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Reviewed, UniProtKB/Swiss-Prot Q80W94 (MOGT2_MOUSE)

Last modified November 25, 2008. Version 39. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    2-acylglycerol O-acyltransferase 2
    EC=2.3.1.22
Alternative name(s):
    Monoacylglycerol O-acyltransferase 2
    Acyl CoA:monoacylglycerol acyltransferase 2
      Short name=MGAT2
    Diacylglycerol acyltransferase 2-like protein 5
    Monoacylglycerol O-acyltransferase 1-like
Gene names
Name: Mogat2
Synonyms: Dgat2l5, Mgat1l
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMus

Protein attributes

Sequence length334 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Catalyzes the formation of diacylglycerol from 2-monoacylglycerol and fatty acyl-CoA. Has a preference toward monoacylglycerols containing unsaturated fatty acids in an order of C18:3 > C18:2 > C18:1 > C18:0. Plays a central role in absorption of dietary fat in the small intestine by catalyzing the resynthesis of triacylglycerol in enterocytes. May play a role in diet-induced obesity.

Catalytic activity

Acyl-CoA + 2-acylglycerol = CoA + diacylglycerol.

Enzyme regulation

Inhibited by oleic acid and sphingosine, while it is stimulated by phosphatidylcholine, phosphatidylserine and phosphatidic acid.

Pathway

Glycerolipid metabolism; triacylglycerol biosynthesis.

Subcellular location

Endoplasmic reticulum membrane; Multi-pass membrane protein.

Tissue specificity

Mainly expressed in small intestine. Detected in the small intestine in a proximal-to-distal gradient that correlated with fat absorption pattern. Present not only in the villi, but also in the crypt regions of the small intestine, which suggests that expression occurs prior to the maturation of enterocytes. Not detectable in other sections of the digestive tract, including stomach, cecum, colon and rectum, or other tissues such as kidney, liver and adipocytes (at protein level). Also detected in kidney, adipose and stomach. Expressed at very low level in liver, skeletal muscle and spleen. Not expressed in brain, heart, lung, skin, testis and thymus.

Induction

Up-regulated in mice fed a high fat diet, implicating a role in diet-induced obesity (at protein level).

Sequence similarities

Belongs to the diacylglycerol acyltransferase family.

Biophysicochemical properties

pH dependence:

Optimum pH is 7.0.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 3343342-acylglycerol O-acyltransferase 2
PRO_0000249063

Regions

Transmembrane23 – 4321 Potential
Transmembrane212 – 23221 Potential

Sequences

Sequence LengthMass (Da)Tools
Q80W94-1 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: BFC7C84A22B607BD

FASTA33438,591
        10         20         30         40         50         60 
MVEFAPLLVP WERRLQTFAV LQWVFSFLAL AQLCIVIFVG LLFTRFWLFS VLYATWWYLD 

        70         80         90        100        110        120 
WDKPRQGGRP IQFFRRLAIW KYMKDYFPVS LVKTAELDPS RNYIAGFHPH GVLAAGAFLN 

       130        140        150        160        170        180 
LCTESTGFTS LFPGIRSYLM MLTVWFRAPF FRDYIMSGGL VSSEKVSADH ILSRKGGGNL 

       190        200        210        220        230        240 
LAIIVGGAQE ALDARPGAYR LLLKNRKGFI RLALMHGAAL VPIFSFGENN LFNQVENTPG 

       250        260        270        280        290        300 
TWLRWIQNRL QKIMGISLPL FHGRGVFQYS FGLMPFRQPI TTIVGKPIEV QMTPQPSREE 

       310        320        330 
VDRLHQRYIK ELCKLFEEHK LKFNVPEDQH LEFC 

« Hide

References

« Hide 'large scale' references
[1]"MGAT2, a monoacylglycerol acyltransferase expressed in the small intestine."
Yen C.-L.E., Farese R.V. Jr.
J. Biol. Chem. 278:18532-18537(2003) [PubMed: 12621063] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
Strain: C57BL/6J.
Tissue: Intestine.
[2]"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.
[3]"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/6NCr.
Tissue: Hematopoietic stem cell.
[4]"Cloning and functional characterization of a mouse intestinal acyl-CoA:monoacylglycerol acyltransferase, MGAT2."
Cao J., Lockwood J., Burn P., Shi Y.
J. Biol. Chem. 278:13860-13866(2003) [PubMed: 12576479] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY.
[5]"Properties of the mouse intestinal acyl-CoA:monoacylglycerol acyltransferase, MGAT2."
Cao J., Burn P., Shi Y.
J. Biol. Chem. 278:25657-25663(2003) [PubMed: 12730219] [Abstract]
Cited for: FUNCTION, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
[6]"A predominant role of acyl-CoA:monoacylglycerol acyltransferase-2 in dietary fat absorption implicated by tissue distribution, subcellular localization, and up-regulation by high fat diet."
Cao J., Hawkins E., Brozinick J., Liu X., Zhang H., Burn P., Shi Y.
J. Biol. Chem. 279:18878-18886(2004) [PubMed: 14966132] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

AY157609 mRNA. Translation: AAO23673.1.
AK133854 mRNA. Translation: BAE21888.1.
BC052831 mRNA. Translation: AAH52831.1.
RefSeqNP_803231.1.
UniGeneMm.208030

3D structure databases

ModBaseSearch...

PTM databases

PhosphoSiteQ80W94.

Genome annotation databases

EnsemblENSMUSG00000052396. Mus musculus. [Contig view]
GeneID233549.
KEGGmmu:233549.

Organism-specific databases

MGIMGI:2663253. Mogat2.

Phylogenomic databases

HOVERGENQ80W94.

Gene expression databases

ArrayExpressQ80W94.
CleanExMM_MOGAT2.
GermOnlineENSMUSG00000052396. Mus musculus.

Family and domain databases

InterProIPR007130. DAGAT.
[Graphical view]
PANTHERPTHR12317. DAGAT. 1 hit.
PfamPF03982. DAGAT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio381755.
SOURCESearch...

Entry information

Entry nameMOGT2_MOUSE
AccessionPrimary (citable) accession number: Q80W94
Entry history
Integrated into UniProtKB/Swiss-Prot: September 5, 2006
Last sequence update: June 1, 2003
Last modified: November 25, 2008
This is version 39 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

MGD cross-references

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

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents