholine esterase) (EC 3.1.1.47) (Lecithin-cholesterol acyltransferase) (Phospholipid-cholesterol acyltransferase) (Platelet-activating factor acetylhydrolase) (PAF acetylhydrolase)
[Lcat] Phosphatidylcholine-sterol acyltransferase (EC 2.3.1.43) (1-alkyl-2-acetylglycerophosphocholine esterase) (EC 3.1.1.47) (Lecithin-cholesterol acyltransferase) (Phospholipid-cholesterol acyltransferase) (Platelet-activating factor acetylhydrolase) (PAF acetylhydrolase)
[LCAT] Phosphatidylcholine-sterol acyltransferase (EC 2.3.1.43) (1-alkyl-2-acetylglycerophosphocholine esterase) (EC 3.1.1.47) (Lecithin-cholesterol acyltransferase) (Phospholipid-cholesterol acyltransferase) (Platelet-activating factor acetylhydrolase) (PAF acetylhydrolase) (Fragments)
[LCAT] Phosphatidylcholine-sterol acyltransferase (EC 2.3.1.43) (1-alkyl-2-acetylglycerophosphocholine esterase) (EC 3.1.1.47) (Lecithin-cholesterol acyltransferase) (Phospholipid-cholesterol acyltransferase) (Platelet-activating factor acetylhydrolase) (PAF acetylhydrolase)
[PSAT LCAT2 PSAT1 At1g04010 F21M11.5] Phospholipid--sterol O-acyltransferase (EC 2.3.1.-) (Lecithin-cholesterol acyltransferase-like 2)
[mboa-2 CELE_H19N07.4 H19N07.4] Acyl-CoA retinol O-fatty-acyltransferase (EC 2.3.1.20) (EC 2.3.1.76) (Diacylglycerol O-acyltransferase 1) (Diglyceride acyltransferase)
[Dgat1 CSKR_8129s] Acyl-CoA retinol O-fatty-acyltransferase (EC 2.3.1.20) (EC 2.3.1.76) (Diacylglycerol O-acyltransferase 1) (Diglyceride acyltransferase) (Fragment)
[Mboat2 Lpcat4 Oact2] Lysophospholipid acyltransferase 2 (LPLAT 2) (EC 2.3.1.-) (1-acylglycerophosphocholine O-acyltransferase) (EC 2.3.1.23) (1-acylglycerophosphoethanolamine O-acyltransferase) (EC 2.3.1.n7) (Lysophosphatidylcholine acyltransferase) (LPCAT) (Lyso-PC acyltransferase) (Lysophosphatidylcholine acyltransferase 4) (Lyso-PC acyltransferase 4) (mLPCAT4) (Lysophosphatidylethanolamine acyltransferase) (LPEAT) (Lyso-PE acyltransferase) (Membrane-bound O-acyltransferase domain-containing protein 2) (O-acyltransferase domain-containing protein 2)
[Lpcat1 Aytl2] Lysophosphatidylcholine acyltransferase 1 (LPC acyltransferase 1) (LPCAT-1) (LysoPC acyltransferase 1) (mLPCAT1) (EC 2.3.1.23) (1-acylglycerol-3-phosphate O-acyltransferase) (EC 2.3.1.51) (1-acylglycerophosphocholine O-acyltransferase) (1-alkenylglycerophosphocholine O-acyltransferase) (EC 2.3.1.25) (1-alkylglycerophosphocholine O-acetyltransferase) (EC 2.3.1.67) (Acetyl-CoA:lyso-platelet-activating factor acetyltransferase) (Acetyl-CoA:lyso-PAF acetyltransferase) (Lyso-PAF acetyltransferase) (LysoPAFAT) (Acyltransferase-like 2)
[Dyak\GE12771 Dyak_GE12771] Acyl-CoA retinol O-fatty-acyltransferase (EC 2.3.1.20) (EC 2.3.1.76) (Diacylglycerol O-acyltransferase 1) (Diglyceride acyltransferase)
[mboa-6 R155.1] Lysophospholipid acyltransferase 5 (LPLAT 5) (EC 2.3.1.-) (Probable 1-acylglycerophosphocholine O-acyltransferase) (EC 2.3.1.23) (Probable 1-acylglycerophosphoethanolamine O-acyltransferase) (EC 2.3.1.n7) (Probable 1-acylglycerophosphoserine O-acyltransferase) (EC 2.3.1.n6) (Probable lysophosphatidylcholine acyltransferase) (LPCAT) (Lyso-PC acyltransferase) (Probable lysophosphatidylethanolamine acyltransferase) (LPEAT) (Lyso-PE acyltransferase) (Probable lysophosphatidylserine acyltransferase) (LPSAT) (Lyso-PS acyltransferase)
[Lpcat3 Grcc3f Mboat5 Oact5] Lysophospholipid acyltransferase 5 (LPLAT 5) (EC 2.3.1.-) (1-acylglycerophosphocholine O-acyltransferase) (EC 2.3.1.23) (1-acylglycerophosphoethanolamine O-acyltransferase) (EC 2.3.1.n7) (1-acylglycerophosphoserine O-acyltransferase) (EC 2.3.1.n6) (Lysophosphatidylcholine acyltransferase) (LPCAT) (Lyso-PC acyltransferase) (Lysophosphatidylcholine acyltransferase 3) (Lyso-PC acyltransferase 3) (mLPCAT3) (Lysophosphatidylethanolamine acyltransferase) (LPEAT) (Lyso-PE acyltransferase) (Lysophosphatidylserine acyltransferase) (LPSAT) (Lyso-PS acyltransferase) (Membrane-bound O-acyltransferase domain-containing protein 5) (O-acyltransferase domain-containing protein 5)
[Gpat4 Agpat6 Tsarg7] Glycerol-3-phosphate acyltransferase 4 (GPAT4) (EC 2.3.1.15) (1-acylglycerol-3-phosphate O-acyltransferase 6) (1-AGP acyltransferase 6) (1-AGPAT 6) (Acyl-CoA:glycerol-3-phosphate acyltransferase 4) (Lysophosphatidic acid acyltransferase zeta) (LPAAT-zeta) (Testis spermatogenesis apoptosis-related protein 7)
[Agpat5 D8Ertd319e] 1-acyl-sn-glycerol-3-phosphate acyltransferase epsilon (EC 2.3.1.51) (1-acylglycerol-3-phosphate O-acyltransferase 5) (1-AGP acyltransferase 5) (1-AGPAT 5) (Lysophosphatidic acid acyltransferase epsilon) (LPAAT-epsilon)
[LPCAT3 MBOAT5 OACT5] Lysophospholipid acyltransferase 5 (LPLAT 5) (EC 2.3.1.-) (1-acylglycerophosphocholine O-acyltransferase) (EC 2.3.1.23) (1-acylglycerophosphoethanolamine O-acyltransferase) (EC 2.3.1.n7) (1-acylglycerophosphoserine O-acyltransferase) (EC 2.3.1.n6) (Lysophosphatidylcholine acyltransferase) (LPCAT) (Lyso-PC acyltransferase) (Lysophosphatidylcholine acyltransferase 3) (Lyso-PC acyltransferase 3) (Lysophosphatidylserine acyltransferase) (LPSAT) (Lyso-PS acyltransferase) (Membrane-bound O-acyltransferase domain-containing protein 5) (O-acyltransferase domain-containing protein 5)
[Ces1 Ces1g] Liver carboxylesterase 1 (EC 3.1.1.1) (Acyl-coenzyme A:cholesterol acyltransferase) (Carboxylesterase 1G) (Cholesteryl ester hydrolase) (CEH) (EC 3.1.1.13) (ES-x)
[mboa-7 lpiat tag-289 F14F3.3] Lysophospholipid acyltransferase 7 (LPLAT 7) (EC 2.3.1.-) (1-acylglycerophosphatidylinositol O-acyltransferase) (EC 2.3.1.n4) (Lysophosphatidylinositol acyltransferase) (LPIAT) (Lyso-PI acyltransferase) (Membrane-bound O-acyltransferase domain-containing protein 7)

Bibliography :
[27329301] Identification of potential ACAT-2 selective inhibitors using pharmacophore, SVM and SVR from Chinese herbs.
[23124952] Using self-organizing map (SOM) and support vector machine (SVM) for classification of selectivity of ACAT inhibitors.
[21232182] Regulation of acyl-coenzyme A: cholesterol acyltransferase 2 expression by saturated fatty acids.
[19495703] A novel technical approach for the measurement of individual ACAT-1 and ACAT-2 enzymatic activity in the testis.
[16820149] A selective ACAT-1 inhibitor, K-604, suppresses fatty streak lesions in fat-fed hamsters without affecting plasma cholesterol levels.
[16042405] Acyl-coenzyme A binding protein expression alters liver fatty acyl-coenzyme A metabolism.
[15458444] HMG-CoA reductase, cholesterol 7alpha-hydroxylase, LDL receptor, SR-B1, and ACAT in diet-induced syndrome X.
[15262831] Acyl-coenzyme A:cholesterol acyltransferase inhibition ameliorates proteinuria, hyperlipidemia, lecithin-cholesterol acyltransferase, SRB-1, and low-denisty lipoprotein receptor deficiencies in nephrotic syndrome.
[15242859] Acyl-coenzyme A:cholesterol acyltransferase-2 (ACAT-2) is responsible for elevated intestinal ACAT activity in diabetic rats.
[12621162] Effects of a new single-nucleotide polymorphism in the Acyl-CoA:cholesterol acyltransferase-2 gene on plasma lipids and apolipoproteins in patients with hyperlipidemia.