GPAT3_HUMAN
ID GPAT3_HUMAN Reviewed; 434 AA.
AC Q53EU6; Q68CJ4; Q6GPI6; Q96NA3;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2007, sequence version 2.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Glycerol-3-phosphate acyltransferase 3 {ECO:0000312|HGNC:HGNC:28157};
DE Short=GPAT-3;
DE EC=2.3.1.15 {ECO:0000269|PubMed:17170135};
DE AltName: Full=1-acyl-sn-glycerol-3-phosphate O-acyltransferase 10 {ECO:0000303|PubMed:19318427};
DE Short=AGPAT 10 {ECO:0000303|PubMed:19318427};
DE AltName: Full=1-acyl-sn-glycerol-3-phosphate O-acyltransferase 9;
DE Short=1-AGP acyltransferase 9;
DE Short=1-AGPAT 9;
DE EC=2.3.1.51 {ECO:0000269|PubMed:19318427};
DE AltName: Full=Acyl-CoA:glycerol-3-phosphate acyltransferase 3 {ECO:0000303|PubMed:19318427};
DE Short=hGPAT3 {ECO:0000303|PubMed:19318427};
DE AltName: Full=Lung cancer metastasis-associated protein 1;
DE AltName: Full=Lysophosphatidic acid acyltransferase theta;
DE Short=LPAAT-theta;
DE AltName: Full=MAG-1;
GN Name=GPAT3 {ECO:0000312|HGNC:HGNC:28157}; Synonyms=AGPAT9, MAG1;
GN ORFNames=HMFN0839, UNQ2753/PRO6492;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Zhang J., Meng Y., Du Z., Chen Z., Ling X., Xu Y., Lu Y.;
RT "Identification of metastasis associated genes MAG-1 and MAG-2.";
RL Zhongguo Fei Ai Za Zhi 6:460-463(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=17002884; DOI=10.5483/bmbrep.2006.39.5.626;
RA Tang W., Yuan J., Chen X., Gu X., Luo K., Li J., Wan B., Wang Y., Yu L.;
RT "Identification of a novel human lysophosphatidic acid acyltransferase,
RT LPAAT-theta, which activates mTOR pathway.";
RL J. Biochem. Mol. Biol. 39:626-635(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=PNS, and Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 167-434.
RX PubMed=15221005; DOI=10.1038/sj.onc.1207782;
RA Yamada S., Ohira M., Horie H., Ando K., Takayasu H., Suzuki Y., Sugano S.,
RA Hirata T., Goto T., Matsunaga T., Hiyama E., Hayashi Y., Ando H., Suita S.,
RA Kaneko M., Sasaki F., Hashizume K., Ohnuma N., Nakagawara A.;
RT "Expression profiling and differential screening between hepatoblastomas
RT and the corresponding normal livers: identification of high expression of
RT the PLK1 oncogene as a poor-prognostic indicator of hepatoblastomas.";
RL Oncogene 23:5901-5911(2004).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND TISSUE SPECIFICITY.
RX PubMed=17170135; DOI=10.1073/pnas.0609140103;
RA Cao J., Li J.-L., Li D., Tobin J.F., Gimeno R.E.;
RT "Molecular identification of microsomal acyl-CoA:glycerol-3-phosphate
RT acyltransferase, a key enzyme in de novo triacylglycerol synthesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:19695-19700(2006).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-68 AND SER-77, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [10]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY,
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=19318427; DOI=10.1677/jme-09-0010;
RA Sukumaran S., Barnes R.I., Garg A., Agarwal A.K.;
RT "Functional characterization of the human 1-acylglycerol-3-phosphate-O-
RT acyltransferase isoform 10/glycerol-3-phosphate acyltransferase isoform
RT 3.";
RL J. Mol. Endocrinol. 42:469-478(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-68 AND SER-77, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-68, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [13]
RP FUNCTION.
RX PubMed=30846318; DOI=10.1016/j.molcel.2019.01.036;
RA Piccolis M., Bond L.M., Kampmann M., Pulimeno P., Chitraju C.,
RA Jayson C.B.K., Vaites L.P., Boland S., Lai Z.W., Gabriel K.R.,
RA Elliott S.D., Paulo J.A., Harper J.W., Weissman J.S., Walther T.C.,
RA Farese R.V. Jr.;
RT "Probing the global cellular responses to lipotoxicity caused by saturated
RT fatty acids.";
RL Mol. Cell 74:32-44(2019).
CC -!- FUNCTION: Converts glycerol-3-phosphate to 1-acyl-sn-glycerol-3-
CC phosphate (lysophosphatidic acid or LPA) by incorporating an acyl
CC moiety at the sn-1 position of the glycerol backbone (PubMed:17170135).
CC Also converts LPA into 1,2-diacyl-sn-glycerol-3-phosphate (phosphatidic
CC acid or PA) by incorporating an acyl moiety at the sn-2 position of the
CC glycerol backbone (PubMed:19318427). Protects cells against
CC lipotoxicity (PubMed:30846318). {ECO:0000269|PubMed:17170135,
CC ECO:0000269|PubMed:19318427, ECO:0000269|PubMed:30846318}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an acyl-CoA + sn-glycerol 3-phosphate = a 1-acyl-sn-glycero-3-
CC phosphate + CoA; Xref=Rhea:RHEA:15325, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57597, ChEBI:CHEBI:57970, ChEBI:CHEBI:58342; EC=2.3.1.15;
CC Evidence={ECO:0000269|PubMed:17170135};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15326;
CC Evidence={ECO:0000305|PubMed:17170135};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-acyl-sn-glycero-3-phosphate + an acyl-CoA = a 1,2-diacyl-
CC sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:19709,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57970, ChEBI:CHEBI:58342,
CC ChEBI:CHEBI:58608; EC=2.3.1.51;
CC Evidence={ECO:0000269|PubMed:19318427};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19710;
CC Evidence={ECO:0000305|PubMed:19318427};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dodecanoyl-CoA + sn-glycerol 3-phosphate = 1-dodecanoyl-sn-
CC glycerol 3-phosphate + CoA; Xref=Rhea:RHEA:35727, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57375, ChEBI:CHEBI:57597, ChEBI:CHEBI:72682;
CC Evidence={ECO:0000269|PubMed:17170135};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35728;
CC Evidence={ECO:0000305|PubMed:17170135};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=hexadecanoyl-CoA + sn-glycerol 3-phosphate = 1-hexadecanoyl-
CC sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:35723,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57379, ChEBI:CHEBI:57518,
CC ChEBI:CHEBI:57597; Evidence={ECO:0000269|PubMed:17170135};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35724;
CC Evidence={ECO:0000305|PubMed:17170135};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + sn-glycerol 3-phosphate = 1-(9Z-
CC octadecenoyl)-sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:37199,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57387, ChEBI:CHEBI:57597,
CC ChEBI:CHEBI:74544; Evidence={ECO:0000269|PubMed:17170135};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37200;
CC Evidence={ECO:0000305|PubMed:17170135};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z)-octadecadienoyl-CoA + sn-glycerol 3-phosphate = 1-
CC (9Z,12Z)-octadecadienoyl-sn-glycero-3-phosphate + CoA;
CC Xref=Rhea:RHEA:37203, ChEBI:CHEBI:57287, ChEBI:CHEBI:57383,
CC ChEBI:CHEBI:57597, ChEBI:CHEBI:74547;
CC Evidence={ECO:0000269|PubMed:17170135};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37204;
CC Evidence={ECO:0000305|PubMed:17170135};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 1-tetradecanoyl-sn-glycerol 3-
CC phosphate = 1-tetradecanoyl-2-(9Z)-octadecenoyl-sn-glycero-3-
CC phosphate + CoA; Xref=Rhea:RHEA:37187, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57387, ChEBI:CHEBI:72683, ChEBI:CHEBI:74586;
CC Evidence={ECO:0000269|PubMed:19318427};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37188;
CC Evidence={ECO:0000305|PubMed:19318427};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 1-hexadecanoyl-sn-glycero-3-phosphate
CC = 1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphate + CoA;
CC Xref=Rhea:RHEA:33187, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387,
CC ChEBI:CHEBI:57518, ChEBI:CHEBI:64839;
CC Evidence={ECO:0000269|PubMed:19318427};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33188;
CC Evidence={ECO:0000305|PubMed:19318427};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 1-(9Z-octadecenoyl)-sn-glycero-3-
CC phosphate = 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphate + CoA;
CC Xref=Rhea:RHEA:37131, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387,
CC ChEBI:CHEBI:74544, ChEBI:CHEBI:74546;
CC Evidence={ECO:0000269|PubMed:19318427};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37132;
CC Evidence={ECO:0000305|PubMed:19318427};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 1-(6Z,9Z,12Z-octadecatrienoyl)-sn-
CC glycero-3-phosphate = (6Z,9Z,12Z)-octadecatrienoyl-2-(9Z)-
CC octadecenoyl-sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:37179,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57387, ChEBI:CHEBI:74581,
CC ChEBI:CHEBI:74582; Evidence={ECO:0000269|PubMed:19318427};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37180;
CC Evidence={ECO:0000305|PubMed:19318427};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 1-(9Z,12Z,15Z)-octadecatrienoyl-sn-
CC glycero-3-phosphate = 1-(9Z,12Z,15Z)-octadecatrienoyl-2-(9Z)-
CC octadecenoyl-sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:37139,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57387, ChEBI:CHEBI:74549,
CC ChEBI:CHEBI:74550; Evidence={ECO:0000269|PubMed:19318427};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37140;
CC Evidence={ECO:0000305|PubMed:19318427};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphate + tetradecanoyl-CoA
CC = 1-(9Z)-octadecenoyl-2-tetradecanoyl-sn-glycero-3-phosphate + CoA;
CC Xref=Rhea:RHEA:37171, ChEBI:CHEBI:57287, ChEBI:CHEBI:57385,
CC ChEBI:CHEBI:74544, ChEBI:CHEBI:74579;
CC Evidence={ECO:0000269|PubMed:19318427};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37172;
CC Evidence={ECO:0000305|PubMed:19318427};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphate + hexadecanoyl-CoA
CC = 1-(9Z)-octadecenoyl-2-hexadecanoyl-sn-glycero-3-phosphate + CoA;
CC Xref=Rhea:RHEA:37143, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379,
CC ChEBI:CHEBI:74544, ChEBI:CHEBI:74551;
CC Evidence={ECO:0000269|PubMed:19318427};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37144;
CC Evidence={ECO:0000305|PubMed:19318427};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphate + octadecanoyl-CoA
CC = 1-(9Z-octadecenoyl)-2-octadecanoyl-sn-glycero-3-phosphate + CoA;
CC Xref=Rhea:RHEA:37147, ChEBI:CHEBI:57287, ChEBI:CHEBI:57394,
CC ChEBI:CHEBI:74544, ChEBI:CHEBI:74552;
CC Evidence={ECO:0000269|PubMed:19318427};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37148;
CC Evidence={ECO:0000305|PubMed:19318427};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z)-octadecadienoyl-CoA + 1-(9Z-octadecenoyl)-sn-glycero-
CC 3-phosphate = 1-(9Z)-octadecenoyl-2-(9Z,12Z)-octadecadienoyl-sn-
CC glycero-3-phosphate + CoA; Xref=Rhea:RHEA:37159, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57383, ChEBI:CHEBI:74544, ChEBI:CHEBI:74563;
CC Evidence={ECO:0000269|PubMed:19318427};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37160;
CC Evidence={ECO:0000305|PubMed:19318427};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 1-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-
CC glycero-3-phosphate = 1-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-2-(9Z)-
CC octadecenoyl-sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:37455,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57387, ChEBI:CHEBI:74938,
CC ChEBI:CHEBI:74941; Evidence={ECO:0000269|PubMed:19318427};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37456;
CC Evidence={ECO:0000305|PubMed:19318427};
CC -!- ACTIVITY REGULATION: Inhibited by N-ethylmaleimide (NEM).
CC {ECO:0000269|PubMed:17170135}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=9.2 uM for 1-oleoyl-lysophosphatidic acid
CC {ECO:0000269|PubMed:19318427};
CC KM=60 uM for 1-oleoyl-CoA {ECO:0000269|PubMed:19318427};
CC Vmax=14.19 nmol/min/mg enzyme for 1-oleoyl-lysophosphatidic acid
CC {ECO:0000269|PubMed:19318427};
CC Vmax=2.7 nmol/min/mg enzyme for 1-oleoyl-CoA
CC {ECO:0000269|PubMed:19318427};
CC -!- PATHWAY: Glycerolipid metabolism; triacylglycerol biosynthesis.
CC -!- PATHWAY: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-
CC diacylglycerol from sn-glycerol 3-phosphate: step 1/3.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:17002884, ECO:0000269|PubMed:19318427}; Multi-pass
CC membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Widely expressed. Expressed in liver, kidney,
CC testis, brain, heart, skeletal muscle, thyroid, prostate, thymus and
CC placenta. Also expressed lung and adipose tissue.
CC {ECO:0000269|PubMed:17002884, ECO:0000269|PubMed:17170135,
CC ECO:0000269|PubMed:19318427}.
CC -!- DOMAIN: The HXXXXD motif is essential for acyltransferase activity and
CC may constitute the binding site for the phosphate moiety of the
CC glycerol-3-phosphate. {ECO:0000250|UniProtKB:Q9D517}.
CC -!- SIMILARITY: Belongs to the 1-acyl-sn-glycerol-3-phosphate
CC acyltransferase family. {ECO:0000305}.
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DR EMBL; DQ324782; ABC55674.1; -; mRNA.
DR EMBL; DQ345298; ABC70186.1; -; mRNA.
DR EMBL; AY358100; AAQ88467.1; -; mRNA.
DR EMBL; AK055749; BAB71002.1; -; mRNA.
DR EMBL; AK223543; BAD97263.1; -; mRNA.
DR EMBL; BC073136; AAH73136.1; -; mRNA.
DR EMBL; BC090956; AAH90956.1; -; mRNA.
DR EMBL; AB075872; BAD38654.1; -; mRNA.
DR CCDS; CCDS3606.1; -.
DR RefSeq; NP_001243350.1; NM_001256421.1.
DR RefSeq; NP_001243351.1; NM_001256422.1.
DR RefSeq; NP_116106.2; NM_032717.4.
DR RefSeq; XP_016864270.1; XM_017008781.1.
DR AlphaFoldDB; Q53EU6; -.
DR BioGRID; 124267; 138.
DR IntAct; Q53EU6; 9.
DR MINT; Q53EU6; -.
DR STRING; 9606.ENSP00000482571; -.
DR ChEMBL; CHEMBL4523318; -.
DR SwissLipids; SLP:000000290; -.
DR iPTMnet; Q53EU6; -.
DR PhosphoSitePlus; Q53EU6; -.
DR BioMuta; GPAT3; -.
DR DMDM; 150403919; -.
DR EPD; Q53EU6; -.
DR jPOST; Q53EU6; -.
DR MassIVE; Q53EU6; -.
DR MaxQB; Q53EU6; -.
DR PaxDb; Q53EU6; -.
DR PeptideAtlas; Q53EU6; -.
DR PRIDE; Q53EU6; -.
DR ProteomicsDB; 62449; -.
DR Antibodypedia; 25231; 214 antibodies from 27 providers.
DR DNASU; 84803; -.
DR Ensembl; ENST00000264409.5; ENSP00000264409.4; ENSG00000138678.11.
DR Ensembl; ENST00000395226.6; ENSP00000378651.2; ENSG00000138678.11.
DR Ensembl; ENST00000611707.4; ENSP00000482571.1; ENSG00000138678.11.
DR GeneID; 84803; -.
DR KEGG; hsa:84803; -.
DR MANE-Select; ENST00000264409.5; ENSP00000264409.4; NM_032717.5; NP_116106.2.
DR UCSC; uc003how.5; human.
DR CTD; 84803; -.
DR DisGeNET; 84803; -.
DR GeneCards; GPAT3; -.
DR HGNC; HGNC:28157; GPAT3.
DR HPA; ENSG00000138678; Tissue enhanced (kidney).
DR MIM; 610958; gene.
DR neXtProt; NX_Q53EU6; -.
DR OpenTargets; ENSG00000138678; -.
DR PharmGKB; PA162375888; -.
DR VEuPathDB; HostDB:ENSG00000138678; -.
DR eggNOG; KOG2898; Eukaryota.
DR GeneTree; ENSGT01030000234574; -.
DR HOGENOM; CLU_031080_0_1_1; -.
DR InParanoid; Q53EU6; -.
DR OMA; YMRILVK; -.
DR OrthoDB; 526132at2759; -.
DR PhylomeDB; Q53EU6; -.
DR TreeFam; TF315039; -.
DR BRENDA; 2.3.1.15; 2681.
DR PathwayCommons; Q53EU6; -.
DR Reactome; R-HSA-1483166; Synthesis of PA.
DR SABIO-RK; Q53EU6; -.
DR SignaLink; Q53EU6; -.
DR UniPathway; UPA00282; -.
DR UniPathway; UPA00557; UER00612.
DR BioGRID-ORCS; 84803; 5 hits in 1063 CRISPR screens.
DR ChiTaRS; GPAT3; human.
DR GeneWiki; AGPAT9; -.
DR GenomeRNAi; 84803; -.
DR Pharos; Q53EU6; Tbio.
DR PRO; PR:Q53EU6; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; Q53EU6; protein.
DR Bgee; ENSG00000138678; Expressed in kidney epithelium and 176 other tissues.
DR ExpressionAtlas; Q53EU6; baseline and differential.
DR Genevisible; Q53EU6; HS.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0003841; F:1-acylglycerol-3-phosphate O-acyltransferase activity; IDA:UniProtKB.
DR GO; GO:0004366; F:glycerol-3-phosphate O-acyltransferase activity; IDA:UniProtKB.
DR GO; GO:0102420; F:sn-1-glycerol-3-phosphate C16:0-DCA-CoA acyl transferase activity; IEA:UniProtKB-EC.
DR GO; GO:0016024; P:CDP-diacylglycerol biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006072; P:glycerol-3-phosphate metabolic process; IEA:Ensembl.
DR GO; GO:0006654; P:phosphatidic acid biosynthetic process; TAS:Reactome.
DR GO; GO:0032006; P:regulation of TOR signaling; IDA:UniProtKB.
DR GO; GO:0019432; P:triglyceride biosynthetic process; IDA:UniProtKB.
DR CDD; cd07991; LPLAT_LPCAT1-like; 1.
DR InterPro; IPR045252; LPCAT1-like.
DR InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR Pfam; PF01553; Acyltransferase; 1.
DR SMART; SM00563; PlsC; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Endoplasmic reticulum; Lipid biosynthesis;
KW Lipid metabolism; Membrane; Phospholipid biosynthesis;
KW Phospholipid metabolism; Phosphoprotein; Reference proteome; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..434
FT /note="Glycerol-3-phosphate acyltransferase 3"
FT /id="PRO_0000291570"
FT TRANSMEM 14..34
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 137..157
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 161..181
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOTIF 229..234
FT /note="HXXXXD motif"
FT /evidence="ECO:0000250|UniProtKB:Q9D517"
FT MOD_RES 68
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 77
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT CONFLICT 156
FT /note="L -> I (in Ref. 5; BAD97263)"
FT /evidence="ECO:0000305"
SQ 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
