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Sterol O-acyltransferase 1 (EC 2.3.1.26) (Acyl-coenzyme A:cholesterol acyltransferase 1) (ACAT-1) (Cholesterol acyltransferase 1)

 SOAT1_HUMAN             Reviewed;         550 AA.
P35610; A6NC40; A8K3P4; A9Z1V7; B4DU95; Q5T0X4; Q8N1E4;
01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
25-JUL-2003, sequence version 3.
11-DEC-2019, entry version 188.
RecName: Full=Sterol O-acyltransferase 1;
EC=2.3.1.26 {ECO:0000269|PubMed:18480028};
AltName: Full=Acyl-coenzyme A:cholesterol acyltransferase 1;
Short=ACAT-1;
AltName: Full=Cholesterol acyltransferase 1;
Name=SOAT1; Synonyms=ACACT, ACACT1, ACAT, ACAT1, SOAT, STAT;
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), AND VARIANT ARG-526.
TISSUE=Macrophage;
PubMed=8407899;
Chang C.C.Y., Huh H.Y., Cadigan K.M., Chang T.-Y.;
"Molecular cloning and functional expression of human acyl-coenzyme
A:cholesterol acyltransferase cDNA in mutant Chinese hamster ovary cells.";
J. Biol. Chem. 268:20747-20755(1993).
[2]
SEQUENCE REVISION TO 207.
Chang C.C.Y., Chang T.-Y.;
Submitted (MAY-1999) to UniProtKB.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
Hunkapiller M.W., Myers E.W., Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Placenta;
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]
PRELIMINARY TOPOLOGY.
PubMed=10438503; DOI=10.1074/jbc.274.33.23276;
Lin S., Cheng D., Liu M.S., Chen J., Chang T.-Y.;
"Human acyl-CoA:cholesterol acyltransferase-1 in the endoplasmic reticulum
contains seven transmembrane domains.";
J. Biol. Chem. 274:23276-23285(1999).
[8]
SUBCELLULAR LOCATION, TOPOLOGY, ACTIVE SITE, DISULFIDE BOND, AND
MUTAGENESIS OF SER-269 AND HIS-460.
PubMed=16154994; DOI=10.1074/jbc.m508384200;
Guo Z.Y., Lin S., Heinen J.A., Chang C.C., Chang T.Y.;
"The active site His-460 of human acyl-coenzyme A:cholesterol
acyltransferase 1 resides in a hitherto undisclosed transmembrane domain.";
J. Biol. Chem. 280:37814-37826(2005).
[9]
CATALYTIC ACTIVITY, ACTIVE SITE, AND MUTAGENESIS OF ASP-400; SER-456;
HIS-460 AND TYR-518.
PubMed=18480028; DOI=10.1194/jlr.m800131-jlr200;
Das A., Davis M.A., Rudel L.L.;
"Identification of putative active site residues of ACAT enzymes.";
J. Lipid Res. 49:1770-1781(2008).
[10]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-terminal
acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[11]
INTERACTION WITH UBIAD1.
PubMed=23169578; DOI=10.1002/humu.22230;
Nickerson M.L., Bosley A.D., Weiss J.S., Kostiha B.N., Hirota Y.,
Brandt W., Esposito D., Kinoshita S., Wessjohann L., Morham S.G.,
Andresson T., Kruth H.S., Okano T., Dean M.;
"The UBIAD1 prenyltransferase links menaquione-4 synthesis to cholesterol
metabolic enzymes.";
Hum. Mutat. 34:317-329(2013).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-8, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
-!- 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. In addition to
its acyltransferase activity, it may act as a ligase.
-!- 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:0000269|PubMed:18480028};
-!- SUBUNIT: May form homo- or heterodimers. Interacts with UBIAD1.
{ECO:0000269|PubMed:23169578}.
-!- INTERACTION:
P54274:TERF1; NbExp=2; IntAct=EBI-6621955, EBI-710997;
Q9Y5Z9:UBIAD1; NbExp=3; IntAct=EBI-6621997, EBI-2819725;
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
{ECO:0000269|PubMed:16154994}; Multi-pass membrane protein
{ECO:0000269|PubMed:16154994}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=P35610-1; Sequence=Displayed;
Name=2;
IsoId=P35610-2; Sequence=VSP_045331;
Name=3;
IsoId=P35610-3; Sequence=VSP_045330;
-!- INDUCTION: Highly activated by the presence of cholesterol.
-!- SIMILARITY: Belongs to the membrane-bound acyltransferase family.
Sterol o-acyltransferase subfamily. {ECO:0000305}.
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EMBL; L21934; AAC37532.2; -; mRNA.
EMBL; AK290659; BAF83348.1; -; mRNA.
EMBL; AK300551; BAG62257.1; -; mRNA.
EMBL; AL451075; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL512326; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471067; EAW91043.1; -; Genomic_DNA.
EMBL; CH471067; EAW91044.1; -; Genomic_DNA.
EMBL; BC028940; AAH28940.1; -; mRNA.
CCDS; CCDS1330.1; -. [P35610-1]
CCDS; CCDS58047.1; -. [P35610-2]
CCDS; CCDS58048.1; -. [P35610-3]
PIR; A59038; A48026.
RefSeq; NP_001239440.1; NM_001252511.1. [P35610-2]
RefSeq; NP_001239441.1; NM_001252512.1. [P35610-3]
RefSeq; NP_003092.4; NM_003101.5. [P35610-1]
RefSeq; XP_011508213.1; XM_011509911.1. [P35610-1]
BioGrid; 112529; 189.
IntAct; P35610; 172.
MINT; P35610; -.
STRING; 9606.ENSP00000356591; -.
BindingDB; P35610; -.
ChEMBL; CHEMBL2782; -.
DrugBank; DB00973; Ezetimibe.
DrugBank; DB01094; Hesperetin.
DrugBank; DB09539; Omega-3-acid ethyl esters.
DrugCentral; P35610; -.
SwissLipids; SLP:000000702; -.
iPTMnet; P35610; -.
PhosphoSitePlus; P35610; -.
SwissPalm; P35610; -.
BioMuta; SOAT1; -.
DMDM; 33302623; -.
EPD; P35610; -.
jPOST; P35610; -.
MassIVE; P35610; -.
MaxQB; P35610; -.
PaxDb; P35610; -.
PeptideAtlas; P35610; -.
PRIDE; P35610; -.
ProteomicsDB; 1856; -.
ProteomicsDB; 5164; -.
ProteomicsDB; 55101; -. [P35610-1]
DNASU; 6646; -.
Ensembl; ENST00000367619; ENSP00000356591; ENSG00000057252. [P35610-1]
Ensembl; ENST00000539888; ENSP00000441356; ENSG00000057252. [P35610-3]
Ensembl; ENST00000540564; ENSP00000445315; ENSG00000057252. [P35610-2]
GeneID; 6646; -.
KEGG; hsa:6646; -.
UCSC; uc001gml.4; human. [P35610-1]
CTD; 6646; -.
DisGeNET; 6646; -.
EuPathDB; HostDB:ENSG00000057252.12; -.
GeneCards; SOAT1; -.
HGNC; HGNC:11177; SOAT1.
HPA; CAB009533; -.
HPA; HPA047171; -.
MIM; 102642; gene.
neXtProt; NX_P35610; -.
OpenTargets; ENSG00000057252; -.
PharmGKB; PA36015; -.
eggNOG; KOG0380; Eukaryota.
eggNOG; COG5056; LUCA.
GeneTree; ENSGT00950000183081; -.
HOGENOM; HOG000020782; -.
InParanoid; P35610; -.
KO; K00637; -.
OMA; IMWTSLF; -.
OrthoDB; 1275897at2759; -.
PhylomeDB; P35610; -.
TreeFam; TF105767; -.
BRENDA; 2.3.1.26; 2681.
Reactome; R-HSA-8964038; LDL clearance.
SABIO-RK; P35610; -.
SIGNOR; P35610; -.
ChiTaRS; SOAT1; human.
GeneWiki; SOAT1; -.
GenomeRNAi; 6646; -.
Pharos; P35610; Tchem.
PRO; PR:P35610; -.
Proteomes; UP000005640; Chromosome 1.
RNAct; P35610; protein.
Bgee; ENSG00000057252; Expressed in 209 organ(s), highest expression level in adrenal tissue.
ExpressionAtlas; P35610; baseline and differential.
Genevisible; P35610; HS.
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:0016020; C:membrane; IDA:MGI.
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:0004772; F:sterol O-acyltransferase activity; IDA:MGI.
GO; GO:0033344; P:cholesterol efflux; IMP:BHF-UCL.
GO; GO:0034435; P:cholesterol esterification; IDA:BHF-UCL.
GO; GO:0042632; P:cholesterol homeostasis; TAS:BHF-UCL.
GO; GO:0008203; P:cholesterol metabolic process; IDA:BHF-UCL.
GO; GO:0010878; P:cholesterol storage; IMP:BHF-UCL.
GO; GO:0034383; P:low-density lipoprotein particle clearance; TAS:Reactome.
GO; GO:0010742; P:macrophage derived foam cell differentiation; IMP:BHF-UCL.
GO; GO:0042986; P:positive regulation of amyloid precursor protein biosynthetic process; IMP: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;
Acetylation; Acyltransferase; Alternative splicing; Cholesterol metabolism;
Disulfide bond; Endoplasmic reticulum; Lipid metabolism; Membrane;
Phosphoprotein; Polymorphism; Reference proteome; Steroid metabolism;
Sterol metabolism; Transferase; Transmembrane; Transmembrane helix.
CHAIN 1..550
/note="Sterol O-acyltransferase 1"
/id="PRO_0000207640"
TOPO_DOM 1..140
/note="Cytoplasmic"
/evidence="ECO:0000255"
TRANSMEM 141..159
/note="Helical"
/evidence="ECO:0000255"
TOPO_DOM 160..181
/note="Lumenal"
/evidence="ECO:0000255"
TRANSMEM 182..201
/note="Helical"
/evidence="ECO:0000255"
TOPO_DOM 202..224
/note="Cytoplasmic"
/evidence="ECO:0000255"
TRANSMEM 225..243
/note="Helical"
/evidence="ECO:0000255"
TOPO_DOM 244..246
/note="Lumenal"
/evidence="ECO:0000255"
TRANSMEM 247..264
/note="Helical"
/evidence="ECO:0000255"
TOPO_DOM 265..501
/note="Cytoplasmic"
/evidence="ECO:0000255"
TRANSMEM 502..517
/note="Helical"
/evidence="ECO:0000255"
TOPO_DOM 518..550
/note="Lumenal"
/evidence="ECO:0000255"
ACT_SITE 460
/evidence="ECO:0000269|PubMed:16154994"
MOD_RES 1
/note="N-acetylmethionine"
/evidence="ECO:0000244|PubMed:22814378"
MOD_RES 8
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:23186163"
DISULFID 528..546
/evidence="ECO:0000269|PubMed:16154994"
VAR_SEQ 1..65
/note="Missing (in isoform 3)"
/evidence="ECO:0000303|PubMed:14702039"
/id="VSP_045330"
VAR_SEQ 1..59
/note="MVGEEKMSLRNRLSKSRENPEEDEDQRNPAKESLETPSNGRIDIKQLIAKKI
KLTAEAE -> M (in isoform 2)"
/evidence="ECO:0000303|PubMed:14702039"
/id="VSP_045331"
VARIANT 526
/note="Q -> R (in dbSNP:rs13306731)"
/evidence="ECO:0000269|PubMed:8407899"
/id="VAR_052031"
MUTAGEN 269
/note="S->A,T: Nearly normal expression and enzyme
activity."
/evidence="ECO:0000269|PubMed:16154994"
MUTAGEN 269
/note="S->L: No expression nor activity."
/evidence="ECO:0000269|PubMed:16154994"
MUTAGEN 400
/note="D->N: Low expression, loss of enzymatic activity."
/evidence="ECO:0000269|PubMed:18480028"
MUTAGEN 456
/note="S->A: Loss of enzymatic activity."
/evidence="ECO:0000269|PubMed:18480028"
MUTAGEN 460
/note="H->A,C,N: Loss of enzymatic activity."
/evidence="ECO:0000269|PubMed:16154994"
MUTAGEN 518
/note="Y->F: Loss of enzymatic activity."
/evidence="ECO:0000269|PubMed:18480028"
SEQUENCE 550 AA; 64735 MW; 5F5ACD525D541DEE CRC64;
MVGEEKMSLR NRLSKSRENP EEDEDQRNPA KESLETPSNG RIDIKQLIAK KIKLTAEAEE
LKPFFMKEVG SHFDDFVTNL IEKSASLDNG GCALTTFSVL EGEKNNHRAK DLRAPPEQGK
IFIARRSLLD ELLEVDHIRT IYHMFIALLI LFILSTLVVD YIDEGRLVLE FSLLSYAFGK
FPTVVWTWWI MFLSTFSVPY FLFQHWATGY SKSSHPLIRS LFHGFLFMIF QIGVLGFGPT
YVVLAYTLPP ASRFIIIFEQ IRFVMKAHSF VRENVPRVLN SAKEKSSTVP IPTVNQYLYF
LFAPTLIYRD SYPRNPTVRW GYVAMKFAQV FGCFFYVYYI FERLCAPLFR NIKQEPFSAR
VLVLCVFNSI LPGVLILFLT FFAFLHCWLN AFAEMLRFGD RMFYKDWWNS TSYSNYYRTW
NVVVHDWLYY YAYKDFLWFF SKRFKSAAML AVFAVSAVVH EYALAVCLSF FYPVLFVLFM
FFGMAFNFIV NDSRKKPIWN VLMWTSLFLG NGVLLCFYSQ EWYARQHCPL KNPTFLDYVR
PRSWTCRYVF


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U2114Rb CLIA kit LCAT,Lecithin-cholesterol acyltransferase,Oryctolagus cuniculus,Phosphatidylcholine-sterol acyltransferase,Phospholipid-cholesterol acyltransferase,Rabbit 96T
E2114Rb ELISA LCAT,Lecithin-cholesterol acyltransferase,Oryctolagus cuniculus,Phosphatidylcholine-sterol acyltransferase,Phospholipid-cholesterol acyltransferase,Rabbit 96T
U2114h CLIA kit Homo sapiens,Human,LCAT,Lecithin-cholesterol acyltransferase,Phosphatidylcholine-sterol acyltransferase,Phospholipid-cholesterol acyltransferase 96T
U2114Rb CLIA LCAT,Lecithin-cholesterol acyltransferase,Oryctolagus cuniculus,Phosphatidylcholine-sterol acyltransferase,Phospholipid-cholesterol acyltransferase,Rabbit 96T
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
E2114m ELISA Lcat,Lecithin-cholesterol acyltransferase,Mouse,Mus musculus,Phosphatidylcholine-sterol acyltransferase,Phospholipid-cholesterol acyltransferase 96T
U2114r CLIA Lcat,Lecithin-cholesterol acyltransferase,Phosphatidylcholine-sterol acyltransferase,Phospholipid-cholesterol acyltransferase,Rat,Rattus norvegicus 96T
E2114m ELISA kit Lcat,Lecithin-cholesterol acyltransferase,Mouse,Mus musculus,Phosphatidylcholine-sterol acyltransferase,Phospholipid-cholesterol acyltransferase 96T
E2114p ELISA kit LCAT,Lecithin-cholesterol acyltransferase,Phosphatidylcholine-sterol acyltransferase,Phospholipid-cholesterol acyltransferase,Pig,Sus scrofa 96T
U2114p CLIA kit LCAT,Lecithin-cholesterol acyltransferase,Phosphatidylcholine-sterol acyltransferase,Phospholipid-cholesterol acyltransferase,Pig,Sus scrofa 96T
E2114p ELISA LCAT,Lecithin-cholesterol acyltransferase,Phosphatidylcholine-sterol acyltransferase,Phospholipid-cholesterol acyltransferase,Pig,Sus scrofa 96T
Pathways :
WP1668: Lipopolysaccharide biosynthesis
WP1614: 1- and 2-Methylnaphthalene degradation
WP1657: Glycerolipid metabolism
WP627: Triacylglycerol Biosynthesis
WP1714: Tyrosine metabolism
WP1665: Limonene and pinene degradation
WP1686: Phenylalanine metabolism
WP1626: Benzoate degradation via CoA ligation
WP1646: Ethylbenzene degradation
WP1658: Glycerophospholipid metabolism
WP103: Cholesterol Biosynthesis
WP833: Cholesterol Biosynthesis
WP1795: Cholesterol biosynthesis
WP132: Cholesterol Biosynthesis
WP2084: SREBF and miR33 in cholesterol and lipid homeostasis
WP461: Cholesterol Biosynthesis
WP1634: Butanoate metabolism
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 :
[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 ACACT2 ACAT2] Sterol O-acyltransferase 2 (EC 2.3.1.26) (Acyl-coenzyme A:cholesterol acyltransferase 2) (ACAT-2) (Cholesterol acyltransferase 2)
[Soat1 Acact] Sterol O-acyltransferase 1 (EC 2.3.1.26) (Acyl-coenzyme A:cholesterol acyltransferase 1) (ACAT-1) (Cholesterol acyltransferase 1)
[Soat1 Acact Acat] Sterol O-acyltransferase 1 (EC 2.3.1.26) (Acyl-coenzyme A:cholesterol acyltransferase 1) (ACAT-1) (Cholesterol acyltransferase 1)
[Soat2 Acact-2 Acat2] Sterol O-acyltransferase 2 (EC 2.3.1.26) (Acyl-coenzyme A:cholesterol acyltransferase 2) (ACAT-2) (Cholesterol acyltransferase 2)
[Soat2 Acat2] Sterol O-acyltransferase 2 (EC 2.3.1.26) (Acyl-coenzyme A:cholesterol acyltransferase 2) (ACAT-2) (Cholesterol acyltransferase 2)
[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) (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)
[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)
[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)
[LCAT] Phosphatidylcholine-sterol acyltransferase (EC 2.3.1.43) (Lecithin-cholesterol acyltransferase) (Phospholipid-cholesterol acyltransferase)
[PSAT LCAT2 PSAT1 At1g04010 F21M11.5] Phospholipid--sterol O-acyltransferase (EC 2.3.1.-) (Lecithin-cholesterol acyltransferase-like 2)
[Lcat] Phosphatidylcholine-sterol acyltransferase (EC 2.3.1.43) (Lecithin-cholesterol acyltransferase) (Phospholipid-cholesterol acyltransferase)
[Lcat] Phosphatidylcholine-sterol acyltransferase (EC 2.3.1.43) (Lecithin-cholesterol acyltransferase) (Phospholipid-cholesterol acyltransferase)
[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)
[Gpat3 Agpat9] Glycerol-3-phosphate acyltransferase 3 (GPAT-3) (EC 2.3.1.15) (1-acyl-sn-glycerol-3-phosphate O-acyltransferase 10) (AGPAT 10) (1-acyl-sn-glycerol-3-phosphate O-acyltransferase 9) (1-AGP acyltransferase 9) (1-AGPAT 9) (EC 2.3.1.51) (Acyl-CoA:glycerol-3-phosphate acyltransferase 3) (mGPAT3) (Lysophosphatidic acid acyltransferase theta) (LPAAT-theta)
[Dgat1 Dgat] Diacylglycerol O-acyltransferase 1 (EC 2.3.1.20) (Acyl-CoA retinol O-fatty-acyltransferase) (ARAT) (Retinol O-fatty-acyltransferase) (EC 2.3.1.76) (Diglyceride acyltransferase)
[Agpat3 Lpaat3] 1-acyl-sn-glycerol-3-phosphate acyltransferase gamma (EC 2.3.1.51) (1-acylglycerol-3-phosphate O-acyltransferase 3) (1-AGP acyltransferase 3) (1-AGPAT 3) (Lysophosphatidic acid acyltransferase gamma) (LPAAT-gamma)
[Dgat1 Dgat] Diacylglycerol O-acyltransferase 1 (EC 2.3.1.20) (Acyl-CoA retinol O-fatty-acyltransferase) (ARAT) (Retinol O-fatty-acyltransferase) (EC 2.3.1.76) (Diglyceride acyltransferase)
[Ces1 Ces1g] Liver carboxylesterase 1 (EC 3.1.1.1) (Acyl-coenzyme A:cholesterol acyltransferase) (Carboxylesterase 1G) (ES-x)
[tgs1 Rv3130c MTCY03A2.28 MTCY164.41c] Probable diacyglycerol O-acyltransferase tgs1 (TGS1) (EC 2.3.1.20) (Probable triacylglycerol synthase tgs1)
[LCAT] Phosphatidylcholine-sterol acyltransferase (EC 2.3.1.43) (Lecithin-cholesterol acyltransferase) (Phospholipid-cholesterol acyltransferase)
[GPAT3 AGPAT9 MAG1 HMFN0839 UNQ2753/PRO6492] Glycerol-3-phosphate acyltransferase 3 (GPAT-3) (EC 2.3.1.15) (1-acyl-sn-glycerol-3-phosphate O-acyltransferase 10) (AGPAT 10) (1-acyl-sn-glycerol-3-phosphate O-acyltransferase 9) (1-AGP acyltransferase 9) (1-AGPAT 9) (EC 2.3.1.51) (Acyl-CoA:glycerol-3-phosphate acyltransferase 3) (hGPAT3) (Lung cancer metastasis-associated protein 1) (Lysophosphatidic acid acyltransferase theta) (LPAAT-theta) (MAG-1)
[gpat3 agpat9 si:ch211-85e10.5 zgc:91857] Glycerol-3-phosphate acyltransferase 3 (GPAT-3) (EC 2.3.1.15) (1-acyl-sn-glycerol-3-phosphate O-acyltransferase 10) (AGPAT 10) (1-acyl-sn-glycerol-3-phosphate O-acyltransferase 9) (1-AGP acyltransferase 9) (1-AGPAT 9) (EC 2.3.1.51) (Lysophosphatidic acid acyltransferase theta) (LPAAT-theta)
[Gpat3 Agpat9] Glycerol-3-phosphate acyltransferase 3 (GPAT-3) (EC 2.3.1.15) (1-acyl-sn-glycerol-3-phosphate O-acyltransferase 10) (AGPAT 10) (1-acyl-sn-glycerol-3-phosphate O-acyltransferase 9) (1-AGP acyltransferase 9) (1-AGPAT 9) (EC 2.3.1.51) (Lysophosphatidic acid acyltransferase theta) (LPAAT-theta)
[GPAT3 AGPAT9 RCJMB04_5j9] Glycerol-3-phosphate acyltransferase 3 (GPAT-3) (EC 2.3.1.15) (1-acyl-sn-glycerol-3-phosphate O-acyltransferase 10) (AGPAT 10) (1-acyl-sn-glycerol-3-phosphate O-acyltransferase 9) (1-AGP acyltransferase 9) (1-AGPAT 9) (EC 2.3.1.51) (Lysophosphatidic acid acyltransferase theta) (LPAAT-theta)
[gpat3 agpat9] Glycerol-3-phosphate acyltransferase 3 (GPAT-3) (EC 2.3.1.15) (1-acyl-sn-glycerol-3-phosphate O-acyltransferase 10) (AGPAT 10) (1-acyl-sn-glycerol-3-phosphate O-acyltransferase 9) (1-AGP acyltransferase 9) (1-AGPAT 9) (EC 2.3.1.51) (Lysophosphatidic acid acyltransferase theta) (LPAAT-theta)
[GLYAT ACGNAT CAT GAT] Glycine N-acyltransferase (EC 2.3.1.13) (Acyl-CoA:glycine N-acyltransferase) (AAc) (Aralkyl acyl-CoA N-acyltransferase) (Aralkyl acyl-CoA:amino acid N-acyltransferase) (Benzoyl-coenzyme A:glycine N-acyltransferase) (Glycine N-benzoyltransferase) (EC 2.3.1.71) (HRP-1(CLP))
[DGA1 YOR245C] Diacylglycerol O-acyltransferase 1 (DGAT) (EC 2.3.1.20) (Acyl-CoA:monoacylglycerol acyltransferase) (MGAT) (EC 2.3.1.22)

Bibliography :
[23124952] Using self-organizing map (SOM) and support vector machine (SVM) for classification of selectivity of ACAT inhibitors.
[19495703] A novel technical approach for the measurement of individual ACAT-1 and ACAT-2 enzymatic activity in the testis.
[18212280] Impact of salusin-alpha and -beta on human macrophage foam cell formation and coronary atherosclerosis.
[17497288] Effect of tumor necrosis factor-alpha on acyl coenzyme A: cholesteryl acyltransferase activity and ACAT1 gene expression in THP-1 macrophages.
[17412327] Knockdown of ACAT-1 reduces amyloidogenic processing of APP.
[16820149] A selective ACAT-1 inhibitor, K-604, suppresses fatty streak lesions in fat-fed hamsters without affecting plasma cholesterol levels.
[16172428] Human urotensin II accelerates foam cell formation in human monocyte-derived macrophages.
[16157345] Serotonin acts as an up-regulator of acyl-coenzyme A:cholesterol acyltransferase-1 in human monocyte-macrophages.
[16081263] Expression levels of ACAT1 and ACAT2 genes in the liver and intestine of baboons with high and low lipemic responses to dietary lipids.