AGPAT9

Mammalian protein found in Homo sapiens
GPAT3
Identifiers
AliasesGPAT3, AGPAT 10, AGPAT8, LPAAT-theta, MAG1, AGPAT9, HMFN0839, AGPAT10, glycerol-3-phosphate acyltransferase 3
External IDsOMIM: 610958; MGI: 3603816; HomoloGene: 13099; GeneCards: GPAT3; OMA:GPAT3 - orthologs
EC number2.3.1.51
Gene location (Human)
Chromosome 4 (human)
Chr.Chromosome 4 (human)[1]
Chromosome 4 (human)
Genomic location for GPAT3
Genomic location for GPAT3
Band4q21.23Start83,535,914 bp[1]
End83,605,875 bp[1]
Gene location (Mouse)
Chromosome 5 (mouse)
Chr.Chromosome 5 (mouse)[2]
Chromosome 5 (mouse)
Genomic location for GPAT3
Genomic location for GPAT3
Band5|5 E4Start100,993,579 bp[2]
End101,046,968 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • secondary oocyte

  • jejunal mucosa

  • mucosa of ileum

  • myocardium of left ventricle

  • renal medulla

  • Skeletal muscle tissue of rectus abdominis

  • cardiac muscle tissue of right atrium

  • pancreatic epithelial cell

  • buccal mucosa cell

  • duodenum
Top expressed in
  • jejunum

  • mammary gland

  • white adipose tissue

  • morula

  • pineal gland

  • granulocyte

  • ileum

  • subcutaneous adipose tissue

  • duodenum

  • epithelium of small intestine
More reference expression data
BioGPS
More reference expression data
Gene ontology
Molecular function
  • transferase activity
  • acyltransferase activity
  • glycerol-3-phosphate O-acyltransferase activity
  • 1-acylglycerol-3-phosphate O-acyltransferase activity
  • sn-1-glycerol-3-phosphate C16:0-DCA-CoA acyl transferase activity
Cellular component
  • integral component of membrane
  • endoplasmic reticulum membrane
  • endoplasmic reticulum
  • membrane
Biological process
  • phosphatidic acid biosynthetic process
  • CDP-diacylglycerol biosynthetic process
  • metabolism
  • regulation of TOR signaling
  • lipid metabolism
  • phospholipid biosynthetic process
  • triglyceride biosynthetic process
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

84803

231510

Ensembl

ENSG00000138678

ENSMUSG00000029314

UniProt

Q53EU6

Q8C0N2

RefSeq (mRNA)

NM_001256421
NM_001256422
NM_032717

NM_172715

RefSeq (protein)

NP_001243350
NP_001243351
NP_116106

NP_766303

Location (UCSC)Chr 4: 83.54 – 83.61 MbChr 5: 100.99 – 101.05 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Glycerol-3-phosphate acyltransferase 3 (GPAT-3) is an enzyme that in humans is encoded by the AGPAT9 gene.[5][6][7][8] GPAT-3 is also known as:

  • 1-acylglycerol-3-phosphate O-acyltransferase 9 (AGPAT9),
  • lysophosphatidic acid acyltransferase theta (LPAAT-theta), or
  • lung cancer metastasis-associated protein 1.

Function

Glycerol-3-phosphate (G3P) acyltransferases (GPAT; EC 2.3.1.15), such as GPAM and GPAT3 (this enzyme), catalyze the initial step of de novo triacylglycerol (TAG) synthesis by converting glycerol-3-phosphate (G3P) to lysophosphatidic acid (LPA).[6]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000138678 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000029314 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Clark HF, Gurney AL, Abaya E, et al. (October 2003). "The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment". Genome Res. 13 (10): 2265–70. doi:10.1101/gr.1293003. PMC 403697. PMID 12975309.
  6. ^ a b Cao J, Li JL, Li D, Tobin JF, Gimeno RE (December 2006). "Molecular identification of microsomal acyl-CoA:glycerol-3-phosphate acyltransferase, a key enzyme in de novo triacylglycerol synthesis". Proc. Natl. Acad. Sci. U.S.A. 103 (52): 19695–700. Bibcode:2006PNAS..10319695C. doi:10.1073/pnas.0609140103. PMC 1702318. PMID 17170135.
  7. ^ Tang W, Yuan J, Chen X, Gu X, Luo K, Li J, Wan B, Wang Y, Yu L (September 2006). "Identification of a novel human lysophosphatidic acid acyltransferase, LPAAT-theta, which activates mTOR pathway". J. Biochem. Mol. Biol. 39 (5): 626–35. doi:10.5483/BMBRep.2006.39.5.626. PMID 17002884.
  8. ^ "Entrez Gene: AGPAT9: 1-acylglycerol-3-phosphate O-acyltransferase 9".

Further reading

  • Tang W, Yuan J, Chen X, et al. (2006). "Identification of a novel human lysophosphatidic acid acyltransferase, LPAAT-theta, which activates mTOR pathway". J. Biochem. Mol. Biol. 39 (5): 626–35. doi:10.5483/BMBRep.2006.39.5.626. PMID 17002884.
  • Yamada S, Ohira M, Horie H, et al. (2004). "Expression profiling and differential screening between hepatoblastomas and the corresponding normal livers: identification of high expression of the PLK1 oncogene as a poor-prognostic indicator of hepatoblastomas". Oncogene. 23 (35): 5901–11. doi:10.1038/sj.onc.1207782. PMID 15221005.
  • Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
  • Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
  • Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
  • Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.

This article incorporates text from the United States National Library of Medicine, which is in the public domain.


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