Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

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

 SOAT1_MOUSE             Reviewed;         540 AA.
Q61263; Q5XK32; Q64180;
18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
27-JUL-2011, sequence version 2.
28-FEB-2018, entry version 133.
RecName: Full=Sterol O-acyltransferase 1;
EC=2.3.1.26 {ECO:0000250|UniProtKB:P35610};
AltName: Full=Acyl-coenzyme A:cholesterol acyltransferase 1;
Short=ACAT-1;
AltName: Full=Cholesterol acyltransferase 1;
Name=Soat1; Synonyms=Acact;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Liver;
PubMed=7592824; DOI=10.1074/jbc.270.44.26192;
Uelmen P.J., Oka K., Sullivan M.C., Chang T.-Y., Chang C.C.Y.,
Chan L.;
"Tissue-specific expression and cholesterol regulation of acylcoenzyme
A:cholesterol acyltransferase (ACAT) in mice. Molecular cloning of
mouse ACAT cDNA, chromosomal localization, and regulation of ACAT in
vivo and in vitro.";
J. Biol. Chem. 270:26192-26201(1995).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=8579615; DOI=10.1006/bbrc.1996.0163;
Green S., Steinberg D., Quehenberger O.;
"Cloning and expression in Xenopus oocytes of a mouse homologue of the
human acylcoenzyme A: cholesterol acyltransferase and its potential
role in metabolism of oxidized LDL.";
Biochem. Biophys. Res. Commun. 218:924-929(1996).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Stomach;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Embryo;
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).
[5]
TOPOLOGY, AND SUBCELLULAR LOCATION.
PubMed=11071899; DOI=10.1091/mbc.11.11.3675;
Joyce C.W., Shelness G.S., Davis M.A., Lee R.G., Skinner K.,
Anderson R.A., Rudel L.L.;
"ACAT1 and ACAT2 membrane topology segregates a serine residue
essential for activity to opposite sides of the endoplasmic reticulum
membrane.";
Mol. Biol. Cell 11:3675-3687(2000).
[6]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Lung, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- 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.
-!- CATALYTIC ACTIVITY: Acyl-CoA + cholesterol = CoA + cholesterol
ester. {ECO:0000250|UniProtKB:P35610}.
-!- SUBUNIT: May form homo- or heterodimers. Interacts with UBIAD1.
{ECO:0000250|UniProtKB:P35610}.
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass
membrane protein {ECO:0000269|PubMed:11071899}.
-!- SIMILARITY: Belongs to the membrane-bound acyltransferase family.
Sterol o-acyltransferase subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; L42293; AAC42075.1; -; mRNA.
EMBL; S81092; AAB36050.1; -; mRNA.
EMBL; AK142486; BAE25081.1; -; mRNA.
EMBL; AK159393; BAE35047.1; -; mRNA.
EMBL; AK159529; BAE35158.1; -; mRNA.
EMBL; AK160017; BAE35563.1; -; mRNA.
EMBL; BC083092; AAH83092.1; -; mRNA.
CCDS; CCDS35743.1; -.
PIR; I49454; I49454.
RefSeq; NP_033256.2; NM_009230.3.
UniGene; Mm.28099; -.
BioGrid; 203385; 1.
IntAct; Q61263; 2.
MINT; Q61263; -.
STRING; 10090.ENSMUSP00000058344; -.
BindingDB; Q61263; -.
ChEMBL; CHEMBL4464; -.
iPTMnet; Q61263; -.
PhosphoSitePlus; Q61263; -.
SwissPalm; Q61263; -.
EPD; Q61263; -.
MaxQB; Q61263; -.
PaxDb; Q61263; -.
PRIDE; Q61263; -.
Ensembl; ENSMUST00000051396; ENSMUSP00000058344; ENSMUSG00000026600.
Ensembl; ENSMUST00000189661; ENSMUSP00000140721; ENSMUSG00000026600.
GeneID; 20652; -.
KEGG; mmu:20652; -.
UCSC; uc007dcj.1; mouse.
CTD; 6646; -.
MGI; MGI:104665; Soat1.
eggNOG; KOG0380; Eukaryota.
eggNOG; COG5056; LUCA.
GeneTree; ENSGT00530000063122; -.
HOGENOM; HOG000020782; -.
HOVERGEN; HBG058198; -.
InParanoid; Q61263; -.
KO; K00637; -.
OMA; LFMCFGM; -.
OrthoDB; EOG091G0991; -.
TreeFam; TF105767; -.
BRENDA; 2.3.1.26; 3474.
Reactome; R-MMU-8964038; LDL clearance.
ChiTaRS; Soat1; mouse.
PRO; PR:Q61263; -.
Proteomes; UP000000589; Chromosome 1.
Bgee; ENSMUSG00000026600; -.
CleanEx; MM_SOAT1; -.
ExpressionAtlas; Q61263; baseline and differential.
Genevisible; Q61263; MM.
GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
GO; GO:0005789; C:endoplasmic reticulum membrane; ISO:MGI.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0016020; C:membrane; ISO:MGI.
GO; GO:0015485; F:cholesterol binding; ISO:MGI.
GO; GO:0034736; F:cholesterol O-acyltransferase activity; ISO:MGI.
GO; GO:0000062; F:fatty-acyl-CoA binding; ISO:MGI.
GO; GO:0004772; F:sterol O-acyltransferase activity; IDA:MGI.
GO; GO:0033344; P:cholesterol efflux; ISO:MGI.
GO; GO:0034435; P:cholesterol esterification; ISO:MGI.
GO; GO:0042632; P:cholesterol homeostasis; IEA:InterPro.
GO; GO:0008203; P:cholesterol metabolic process; IDA:MGI.
GO; GO:0010878; P:cholesterol storage; ISO:MGI.
GO; GO:0010742; P:macrophage derived foam cell differentiation; ISO:MGI.
GO; GO:0042986; P:positive regulation of amyloid precursor protein biosynthetic process; ISO:MGI.
GO; GO:0034379; P:very-low-density lipoprotein particle assembly; ISO:MGI.
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; Cholesterol metabolism; Complete proteome;
Disulfide bond; Endoplasmic reticulum; Lipid metabolism; Membrane;
Phosphoprotein; Reference proteome; Steroid metabolism;
Sterol metabolism; Transferase; Transmembrane; Transmembrane helix.
CHAIN 1 540 Sterol O-acyltransferase 1.
/FTId=PRO_0000207642.
TOPO_DOM 1 140 Cytoplasmic. {ECO:0000255}.
TRANSMEM 141 159 Helical. {ECO:0000255}.
TOPO_DOM 160 181 Lumenal. {ECO:0000255}.
TRANSMEM 182 199 Helical. {ECO:0000255}.
TOPO_DOM 200 224 Cytoplasmic. {ECO:0000255}.
TRANSMEM 225 243 Helical. {ECO:0000255}.
TOPO_DOM 244 246 Lumenal. {ECO:0000255}.
TRANSMEM 247 264 Helical. {ECO:0000255}.
TOPO_DOM 265 501 Cytoplasmic. {ECO:0000255}.
TRANSMEM 502 517 Helical. {ECO:0000255}.
TOPO_DOM 518 540 Lumenal. {ECO:0000255}.
ACT_SITE 450 450 {ECO:0000250}.
MOD_RES 2 2 Phosphoserine.
{ECO:0000250|UniProtKB:P35610}.
DISULFID 518 536 {ECO:0000250}.
CONFLICT 195 195 R -> P (in Ref. 1; AAC42075).
{ECO:0000305}.
SEQUENCE 540 AA; 63799 MW; F2A6C91774762E23 CRC64;
MSLRNRLSKS GENPEQDEAQ KNFMDTYRNG HITMKQLIAK KRLLAAEAEE LKPLFMKEVG
CHFDDFVTNL IEKSASLDNG GCALTTFSIL EEMKKNHRAK DLRAPPEQGK IFISRQSLLD
ELFEVDHIRT IYHMFIALLI LFVLSTIVVD YIDEGRLVLE FNLLAYAFGK FPTVIWTWWA
MFLSTLSIPY FLFQRWAHGY SKSSHPLIYS LVHGLLFLVF QLGVLGFVPT YVVLAYTLPP
ASRFILILEQ IRLIMKAHSF VRENIPRVLN AAKEKSSKDP LPTVNQYLYF LFAPTLIYRD
NYPRTPTVRW GYVAMQFLQV FGCLFYVYYI FERLCAPLFR NIKQEPFSAR VLVLCVFNSI
LPGVLILFLS FFAFLHCWLN AFAEMLRFGD RMFYKDWWNS TSYSNYYRTW NVVVHDWLYY
YVYKDLLWFF SKRFKSAAML AVFALSAVVH EYALAICLSY FYPVLFVLFM FFGMAFNFIV
NDSRKRPIWN IMVWASLFLG YGLILCFYSQ EWYARQHCPL KNPTFLDYVR PRTWTCRYVF


Related products :

Catalog number Product name Quantity
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
EIAAB39179 Acact,Acat,ACAT-1,Acyl-coenzyme A cholesterol acyltransferase 1,Cholesterol acyltransferase 1,Rat,Rattus norvegicus,Soat1,Sterol O-acyltransferase 1
EIAAB39180 Acact-2,Acat2,ACAT-2,Acyl-coenzyme A cholesterol acyltransferase 2,Cholesterol acyltransferase 2,Mouse,Mus musculus,Soat2,Sterol O-acyltransferase 2
EIAAB39181 ACACT2,ACAT2,ACAT-2,Acyl-coenzyme A cholesterol acyltransferase 2,Cholesterol acyltransferase 2,Homo sapiens,Human,SOAT2,Sterol O-acyltransferase 2
EIAAB39177 Acact,ACAT-1,Acyl-coenzyme A cholesterol acyltransferase 1,Cholesterol acyltransferase 1,Mouse,Mus musculus,Soat1,Sterol O-acyltransferase 1
EIAAB39182 Acat2,ACAT-2,Acyl-coenzyme A cholesterol acyltransferase 2,Cholesterol acyltransferase 2,Rat,Rattus norvegicus,Soat2,Sterol O-acyltransferase 2
U2114h CLIA Homo sapiens,Human,LCAT,Lecithin-cholesterol acyltransferase,Phosphatidylcholine-sterol acyltransferase,Phospholipid-cholesterol acyltransferase 96T
E2114Rb ELISA kit LCAT,Lecithin-cholesterol acyltransferase,Oryctolagus cuniculus,Phosphatidylcholine-sterol acyltransferase,Phospholipid-cholesterol acyltransferase,Rabbit 96T
E2114h ELISA kit Homo sapiens,Human,LCAT,Lecithin-cholesterol acyltransferase,Phosphatidylcholine-sterol acyltransferase,Phospholipid-cholesterol acyltransferase 96T
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


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur