PLCC_MOUSE
ID PLCC_MOUSE Reviewed; 376 AA.
AC Q9D517; C4B4E7; Q7TT39; Q8BST2;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 2.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=1-acyl-sn-glycerol-3-phosphate acyltransferase gamma;
DE EC=2.3.1.51 {ECO:0000269|PubMed:15367102, ECO:0000269|PubMed:19114731};
DE AltName: Full=1-acylglycerol-3-phosphate O-acyltransferase 3;
DE Short=1-AGP acyltransferase 3;
DE Short=1-AGPAT 3;
DE AltName: Full=Lysophosphatidic acid acyltransferase gamma;
DE Short=LPAAT-gamma;
GN Name=Agpat3 {ECO:0000312|MGI:MGI:1336186};
GN Synonyms=Lpaat3 {ECO:0000303|PubMed:19114731};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, TISSUE
RP SPECIFICITY, AND INDUCTION.
RC STRAIN=C57BL/6J;
RX PubMed=15367102; DOI=10.1042/bj20041348;
RA Lu B., Jiang Y.J., Zhou Y., Xu F.Y., Hatch G.M., Choy P.C.;
RT "Cloning and characterization of murine 1-acyl-sn-glycerol 3-phosphate
RT acyltransferases and their regulation by PPARalpha in murine heart.";
RL Biochem. J. 385:469-477(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, TISSUE
RP SPECIFICITY, SUBCELLULAR LOCATION, BIOPHYSICOCHEMICAL PROPERTIES,
RP MUTAGENESIS OF HIS-96; ASP-101 AND GLU-176, ACTIVITY REGULATION, AND MOTIF
RP HXXXXD.
RX PubMed=19114731; DOI=10.1194/jlr.m800468-jlr200;
RA Yuki K., Shindou H., Hishikawa D., Shimizu T.;
RT "Characterization of mouse lysophosphatidic acid acyltransferase 3: an
RT enzyme with dual functions in the testis.";
RL J. Lipid Res. 50:860-869(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Head, Liver, Pituitary, and Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryonic brain;
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 [6]
RP PROTEIN SEQUENCE OF 237-248, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Converts 1-acyl-sn-glycerol-3-phosphate (lysophosphatidic
CC acid or LPA) into 1,2-diacyl-sn-glycerol-3-phosphate (phosphatidic acid
CC or PA) by incorporating an acyl moiety at the sn-2 position of the
CC glycerol backbone (PubMed:15367102). Acts on LPA containing saturated
CC or unsaturated fatty acids C16:0-C20:4 at the sn-1 position using
CC C18:1, C20:4 or C18:2-CoA as the acyl donor (By similarity). Also acts
CC on lysophosphatidylcholine, lysophosphatidylinositol and
CC lysophosphatidylserine using C18:1 or C20:4-CoA (By similarity). Has a
CC preference for arachidonoyl-CoA as a donor (PubMed:19114731). Has also
CC a modest lysophosphatidylinositol acyltransferase (LPIAT) activity,
CC converts lysophosphatidylinositol (LPI) into phosphatidylinositol
CC (PubMed:19114731). {ECO:0000250|UniProtKB:Q9NRZ7,
CC ECO:0000269|PubMed:15367102, ECO:0000269|PubMed:19114731}.
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:15367102, ECO:0000269|PubMed:19114731};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19710;
CC Evidence={ECO:0000305|PubMed:15367102, ECO:0000305|PubMed:19114731};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphate + pentadecanoyl-CoA
CC = 1-(9Z)-octadecenoyl-2-pentadecanoyl-sn-glycero-3-phosphate + CoA;
CC Xref=Rhea:RHEA:37175, ChEBI:CHEBI:57287, ChEBI:CHEBI:74309,
CC ChEBI:CHEBI:74544, ChEBI:CHEBI:74578;
CC Evidence={ECO:0000250|UniProtKB:Q9NRZ7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37176;
CC Evidence={ECO:0000250|UniProtKB:Q9NRZ7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphate + heptadecanoyl-CoA
CC = 1-(9Z)-octadecenoyl-2-heptadecanoyl-sn-glycero-3-phosphate + CoA;
CC Xref=Rhea:RHEA:37155, ChEBI:CHEBI:57287, ChEBI:CHEBI:74307,
CC ChEBI:CHEBI:74544, ChEBI:CHEBI:74558;
CC Evidence={ECO:0000250|UniProtKB:Q9NRZ7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37156;
CC Evidence={ECO:0000250|UniProtKB:Q9NRZ7};
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:0000250|UniProtKB:Q9NRZ7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37148;
CC Evidence={ECO:0000250|UniProtKB:Q9NRZ7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphate + nonadecanoyl-CoA
CC = 1-(9Z)-octadecenoyl-2-nonadecanoyl-sn-glycero-3-phosphate + CoA;
CC Xref=Rhea:RHEA:37595, ChEBI:CHEBI:57287, ChEBI:CHEBI:74544,
CC ChEBI:CHEBI:75104, ChEBI:CHEBI:75105;
CC Evidence={ECO:0000250|UniProtKB:Q9NRZ7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37596;
CC Evidence={ECO:0000250|UniProtKB:Q9NRZ7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + 1-(9Z-octadecenoyl)-sn-
CC glycero-3-phosphate = 1-(9Z)-octadecenoyl-2-(5Z,8Z,11Z,14Z)-
CC eicosatetraenoyl-sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:37443,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57368, ChEBI:CHEBI:74544,
CC ChEBI:CHEBI:74928; Evidence={ECO:0000269|PubMed:19114731};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37444;
CC Evidence={ECO:0000305|PubMed:19114731};
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:0000250|UniProtKB:Q9NRZ7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37132;
CC Evidence={ECO:0000250|UniProtKB:Q9NRZ7};
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:0000250|UniProtKB:Q9NRZ7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37160;
CC Evidence={ECO:0000250|UniProtKB:Q9NRZ7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + 1-(9Z-octadecenoyl)-sn-
CC glycero-3-phosphocholine = 1-(9Z)-octadecenoyl-2-(5Z,8Z,11Z,14Z)-
CC icosatetraenoyl-sn-glycero-3-phosphocholine + CoA;
CC Xref=Rhea:RHEA:37395, ChEBI:CHEBI:28610, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57368, ChEBI:CHEBI:74671;
CC Evidence={ECO:0000250|UniProtKB:Q9NRZ7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37396;
CC Evidence={ECO:0000250|UniProtKB:Q9NRZ7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + 1-(9Z-octadecenoyl)-sn-
CC glycero-3-phospho-(1D-myo-inositol) = 1-(9Z-octadecenoyl)-2-
CC (5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phospho-1D-myo-inositol
CC + CoA; Xref=Rhea:RHEA:42216, ChEBI:CHEBI:57287, ChEBI:CHEBI:57368,
CC ChEBI:CHEBI:78762, ChEBI:CHEBI:78765;
CC Evidence={ECO:0000250|UniProtKB:Q9NRZ7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42217;
CC Evidence={ECO:0000250|UniProtKB:Q9NRZ7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + 1-(9Z-octadecenoyl)-sn-
CC glycero-3-phospho-L-serine = 1-(9Z-octadecenoyl)-2-(5Z,8Z,11Z,14Z-
CC eicosatetraenoyl)-sn-glycero-3-phospho-L-serine + CoA;
CC Xref=Rhea:RHEA:37379, ChEBI:CHEBI:57287, ChEBI:CHEBI:57368,
CC ChEBI:CHEBI:74617, ChEBI:CHEBI:74897;
CC Evidence={ECO:0000250|UniProtKB:Q9NRZ7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37380;
CC Evidence={ECO:0000250|UniProtKB:Q9NRZ7};
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:19114731};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33188;
CC Evidence={ECO:0000305|PubMed:19114731};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + 1-hexadecanoyl-sn-
CC glycero-3-phosphate = 1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-
CC eicosatetraenoyl)-sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:35915,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57368, ChEBI:CHEBI:57518,
CC ChEBI:CHEBI:72864; Evidence={ECO:0000269|PubMed:19114731};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35916;
CC Evidence={ECO:0000305|PubMed:19114731};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + 1-heptadecanoyl-sn-
CC glycero-3-phosphate = 1-heptadecanoyl-2-(5Z,8Z,11Z,14Z)-
CC eicosatetraenoyl-sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:42220,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57368, ChEBI:CHEBI:74554,
CC ChEBI:CHEBI:78768; Evidence={ECO:0000250|UniProtKB:Q9NRZ7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42221;
CC Evidence={ECO:0000250|UniProtKB:Q9NRZ7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 1-octadecanoyl-sn-glycero-3-phosphate
CC = 1-octadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphate + CoA;
CC Xref=Rhea:RHEA:37163, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387,
CC ChEBI:CHEBI:74560, ChEBI:CHEBI:74565;
CC Evidence={ECO:0000250|UniProtKB:Q9NRZ7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37164;
CC Evidence={ECO:0000250|UniProtKB:Q9NRZ7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + 1-octadecanoyl-sn-
CC glycero-3-phosphate = 1-octadecanoyl-2-(5Z,8Z,11Z,14Z-
CC eicosatetraenoyl)-sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:42588,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57368, ChEBI:CHEBI:74565,
CC ChEBI:CHEBI:77091; Evidence={ECO:0000269|PubMed:19114731};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42589;
CC Evidence={ECO:0000305|PubMed:19114731};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphate + hexadecanoyl-CoA
CC = 1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphate + CoA;
CC Xref=Rhea:RHEA:42592, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379,
CC ChEBI:CHEBI:64839, ChEBI:CHEBI:74544;
CC Evidence={ECO:0000250|UniProtKB:Q9NRZ7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42593;
CC Evidence={ECO:0000250|UniProtKB:Q9NRZ7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + 1-O-(9Z-octadecenyl)-
CC sn-glycero-3-phosphate = 1-O-(9Z-octadecenyl)-2-(5Z,8Z,11Z,14Z-
CC eicosatetraenoyl)-sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:45404,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57368, ChEBI:CHEBI:78402,
CC ChEBI:CHEBI:85231; Evidence={ECO:0000269|PubMed:19114731};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45405;
CC Evidence={ECO:0000305|PubMed:19114731};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + a 1-acyl-sn-glycero-3-
CC phospho-(1D-myo-inositol) = a 1-acyl-2-(5Z,8Z,11Z,14Z-
CC eicosatetraenoyl)-sn-glycero-3-phospho-(1D-myo-inositol) + CoA;
CC Xref=Rhea:RHEA:37015, ChEBI:CHEBI:57287, ChEBI:CHEBI:57368,
CC ChEBI:CHEBI:64771, ChEBI:CHEBI:75243;
CC Evidence={ECO:0000269|PubMed:19114731};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37016;
CC Evidence={ECO:0000305|PubMed:19114731};
CC -!- ACTIVITY REGULATION: In males, activity increases in an age-dependent
CC fashion, maybe derived from the induction by sex-hormones.
CC {ECO:0000269|PubMed:19114731}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=15.9 uM for arachidonoyl-CoA {ECO:0000269|PubMed:19114731};
CC KM=26.3 uM for palmitoyl-LPA {ECO:0000269|PubMed:19114731};
CC Vmax=50.4 nmol/min/mg enzyme toward arachidonoyl-CoA
CC {ECO:0000269|PubMed:19114731};
CC Vmax=21.8 nmol/min/mg enzyme toward palmitoyl-LPA
CC {ECO:0000269|PubMed:19114731};
CC -!- PATHWAY: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-
CC diacylglycerol from sn-glycerol 3-phosphate: step 2/3.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:19114731}; Multi-pass membrane protein
CC {ECO:0000255}. Nucleus envelope {ECO:0000250|UniProtKB:Q9NRZ7}.
CC -!- TISSUE SPECIFICITY: Widely expressed. Mainly expressed in testis,
CC kidney and liver (at protein level). {ECO:0000269|PubMed:19114731}.
CC -!- INDUCTION: Up-regulated in the heart by clofibrate, a PPAR-alpha
CC agonist. {ECO:0000269|PubMed:15367102}.
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:0000305|PubMed:19114731}.
CC -!- SIMILARITY: Belongs to the 1-acyl-sn-glycerol-3-phosphate
CC acyltransferase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC27043.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY167588; AAN75574.1; -; mRNA.
DR EMBL; AB377215; BAH59614.1; -; mRNA.
DR EMBL; AK015906; BAB30025.2; -; mRNA.
DR EMBL; AK030607; BAC27043.1; ALT_INIT; mRNA.
DR EMBL; AK075715; BAC35905.1; -; mRNA.
DR EMBL; AK076414; BAC36329.1; -; mRNA.
DR EMBL; CH466553; EDL31738.1; -; Genomic_DNA.
DR EMBL; CH466553; EDL31739.1; -; Genomic_DNA.
DR EMBL; CH466553; EDL31740.1; -; Genomic_DNA.
DR EMBL; CH466553; EDL31742.1; -; Genomic_DNA.
DR EMBL; BC052382; AAH52382.1; -; mRNA.
DR EMBL; BC058519; AAH58519.1; -; mRNA.
DR CCDS; CCDS23963.1; -.
DR RefSeq; NP_443747.2; NM_053014.3.
DR RefSeq; XP_006513779.1; XM_006513716.2.
DR RefSeq; XP_006513780.1; XM_006513717.3.
DR RefSeq; XP_006513781.1; XM_006513718.1.
DR RefSeq; XP_006513782.1; XM_006513719.2.
DR RefSeq; XP_006513783.1; XM_006513720.1.
DR RefSeq; XP_006513784.1; XM_006513721.1.
DR RefSeq; XP_006513785.1; XM_006513722.3.
DR RefSeq; XP_006513786.1; XM_006513723.3.
DR AlphaFoldDB; Q9D517; -.
DR SMR; Q9D517; -.
DR BioGRID; 205803; 3.
DR STRING; 10090.ENSMUSP00000101028; -.
DR SwissLipids; SLP:000000097; -.
DR iPTMnet; Q9D517; -.
DR PhosphoSitePlus; Q9D517; -.
DR SwissPalm; Q9D517; -.
DR EPD; Q9D517; -.
DR jPOST; Q9D517; -.
DR MaxQB; Q9D517; -.
DR PaxDb; Q9D517; -.
DR PeptideAtlas; Q9D517; -.
DR PRIDE; Q9D517; -.
DR ProteomicsDB; 289922; -.
DR Antibodypedia; 24081; 171 antibodies from 26 providers.
DR DNASU; 28169; -.
DR Ensembl; ENSMUST00000001240; ENSMUSP00000001240; ENSMUSG00000001211.
DR Ensembl; ENSMUST00000105387; ENSMUSP00000101026; ENSMUSG00000001211.
DR Ensembl; ENSMUST00000105388; ENSMUSP00000101027; ENSMUSG00000001211.
DR Ensembl; ENSMUST00000105389; ENSMUSP00000101028; ENSMUSG00000001211.
DR Ensembl; ENSMUST00000105390; ENSMUSP00000101029; ENSMUSG00000001211.
DR Ensembl; ENSMUST00000166360; ENSMUSP00000132954; ENSMUSG00000001211.
DR GeneID; 28169; -.
DR KEGG; mmu:28169; -.
DR UCSC; uc007fxo.1; mouse.
DR CTD; 56894; -.
DR MGI; MGI:1336186; Agpat3.
DR VEuPathDB; HostDB:ENSMUSG00000001211; -.
DR eggNOG; KOG1505; Eukaryota.
DR GeneTree; ENSGT00950000182836; -.
DR HOGENOM; CLU_041844_5_2_1; -.
DR InParanoid; Q9D517; -.
DR OMA; WPTWLIS; -.
DR OrthoDB; 959325at2759; -.
DR PhylomeDB; Q9D517; -.
DR TreeFam; TF314065; -.
DR BRENDA; 2.3.1.51; 3474.
DR Reactome; R-MMU-1483166; Synthesis of PA.
DR Reactome; R-MMU-6811436; COPI-independent Golgi-to-ER retrograde traffic.
DR SABIO-RK; Q9D517; -.
DR UniPathway; UPA00557; UER00613.
DR BioGRID-ORCS; 28169; 3 hits in 74 CRISPR screens.
DR ChiTaRS; Agpat3; mouse.
DR PRO; PR:Q9D517; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q9D517; protein.
DR Bgee; ENSMUSG00000001211; Expressed in retinal neural layer and 266 other tissues.
DR ExpressionAtlas; Q9D517; baseline and differential.
DR Genevisible; Q9D517; MM.
DR GO; GO:0012505; C:endomembrane system; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005635; C:nuclear envelope; ISS:UniProtKB.
DR GO; GO:0003841; F:1-acylglycerol-3-phosphate O-acyltransferase activity; ISS:UniProtKB.
DR GO; GO:0016746; F:acyltransferase activity; IBA:GO_Central.
DR GO; GO:0042171; F:lysophosphatidic acid acyltransferase activity; IDA:MGI.
DR GO; GO:0016024; P:CDP-diacylglycerol biosynthetic process; IEA:UniProtKB-UniPathway.
DR InterPro; IPR032098; Acyltransf_C.
DR InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR Pfam; PF16076; Acyltransf_C; 1.
DR Pfam; PF01553; Acyltransferase; 1.
DR SMART; SM00563; PlsC; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Direct protein sequencing; Endoplasmic reticulum;
KW Lipid biosynthesis; Lipid metabolism; Membrane; Nucleus;
KW Phospholipid biosynthesis; Phospholipid metabolism; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..376
FT /note="1-acyl-sn-glycerol-3-phosphate acyltransferase
FT gamma"
FT /id="PRO_0000208195"
FT TOPO_DOM 1..124
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q9NRZ7"
FT TRANSMEM 125..145
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 146..316
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q9NRZ7"
FT TRANSMEM 317..339
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 340..376
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q9NRZ7"
FT MOTIF 96..101
FT /note="HXXXXD motif"
FT /evidence="ECO:0000305|PubMed:19114731"
FT MUTAGEN 96
FT /note="H->A: Loss of LPA acyltransferase and LPI
FT acyltransferase activities."
FT /evidence="ECO:0000269|PubMed:19114731"
FT MUTAGEN 101
FT /note="D->A: Loss of LPA acyltransferase and LPI
FT acyltransferase activities."
FT /evidence="ECO:0000269|PubMed:19114731"
FT MUTAGEN 176
FT /note="E->A: Loss of LPA acyltransferase and LPI
FT acyltransferase activities."
FT /evidence="ECO:0000269|PubMed:19114731"
FT CONFLICT 21
FT /note="F -> V (in Ref. 5; AAH52382/AAH58519)"
FT /evidence="ECO:0000305"
FT CONFLICT 249
FT /note="Y -> N (in Ref. 3; BAC27043)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 376 AA; 43296 MW; 6F8C8970404B2EC1 CRC64;
MGLLAYLKTQ FVVHLLIGFV FVVSGLIINF TQLCTLALWP ISKHLYRRIN CRLAYSLWSQ
LVMLLEWWSC TECTLFTDQA TVDHFGKEHV VVILNHNFEI DFLCGWTMCE RFGVLGSSKV
LAKRELLCVP LIGWTWYFLE IVFCKRKWEE DRDTVIEGLR RLADYPEYMW FLLYCEGTRF
TETKHRISME VAASKGLPPL KYHLLPRTKG FTTAVQCLRG TVAAIYDVTL NFRGNKNPSL
LGILYGKKYE ADMCVRRFPL EDIPADETSA AQWLHKLYQE KDALQEMYKQ KGVFPGEQFK
PARRPWTLLN FLCWATILLS PLFSFVLGVF ASGSPLLILT FLGFVGAASF GVRRLIGVTE
IEKGSSYGNQ ELKKKE
