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Q8C0N2

- GPAT3_MOUSE

UniProt

Q8C0N2 - GPAT3_MOUSE

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Protein

Glycerol-3-phosphate acyltransferase 3

Gene

Agpat9

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

May transfer the acyl-group from acyl-coA to the sn-1 position of glycerol-3-phosphate, an essential step in glycerolipid biosynthesis. Also transfers the acyl-group from acyl-coA to the sn-2 position of 1-acyl-sn-glycerol-3-phosphate (lysophosphatidic acid, or LPA), forming 1,2-diacyl-sn-glycerol-3-phosphate (phosphatidic acid, or PA).1 Publication

Catalytic activityi

Acyl-CoA + sn-glycerol 3-phosphate = CoA + 1-acyl-sn-glycerol 3-phosphate.
Acyl-CoA + 1-acyl-sn-glycerol 3-phosphate = CoA + 1,2-diacyl-sn-glycerol 3-phosphate.

Pathwayi

GO - Molecular functioni

  1. 1-acylglycerol-3-phosphate O-acyltransferase activity Source: UniProtKB-EC
  2. glycerol-3-phosphate O-acyltransferase activity Source: UniProtKB

GO - Biological processi

  1. CDP-diacylglycerol biosynthetic process Source: UniProtKB-UniPathway
  2. regulation of TOR signaling Source: Ensembl
  3. triglyceride biosynthetic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Lipid biosynthesis, Lipid metabolism, Phospholipid biosynthesis, Phospholipid metabolism

Enzyme and pathway databases

ReactomeiREACT_188640. Synthesis of PA.
REACT_237947. Triglyceride Biosynthesis.
UniPathwayiUPA00282.
UPA00557; UER00612.

Names & Taxonomyi

Protein namesi
Recommended name:
Glycerol-3-phosphate acyltransferase 3 (EC:2.3.1.15)
Short name:
GPAT-3
Alternative name(s):
1-acyl-sn-glycerol-3-phosphate O-acyltransferase 9 (EC:2.3.1.51)
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 namesi
Name:Agpat9
Synonyms:Gpat3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 5

Organism-specific databases

MGIiMGI:3603816. Agpat9.

Subcellular locationi

Endoplasmic reticulum membrane 1 Publication; Multi-pass membrane protein 1 Publication

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei14 – 3421HelicalSequence AnalysisAdd
BLAST
Transmembranei137 – 15721HelicalSequence AnalysisAdd
BLAST
Transmembranei161 – 18121HelicalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. endoplasmic reticulum Source: UniProtKB
  2. endoplasmic reticulum membrane Source: UniProtKB
  3. integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 438438Glycerol-3-phosphate acyltransferase 3PRO_0000291571Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei68 – 681Phosphoserine3 Publications
Modified residuei77 – 771PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ8C0N2.
PaxDbiQ8C0N2.
PRIDEiQ8C0N2.

PTM databases

PhosphoSiteiQ8C0N2.

Expressioni

Tissue specificityi

Most abundant in epididymal fat, followed by small intestine, brown adipose tissue, kidney, heart and colon.1 Publication

Inductioni

During adipocyte differentiation.1 Publication

Gene expression databases

BgeeiQ8C0N2.
CleanExiMM_AGPAT9.
GenevestigatoriQ8C0N2.

Structurei

3D structure databases

ProteinModelPortaliQ8C0N2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi229 – 2346HXXXXD motif

Domaini

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 similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0204.
GeneTreeiENSGT00390000000536.
HOGENOMiHOG000265725.
InParanoidiQ8C0N2.
KOiK13506.
OMAiLVRYCVL.
PhylomeDBiQ8C0N2.
TreeFamiTF315039.

Family and domain databases

InterProiIPR002123. Plipid/glycerol_acylTrfase.
[Graphical view]
PfamiPF01553. Acyltransferase. 1 hit.
[Graphical view]
SMARTiSM00563. PlsC. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8C0N2-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MEGADLAVKL LSTWLTLVGG LILLPSAFGL SLGISEIYMK ILVKTLEWAT
60 70 80 90 100
LRIQKGAPKE SALKNSASVG IIQRDESPME KGLSGLRGRD FELSDVFYFS
110 120 130 140 150
KKGLEAIVED EVTQRFSSEE LVSWNLLTRT NVNFQYISPR LTMVWVLGVL
160 170 180 190 200
VRYCFLLPLR VTLAFIGISL LIIGTTLVGQ LPDSSLKNWL SELVHLTCCR
210 220 230 240 250
ICVRSLSGTI HYHNKQYRPQ KGGICVANHT SPIDVLILAT DGCYAMVGQV
260 270 280 290 300
HGGLMGIIQR AMVKACPHVW FERSEIKDRH LVTKRLKEHI ADKKKLPILI
310 320 330 340 350
FPEGTCINNT SVMMFKKGSF EIGGTIYPVA IKYNPQFGDA FWNSSKYNLV
360 370 380 390 400
SYLLRIMTSW AIVCDVWYMP PMTREEGEDA VQFANRVKSA IAVQGGLTEL
410 420 430
PWDGGLKRAK VKDTFKEEQQ KNYSKMIVGN GSPNLARD
Length:438
Mass (Da):49,000
Last modified:March 1, 2003 - v1
Checksum:i29B4ED7405DCC8BD
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS19470.1.
RefSeqiNP_766303.1. NM_172715.3.
UniGeneiMm.271911.

Genome annotation databases

EnsembliENSMUST00000031255; ENSMUSP00000031255; ENSMUSG00000029314.
ENSMUST00000092990; ENSMUSP00000090667; ENSMUSG00000029314.
ENSMUST00000112887; ENSMUSP00000108508; ENSMUSG00000029314.
GeneIDi231510.
KEGGimmu:231510.
UCSCiuc008yih.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
CCDSi CCDS19470.1.
RefSeqi NP_766303.1. NM_172715.3.
UniGenei Mm.271911.

3D structure databases

ProteinModelPortali Q8C0N2.
ModBasei Search...
MobiDBi Search...

PTM databases

PhosphoSitei Q8C0N2.

Proteomic databases

MaxQBi Q8C0N2.
PaxDbi Q8C0N2.
PRIDEi Q8C0N2.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000031255 ; ENSMUSP00000031255 ; ENSMUSG00000029314 .
ENSMUST00000092990 ; ENSMUSP00000090667 ; ENSMUSG00000029314 .
ENSMUST00000112887 ; ENSMUSP00000108508 ; ENSMUSG00000029314 .
GeneIDi 231510.
KEGGi mmu:231510.
UCSCi uc008yih.1. mouse.

Organism-specific databases

CTDi 84803.
MGIi MGI:3603816. Agpat9.

Phylogenomic databases

eggNOGi COG0204.
GeneTreei ENSGT00390000000536.
HOGENOMi HOG000265725.
InParanoidi Q8C0N2.
KOi K13506.
OMAi LVRYCVL.
PhylomeDBi Q8C0N2.
TreeFami TF315039.

Enzyme and pathway databases

UniPathwayi UPA00282 .
UPA00557 ; UER00612 .
Reactomei REACT_188640. Synthesis of PA.
REACT_237947. Triglyceride Biosynthesis.

Miscellaneous databases

NextBioi 380592.
PROi Q8C0N2.
SOURCEi Search...

Gene expression databases

Bgeei Q8C0N2.
CleanExi MM_AGPAT9.
Genevestigatori Q8C0N2.

Family and domain databases

InterProi IPR002123. Plipid/glycerol_acylTrfase.
[Graphical view ]
Pfami PF01553. Acyltransferase. 1 hit.
[Graphical view ]
SMARTi SM00563. PlsC. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION.
  4. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-68, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  5. "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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-68, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  6. "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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-68, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiGPAT3_MOUSE
AccessioniPrimary (citable) accession number: Q8C0N2
Secondary accession number(s): A6H5X0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 26, 2007
Last sequence update: March 1, 2003
Last modified: November 26, 2014
This is version 98 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Caution

Despite its name, the human ortholog of this protein appears to lack measurable glycerol-3-phosphate acyltransferase activity under some conditions (PMID:19318427).Curated

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3