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Q91ZV4 (MOGT1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 65. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
2-acylglycerol O-acyltransferase 1
EC=2.3.1.22
Alternative name(s):
Acyl-CoA:monoacylglycerol acyltransferase 1
Short name=MGAT1
Diacylglycerol acyltransferase 2-like protein 1
Monoacylglycerol O-acyltransferase 1
Gene names
Name:Mogat1
Synonyms:Dgat2l1
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length335 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the formation of diacylglycerol from 2-monoacylglycerol and fatty acyl-CoA. Probably not involved in absorption of dietary fat in the small intestine. Ref.5

Catalytic activity

Acyl-CoA + 2-acylglycerol = CoA + diacylglycerol. Ref.5

Pathway

Glycerolipid metabolism; triacylglycerol biosynthesis.

Subcellular location

Endoplasmic reticulum membrane; Multi-pass membrane protein Probable Ref.5.

Tissue specificity

Expressed at high level in kidney and stomach. Expressed at lower level in brown and white adipose tissue, uterus and liver. Not detected in small intestine. Ref.5

Sequence similarities

Belongs to the diacylglycerol acyltransferase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 3353352-acylglycerol O-acyltransferase 1
PRO_0000249059

Regions

Transmembrane24 – 4421Helical; Potential
Transmembrane104 – 12421Helical; Potential

Amino acid modifications

Glycosylation1801N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict85 – 862KE → FL in BAB22288. Ref.2
Sequence conflict2941T → I in AAK84177. Ref.1
Sequence conflict2941T → I in AAI06136. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Q91ZV4 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: A2691D9E6451AD30

FASTA33538,791
        10         20         30         40         50         60 
MMVEFAPLNT PLARCLQTAA VLQWVLSFLL LVQVCIGIMV MLVLYNYWFL YIPYLVWFYY 

        70         80         90        100        110        120 
DWRTPEQGGR RWNWVQSWPV WKYFKEYFPI CLVKTQDLDP GHNYIFGFHP HGIFVPGAFG 

       130        140        150        160        170        180 
NFCTKYSDFK KLFPGFTSYL HVAKIWFCFP LFREYLMSNG PVSVSKESLS HVLSKDGGGN 

       190        200        210        220        230        240 
VSIIVLGGAK EALEAHPGTF TLCIRQRKGF VKMALTHGAS LVPVFSFGEN DLYKQINNPK 

       250        260        270        280        290        300 
GSWLRTIQDA MYDSMGVALP LIYARGIFQH YFGIMPYRKL IYTVVGRPIP VQQTLNPTSE 

       310        320        330 
QIEELHQTYL EELKKLFNEH KGKYGIPEHE TLVFK

« Hide

References

« Hide 'large scale' references
[1]"Cloning of DGAT2, a second mammalian diacylglycerol acyltransferase, and related family members."
Cases S., Stone S.J., Zhou P., Yen C.-L.E., Tow B., Lardizabal K.D., Voelker T., Farese R.V. Jr.
J. Biol. Chem. 276:38870-38876(2001) [PubMed: 11481335] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Liver.
[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.
Tissue: Kidney.
[3]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed: 19468303] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6.
[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: FVB/N.
Tissue: Kidney.
[5]"Identification of a gene encoding MGAT1, a monoacylglycerol acyltransferase."
Yen C.-L.E., Stone S.J., Cases S., Zhou P., Farese R.V. Jr.
Proc. Natl. Acad. Sci. U.S.A. 99:8512-8517(2002) [PubMed: 12077311] [Abstract]
Cited for: CATALYTIC ACTIVITY, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF384162 mRNA. Translation: AAK84177.1.
AK002693 mRNA. Translation: BAB22288.1.
AC158559 Genomic DNA. No translation available.
BC106135 mRNA. Translation: AAI06136.1.
IPIIPI00121027.
RefSeqNP_080989.2. NM_026713.3.
UniGeneMm.41325.

3D structure databases

ProteinModelPortalQ91ZV4.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ91ZV4.

Proteomic databases

PRIDEQ91ZV4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000012331; ENSMUSP00000012331; ENSMUSG00000012187.
ENSMUST00000113524; ENSMUSP00000109152; ENSMUSG00000012187.
GeneID68393.
KEGGmmu:68393.
UCSCuc007bqk.1. mouse.

Organism-specific databases

CTD116255.
MGIMGI:1915643. Mogat1.

Phylogenomic databases

GeneTreeENSGT00550000074276.
HOGENOMHBG561030.
HOVERGENHBG065791.
InParanoidQ91ZV4.
OrthoDBEOG4BP1C4.
PhylomeDBQ91ZV4.

Gene expression databases

ArrayExpressQ91ZV4.
BgeeQ91ZV4.
CleanExMM_MOGAT1.
GenevestigatorQ91ZV4.
GermOnlineENSMUSG00000012187. Mus musculus.

Family and domain databases

InterProIPR007130. DAGAT.
[Graphical view]
KOK14458.
PANTHERPTHR12317. DAGAT. 1 hit.
PfamPF03982. DAGAT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio327104.
SOURCESearch...

Entry information

Entry nameMOGT1_MOUSE
AccessionPrimary (citable) accession number: Q91ZV4
Secondary accession number(s): E9QLA2, Q9DCL0
Entry history
Integrated into UniProtKB/Swiss-Prot: September 5, 2006
Last sequence update: July 27, 2011
Last modified: January 25, 2012
This is version 65 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

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents