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GPAT3
Identifiers
Aliases	GPAT3, AGPAT 10, AGPAT8, LPAAT-theta, MAG1, AGPAT9, HMFN0839, AGPAT10, glycerol-3-phosphate acyltransferase 3
External IDs	OMIM: 610958; MGI: 3603816; HomoloGene: 13099; GeneCards: GPAT3; OMA:GPAT3 - orthologs
EC number	2.3.1.51
Gene location (Human) Chr. Chromosome 4 (human) Band 4q21.23 Start 83,535,914 bp End 83,605,875 bp
Gene location (Mouse) Chr. Chromosome 5 (mouse) Band 5|5 E4 Start 100,993,579 bp End 101,046,968 bp
RNA expression pattern Bgee Human Mouse (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 Species Human Mouse 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 Mb Chr 5: 100.99 – 101.05 Mb PubMed search
Wikidata
View/Edit Human View/Edit Mouse

Glycerol-3-phosphate acyltransferase 3 (GPAT-3) is an enzyme that in humans is encoded by the AGPAT9 gene. 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).

References

1. ^ GRCh38: Ensembl release 89: ENSG00000138678 – Ensembl, May 2017
2. ^ 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. ^ 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".

External links

• Human GPAT3 genome location and GPAT3 gene details page in the UCSC Genome Browser.

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.

• Genes on human chromosome 4