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Q8C0N2 (GPAT3_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 76. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glycerol-3-phosphate acyltransferase 3
Short name=GPAT-3
EC=2.3.1.15
Alternative name(s):
1-acylglycerol-3-phosphate O-acyltransferase 9
Short name=1-AGP acyltransferase 9
Short name=1-AGPAT 9
Acyl-CoA:glycerol-3-phosphate acyltransferase 3
Short name=mGPAT3
Lysophosphatidic acid acyltransferase theta
Short name=LPAAT-theta
Gene names
Name:Agpat9
Synonyms:Gpat3
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 length438 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Esterifies acyl-group from acyl-ACP to the sn-1 position of glycerol-3-phosphate, an essential step in glycerolipid biosynthesis. Ref.3

Catalytic activity

Acyl-CoA + sn-glycerol 3-phosphate = CoA + 1-acyl-sn-glycerol 3-phosphate.

Pathway

Glycerolipid metabolism; triacylglycerol biosynthesis.

Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-diacylglycerol from sn-glycerol 3-phosphate: step 1/3.

Subcellular location

Endoplasmic reticulum membrane; Multi-pass membrane protein Ref.3.

Tissue specificity

Most abundant in epididymal fat, followed by small intestine, brown adipose tissue, kidney, heart and colon. Ref.3

Induction

During adipocyte differentiation. Ref.3

Domain

The HXXXXD motif is essential for acyltransferase activity and may constitute the binding site for the phosphate moiety of the glycerol-3-phosphate By similarity.

Sequence similarities

Belongs to the 1-acyl-sn-glycerol-3-phosphate acyltransferase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 438438Glycerol-3-phosphate acyltransferase 3
PRO_0000291571

Regions

Transmembrane14 – 3421Helical; Potential
Transmembrane137 – 15721Helical; Potential
Transmembrane161 – 18121Helical; Potential
Motif229 – 2346HXXXXD motif

Amino acid modifications

Modified residue681Phosphoserine Ref.4 Ref.5
Modified residue771Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8C0N2 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: 29B4ED7405DCC8BD

FASTA43849,000
        10         20         30         40         50         60 
MEGADLAVKL LSTWLTLVGG LILLPSAFGL SLGISEIYMK ILVKTLEWAT LRIQKGAPKE 

        70         80         90        100        110        120 
SALKNSASVG IIQRDESPME KGLSGLRGRD FELSDVFYFS KKGLEAIVED EVTQRFSSEE 

       130        140        150        160        170        180 
LVSWNLLTRT NVNFQYISPR LTMVWVLGVL VRYCFLLPLR VTLAFIGISL LIIGTTLVGQ 

       190        200        210        220        230        240 
LPDSSLKNWL SELVHLTCCR ICVRSLSGTI HYHNKQYRPQ KGGICVANHT SPIDVLILAT 

       250        260        270        280        290        300 
DGCYAMVGQV HGGLMGIIQR AMVKACPHVW FERSEIKDRH LVTKRLKEHI ADKKKLPILI 

       310        320        330        340        350        360 
FPEGTCINNT SVMMFKKGSF EIGGTIYPVA IKYNPQFGDA FWNSSKYNLV SYLLRIMTSW 

       370        380        390        400        410        420 
AIVCDVWYMP PMTREEGEDA VQFANRVKSA IAVQGGLTEL PWDGGLKRAK VKDTFKEEQQ 

       430 
KNYSKMIVGN GSPNLARD

« Hide

References

« Hide 'large scale' references
[1]"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: Hypothalamus and Testis.
[2]"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: CD-1.
Tissue: Brain, Neural stem cell and Testis.
[3]"Molecular identification of microsomal acyl-CoA:glycerol-3-phosphate acyltransferase, a key enzyme in de novo triacylglycerol synthesis."
Cao J., Li J.-L., Li D., Tobin J.F., Gimeno R.E.
Proc. Natl. Acad. Sci. U.S.A. 103:19695-19700(2006) [PubMed: 17170135] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION.
[4]"Specific phosphopeptide enrichment with immobilized titanium ion affinity chromatography adsorbent for phosphoproteome analysis."
Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.
J. Proteome Res. 7:3957-3967(2008) [PubMed: 18630941] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-68, MASS SPECTROMETRY.
Tissue: Liver.
[5]"The phagosomal proteome in interferon-gamma-activated macrophages."
Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
Immunity 30:143-154(2009) [PubMed: 19144319] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-68, MASS SPECTROMETRY.
Tissue: Macrophage.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AK030171 mRNA. Translation: BAC26820.1.
AK160261 mRNA. Translation: BAE35719.1.
AK138410 mRNA. Translation: BAE23647.1.
BC096769 mRNA. Translation: AAH96769.1.
BC138228 mRNA. Translation: AAI38229.1.
BC145669 mRNA. Translation: AAI45670.1.
IPIIPI00223880.
RefSeqNP_766303.1. NM_172715.3.
UniGeneMm.482473.

3D structure databases

ProteinModelPortalQ8C0N2.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ8C0N2.

PTM databases

PhosphoSiteQ8C0N2.

Proteomic databases

PRIDEQ8C0N2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000031255; ENSMUSP00000031255; ENSMUSG00000029314.
ENSMUST00000092990; ENSMUSP00000090667; ENSMUSG00000029314.
ENSMUST00000112887; ENSMUSP00000108508; ENSMUSG00000029314.
GeneID231510.
KEGGmmu:231510.
UCSCuc008yih.1. mouse.

Organism-specific databases

CTD84803.
MGIMGI:3603816. Agpat9.

Phylogenomic databases

eggNOGroNOG12959.
GeneTreeENSGT00390000000536.
HOGENOMHBG408354.
InParanoidQ8C0N2.
OMAKPQKGGI.
OrthoDBEOG4Z62NH.
PhylomeDBQ8C0N2.

Gene expression databases

ArrayExpressQ8C0N2.
BgeeQ8C0N2.
CleanExMM_AGPAT9.
GenevestigatorQ8C0N2.

Family and domain databases

InterProIPR002123. Acyltransferase.
[Graphical view]
KOK13506.
PfamPF01553. Acyltransferase. 1 hit.
[Graphical view]
SMARTSM00563. PlsC. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio380592.
SOURCESearch...

Entry information

Entry nameGPAT3_MOUSE
AccessionPrimary (citable) accession number: Q8C0N2
Secondary accession number(s): A6H5X0
Entry history
Integrated into UniProtKB/Swiss-Prot: June 26, 2007
Last sequence update: March 1, 2003
Last modified: November 16, 2011
This is version 76 of the entry and version 1 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