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Q61263 (SOAT1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 86. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Sterol O-acyltransferase 1

EC=2.3.1.26
Alternative name(s):
Acyl-coenzyme A:cholesterol acyltransferase 1
Short name=ACAT-1
Cholesterol acyltransferase 1
Gene names
Name:Soat1
Synonyms:Acact
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length540 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Catalyzes the formation of fatty acid-cholesterol esters. Plays a role in lipoprotein assembly and dietary cholesterol absorption.

Catalytic activity

Acyl-CoA + cholesterol = CoA + cholesterol ester.

Subcellular location

Endoplasmic reticulum membrane; Multi-pass membrane protein.

Sequence similarities

Belongs to the membrane-bound acyltransferase family. Sterol o-acyltransferase subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 540540Sterol O-acyltransferase 1
PRO_0000207642

Regions

Transmembrane132 – 15221Helical; Potential
Transmembrane311 – 33121Helical; Potential
Transmembrane352 – 37221Helical; Potential
Transmembrane460 – 48021Helical; Potential
Transmembrane488 – 50821Helical; Potential

Sites

Active site4501 Potential

Experimental info

Sequence conflict1951R → P in AAC42075. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q61263 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: F2A6C91774762E23

FASTA54063,799
        10         20         30         40         50         60 
MSLRNRLSKS GENPEQDEAQ KNFMDTYRNG HITMKQLIAK KRLLAAEAEE LKPLFMKEVG 

        70         80         90        100        110        120 
CHFDDFVTNL IEKSASLDNG GCALTTFSIL EEMKKNHRAK DLRAPPEQGK IFISRQSLLD 

       130        140        150        160        170        180 
ELFEVDHIRT IYHMFIALLI LFVLSTIVVD YIDEGRLVLE FNLLAYAFGK FPTVIWTWWA 

       190        200        210        220        230        240 
MFLSTLSIPY FLFQRWAHGY SKSSHPLIYS LVHGLLFLVF QLGVLGFVPT YVVLAYTLPP 

       250        260        270        280        290        300 
ASRFILILEQ IRLIMKAHSF VRENIPRVLN AAKEKSSKDP LPTVNQYLYF LFAPTLIYRD 

       310        320        330        340        350        360 
NYPRTPTVRW GYVAMQFLQV FGCLFYVYYI FERLCAPLFR NIKQEPFSAR VLVLCVFNSI 

       370        380        390        400        410        420 
LPGVLILFLS FFAFLHCWLN AFAEMLRFGD RMFYKDWWNS TSYSNYYRTW NVVVHDWLYY 

       430        440        450        460        470        480 
YVYKDLLWFF SKRFKSAAML AVFALSAVVH EYALAICLSY FYPVLFVLFM FFGMAFNFIV 

       490        500        510        520        530        540 
NDSRKRPIWN IMVWASLFLG YGLILCFYSQ EWYARQHCPL KNPTFLDYVR PRTWTCRYVF 

« Hide

References

« Hide 'large scale' references
[1]"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."
Uelmen P.J., Oka K., Sullivan M.C., Chang T.-Y., Chang C.C.Y., Chan L.
J. Biol. Chem. 270:26192-26201(1995) [PubMed: 7592824] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Liver.
[2]"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."
Green S., Steinberg D., Quehenberger O.
Biochem. Biophys. Res. Commun. 218:924-929(1996) [PubMed: 8579615] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"The transcriptional landscape of the mammalian genome."
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. expand/collapse author list , 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.
Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Stomach.
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Embryo.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L42293 mRNA. Translation: AAC42075.1.
S81092 mRNA. Translation: AAB36050.1.
AK142486 mRNA. Translation: BAE25081.1.
AK159393 mRNA. Translation: BAE35047.1.
AK159529 mRNA. Translation: BAE35158.1.
AK160017 mRNA. Translation: BAE35563.1.
BC083092 mRNA. Translation: AAH83092.1.
IPIIPI00278153.
PIRI49454.
RefSeqNP_033256.2. NM_009230.3.
UniGeneMm.28099.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGQ61263.

Proteomic databases

PRIDEQ61263.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000051396; ENSMUSP00000058344; ENSMUSG00000026600.
GeneID20652.
KEGGmmu:20652.

Organism-specific databases

CTD6646.
MGIMGI:104665. Soat1.

Phylogenomic databases

HOGENOMHBG446698.
HOVERGENHBG058198.
InParanoidQ61263.
OrthoDBEOG4M65H6.

Gene expression databases

ArrayExpressQ61263.
BgeeQ61263.
CleanExMM_SOAT1.
GenevestigatorQ61263.
GermOnlineENSMUSG00000026600. Mus musculus.

Family and domain databases

InterProIPR004299. MBOAT_fam.
IPR014371. Oat_ACAT_DAG_ARE.
[Graphical view]
KOK00637.
PANTHERPTHR10408. PTHR10408. 1 hit.
PfamPF03062. MBOAT. 1 hit.
[Graphical view]
PIRSFPIRSF000439. Oat_ACAT_DAG_ARE. 1 hit.
ProtoNetSearch...

Other

NextBio299075.
SOURCESearch...

Entry information

Entry nameSOAT1_MOUSE
AccessionPrimary (citable) accession number: Q61263
Secondary accession number(s): Q5XK32, Q64180
Entry history
Integrated into UniProtKB/Swiss-Prot: October 18, 2001
Last sequence update: July 27, 2011
Last modified: December 14, 2011
This is version 86 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families