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Glycerol-3-phosphate acyltransferase 3 (GPAT-3) (EC 2.3.1.15) (1-acyl-sn-glycerol-3-phosphate O-acyltransferase 10) (AGPAT 10) (1-acyl-sn-glycerol-3-phosphate O-acyltransferase 9) (1-AGP acyltransferase 9) (1-AGPAT 9) (EC 2.3.1.51) (Acyl-CoA:glycerol-3-phosphate acyltransferase 3) (hGPAT3) (Lung cancer metastasis-associated protein 1) (Lysophosphatidic acid acyltransferase theta) (LPAAT-theta) (MAG-1)

 GPAT3_HUMAN             Reviewed;         434 AA.
Q53EU6; Q68CJ4; Q6GPI6; Q96NA3;
26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
26-JUN-2007, sequence version 2.
28-MAR-2018, entry version 107.
RecName: Full=Glycerol-3-phosphate acyltransferase 3 {ECO:0000312|HGNC:HGNC:28157};
Short=GPAT-3;
EC=2.3.1.15;
AltName: Full=1-acyl-sn-glycerol-3-phosphate O-acyltransferase 10;
Short=AGPAT 10;
AltName: Full=1-acyl-sn-glycerol-3-phosphate O-acyltransferase 9;
Short=1-AGP acyltransferase 9;
Short=1-AGPAT 9;
EC=2.3.1.51;
AltName: Full=Acyl-CoA:glycerol-3-phosphate acyltransferase 3;
Short=hGPAT3;
AltName: Full=Lung cancer metastasis-associated protein 1;
AltName: Full=Lysophosphatidic acid acyltransferase theta;
Short=LPAAT-theta;
AltName: Full=MAG-1;
Name=GPAT3 {ECO:0000312|HGNC:HGNC:28157}; Synonyms=AGPAT9, MAG1;
ORFNames=HMFN0839, UNQ2753/PRO6492;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
Zhang J., Meng Y., Du Z., Chen Z., Ling X., Xu Y., Lu Y.;
"Identification of metastasis associated genes MAG-1 and MAG-2.";
Zhongguo Fei Ai Za Zhi 6:460-463(2003).
[2]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, PATHWAY,
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=17002884; DOI=10.5483/BMBRep.2006.39.5.626;
Tang W., Yuan J., Chen X., Gu X., Luo K., Li J., Wan B., Wang Y.,
Yu L.;
"Identification of a novel human lysophosphatidic acid
acyltransferase, LPAAT-theta, which activates mTOR pathway.";
J. Biochem. Mol. Biol. 39:626-635(2006).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=12975309; DOI=10.1101/gr.1293003;
Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S.,
Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J.,
Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J.,
Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A.,
Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H.,
Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D.,
Wood W.I., Godowski P.J., Gray A.M.;
"The secreted protein discovery initiative (SPDI), a large-scale
effort to identify novel human secreted and transmembrane proteins: a
bioinformatics assessment.";
Genome Res. 13:2265-2270(2003).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Kidney;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Kidney;
Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.;
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=PNS, and Testis;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 167-434.
PubMed=15221005; DOI=10.1038/sj.onc.1207782;
Yamada S., Ohira M., Horie H., Ando K., Takayasu H., Suzuki Y.,
Sugano S., Hirata T., Goto T., Matsunaga T., Hiyama E., Hayashi Y.,
Ando H., Suita S., Kaneko M., Sasaki F., Hashizume K., Ohnuma N.,
Nakagawara A.;
"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 23:5901-5911(2004).
[8]
FUNCTION, ENZYME ACTIVITY, ENZYME REGULATION, AND TISSUE SPECIFICITY.
PubMed=17170135; DOI=10.1073/pnas.0609140103;
Cao J., Li J.-L., Li D., Tobin J.F., Gimeno R.E.;
"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. 103:19695-19700(2006).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-68 AND SER-77, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[10]
FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND SUBCELLULAR LOCATION.
PubMed=19318427; DOI=10.1677/JME-09-0010;
Sukumaran S., Barnes R.I., Garg A., Agarwal A.K.;
"Functional characterization of the human 1-acylglycerol-3-phosphate-
O-acyltransferase isoform 10/glycerol-3-phosphate acyltransferase
isoform 3.";
J. Mol. Endocrinol. 42:469-478(2009).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-68 AND SER-77, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-68, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
-!- FUNCTION: 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).
{ECO:0000269|PubMed:17002884, ECO:0000269|PubMed:17170135,
ECO:0000269|PubMed:19318427}.
-!- CATALYTIC ACTIVITY: Acyl-CoA + sn-glycerol 3-phosphate = CoA + 1-
acyl-sn-glycerol 3-phosphate.
-!- CATALYTIC ACTIVITY: Acyl-CoA + 1-acyl-sn-glycerol 3-phosphate =
CoA + 1,2-diacyl-sn-glycerol 3-phosphate.
-!- ENZYME REGULATION: Inhibited by N-ethylmaleimide (NEM).
{ECO:0000269|PubMed:17170135}.
-!- PATHWAY: Glycerolipid metabolism; triacylglycerol biosynthesis.
-!- PATHWAY: Phospholipid metabolism; CDP-diacylglycerol biosynthesis;
CDP-diacylglycerol from sn-glycerol 3-phosphate: step 1/3.
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
{ECO:0000269|PubMed:17002884, ECO:0000269|PubMed:19318427}; Multi-
pass membrane protein {ECO:0000269|PubMed:17002884,
ECO:0000269|PubMed:19318427}.
-!- TISSUE SPECIFICITY: Widely expressed. Expressed in liver, kidney,
testis, brain, heart, skeletal muscle, thyroid, prostate, thymus
and placenta. Also expressed lung and adipose tissue.
{ECO:0000269|PubMed:17002884, ECO:0000269|PubMed:17170135}.
-!- DOMAIN: The HXXXXD motif is essential for acyltransferase activity
and may constitute the binding site for the phosphate moiety of
the glycerol-3-phosphate. {ECO:0000250}.
-!- SIMILARITY: Belongs to the 1-acyl-sn-glycerol-3-phosphate
acyltransferase family. {ECO:0000305}.
-!- CAUTION: Despite its name, this protein appears to lack measurable
glycerol-3-phosphate acyltransferase activity under some
conditions (PMID:19318427). {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; DQ324782; ABC55674.1; -; mRNA.
EMBL; DQ345298; ABC70186.1; -; mRNA.
EMBL; AY358100; AAQ88467.1; -; mRNA.
EMBL; AK055749; BAB71002.1; -; mRNA.
EMBL; AK223543; BAD97263.1; -; mRNA.
EMBL; BC073136; AAH73136.1; -; mRNA.
EMBL; BC090956; AAH90956.1; -; mRNA.
EMBL; AB075872; BAD38654.1; -; mRNA.
CCDS; CCDS3606.1; -.
RefSeq; NP_001243350.1; NM_001256421.1.
RefSeq; NP_001243351.1; NM_001256422.1.
RefSeq; NP_116106.2; NM_032717.4.
RefSeq; XP_016864270.1; XM_017008781.1.
UniGene; Hs.99196; -.
ProteinModelPortal; Q53EU6; -.
BioGrid; 124267; 16.
IntAct; Q53EU6; 4.
STRING; 9606.ENSP00000264409; -.
SwissLipids; SLP:000000290; -.
iPTMnet; Q53EU6; -.
PhosphoSitePlus; Q53EU6; -.
BioMuta; AGPAT9; -.
DMDM; 150403919; -.
EPD; Q53EU6; -.
MaxQB; Q53EU6; -.
PaxDb; Q53EU6; -.
PeptideAtlas; Q53EU6; -.
PRIDE; Q53EU6; -.
Ensembl; ENST00000264409; ENSP00000264409; ENSG00000138678.
Ensembl; ENST00000395226; ENSP00000378651; ENSG00000138678.
Ensembl; ENST00000611707; ENSP00000482571; ENSG00000138678.
GeneID; 84803; -.
KEGG; hsa:84803; -.
UCSC; uc003how.5; human.
CTD; 84803; -.
DisGeNET; 84803; -.
EuPathDB; HostDB:ENSG00000138678.10; -.
GeneCards; GPAT3; -.
HGNC; HGNC:28157; GPAT3.
HPA; CAB033749; -.
HPA; HPA029414; -.
MIM; 610958; gene.
neXtProt; NX_Q53EU6; -.
OpenTargets; ENSG00000138678; -.
PharmGKB; PA162375888; -.
eggNOG; KOG2898; Eukaryota.
eggNOG; COG0204; LUCA.
GeneTree; ENSGT00390000000536; -.
HOGENOM; HOG000265725; -.
InParanoid; Q53EU6; -.
KO; K13506; -.
OMA; NINFQYI; -.
OrthoDB; EOG091G04E8; -.
PhylomeDB; Q53EU6; -.
TreeFam; TF315039; -.
BRENDA; 2.3.1.15; 2681.
Reactome; R-HSA-1483166; Synthesis of PA.
UniPathway; UPA00282; -.
UniPathway; UPA00557; UER00612.
ChiTaRS; GPAT3; human.
GeneWiki; AGPAT9; -.
GenomeRNAi; 84803; -.
PRO; PR:Q53EU6; -.
Proteomes; UP000005640; Chromosome 4.
Bgee; ENSG00000138678; -.
CleanEx; HS_AGPAT9; -.
ExpressionAtlas; Q53EU6; baseline and differential.
Genevisible; Q53EU6; HS.
GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0003841; F:1-acylglycerol-3-phosphate O-acyltransferase activity; TAS:Reactome.
GO; GO:0004366; F:glycerol-3-phosphate O-acyltransferase activity; IDA:UniProtKB.
GO; GO:0102420; F:sn-1-glycerol-3-phosphate C16:0-DCA-CoA acyl transferase activity; IEA:UniProtKB-EC.
GO; GO:0016024; P:CDP-diacylglycerol biosynthetic process; IEA:UniProtKB-UniPathway.
GO; GO:0006654; P:phosphatidic acid biosynthetic process; TAS:Reactome.
GO; GO:0032006; P:regulation of TOR signaling; IDA:UniProtKB.
GO; GO:0019432; P:triglyceride biosynthetic process; IDA:UniProtKB.
InterPro; IPR002123; Plipid/glycerol_acylTrfase.
Pfam; PF01553; Acyltransferase; 1.
SMART; SM00563; PlsC; 1.
1: Evidence at protein level;
Acyltransferase; Complete proteome; Endoplasmic reticulum;
Lipid biosynthesis; Lipid metabolism; Membrane;
Phospholipid biosynthesis; Phospholipid metabolism; Phosphoprotein;
Reference proteome; Transferase; Transmembrane; Transmembrane helix.
CHAIN 1 434 Glycerol-3-phosphate acyltransferase 3.
/FTId=PRO_0000291570.
TRANSMEM 14 34 Helical. {ECO:0000255}.
TRANSMEM 137 157 Helical. {ECO:0000255}.
TRANSMEM 161 181 Helical. {ECO:0000255}.
MOTIF 229 234 HXXXXD motif.
MOD_RES 68 68 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 77 77 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
CONFLICT 156 156 L -> I (in Ref. 5; BAD97263).
{ECO:0000305}.
SEQUENCE 434 AA; 48705 MW; 80DD5423E5E7847A CRC64;
MEGAELAGKI LSTWLTLVLG FILLPSVFGV SLGISEIYMK ILVKTLEWAT IRIEKGTPKE
SILKNSASVG IIQRDESPME KGLSGLRGRD FELSDVFYFS KKGLEAIVED EVTQRFSSEE
LVSWNLLTRT NVNFQYISLR LTMVWVLGVI VRYCVLLPLR VTLAFIGISL LVIGTTLVGQ
LPDSSLKNWL SELVHLTCCR ICVRALSGTI HYHNKQYRPQ KGGICVANHT SPIDVLILTT
DGCYAMVGQV HGGLMGIIQR AMVKACPHVW FERSEMKDRH LVTKRLKEHI ADKKKLPILI
FPEGTCINNT SVMMFKKGSF EIGGTIHPVA IKYNPQFGDA FWNSSKYNMV SYLLRMMTSW
AIVCDVWYMP PMTREEGEDA VQFANRVKSA IAIQGGLTEL PWDGGLKRAK VKDIFKEEQQ
KNYSKMIVGN GSLS


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