PLCC_HUMAN
ID PLCC_HUMAN Reviewed; 376 AA.
AC Q9NRZ7; D3DSL2; Q3ZCU2; Q6UWP6; Q6ZUC6; Q8N3Q7; Q9NRZ6;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=1-acyl-sn-glycerol-3-phosphate acyltransferase gamma;
DE EC=2.3.1.51 {ECO:0000269|PubMed:21173190};
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; Synonyms=LPAAT3; ORFNames=UNQ759/PRO1490;
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] (ISOFORMS 1 AND 2).
RX PubMed=11487472; DOI=10.2741/leung;
RA Leung D.W.;
RT "The structure and functions of human lysophosphatidic acid
RT acyltransferases.";
RL Front. Biosci. 6:D944-D953(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Fetal liver;
RA Nagamine K., Kudoh J., Minoshima S., Kawasaki K., Hase T., Shimizu N.;
RT "Isolation of a novel gene encoding 1-acylglycerol-3-phosphate O-
RT acyltransferase 3 (AGPAT3) from the human chromosome 21q22.3.";
RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 GENOMIC DNA].
RX PubMed=10830953; DOI=10.1038/35012518;
RA Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T., Park H.-S.,
RA Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y., Soeda E., Ohki M.,
RA Takagi T., Sakaki Y., Taudien S., Blechschmidt K., Polley A., Menzel U.,
RA Delabar J., Kumpf K., Lehmann R., Patterson D., Reichwald K., Rump A.,
RA Schillhabel M., Schudy A., Zimmermann W., Rosenthal A., Kudoh J.,
RA Shibuya K., Kawasaki K., Asakawa S., Shintani A., Sasaki T., Nagamine K.,
RA Mitsuyama S., Antonarakis S.E., Minoshima S., Shimizu N., Nordsiek G.,
RA Hornischer K., Brandt P., Scharfe M., Schoen O., Desario A., Reichelt J.,
RA Kauer G., Bloecker H., Ramser J., Beck A., Klages S., Hennig S.,
RA Riesselmann L., Dagand E., Wehrmeyer S., Borzym K., Gardiner K.,
RA Nizetic D., Francis F., Lehrach H., Reinhardt R., Yaspo M.-L.;
RT "The DNA sequence of human chromosome 21.";
RL Nature 405:311-319(2000).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, Skin, 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 1-372 (ISOFORM 3).
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 [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 70-376.
RC TISSUE=Melanoma;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [9]
RP SUBCELLULAR LOCATION, AND MEMBRANE TOPOLOGY.
RX PubMed=20537980; DOI=10.1016/j.bbrc.2010.05.149;
RA Schmidt J.A., Yvone G.M., Brown W.J.;
RT "Membrane topology of human AGPAT3 (LPAAT3).";
RL Biochem. Biophys. Res. Commun. 397:661-667(2010).
RN [10]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=21173190; DOI=10.1194/jlr.m007575;
RA Prasad S.S., Garg A., Agarwal A.K.;
RT "Enzymatic activities of the human AGPAT isoform 3 and isoform 5:
RT localization of AGPAT5 to mitochondria.";
RL J. Lipid Res. 52:451-462(2011).
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:21173190). 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 (PubMed:21173190). Also
CC acts on lysophosphatidylcholine, lysophosphatidylinositol and
CC lysophosphatidylserine using C18:1 or C20:4-CoA (PubMed:21173190). Has
CC a preference for arachidonoyl-CoA as a donor (By similarity). Has also
CC a modest lysophosphatidylinositol acyltransferase (LPIAT) activity,
CC converts lysophosphatidylinositol (LPI) into phosphatidylinositol (By
CC similarity). {ECO:0000250|UniProtKB:Q9D517,
CC ECO:0000269|PubMed:21173190}.
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:21173190};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19710;
CC Evidence={ECO:0000305|PubMed:21173190};
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:0000269|PubMed:21173190};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37176;
CC Evidence={ECO:0000305|PubMed:21173190};
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:0000269|PubMed:21173190};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37156;
CC Evidence={ECO:0000305|PubMed:21173190};
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:21173190};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37148;
CC Evidence={ECO:0000305|PubMed:21173190};
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:0000269|PubMed:21173190};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37596;
CC Evidence={ECO:0000305|PubMed:21173190};
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:21173190};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37444;
CC Evidence={ECO:0000305|PubMed:21173190};
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:21173190};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37132;
CC Evidence={ECO:0000305|PubMed:21173190};
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:21173190};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37160;
CC Evidence={ECO:0000305|PubMed:21173190};
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:0000269|PubMed:21173190};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37396;
CC Evidence={ECO:0000305|PubMed:21173190};
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:0000269|PubMed:21173190};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42217;
CC Evidence={ECO:0000305|PubMed:21173190};
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:0000269|PubMed:21173190};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37380;
CC Evidence={ECO:0000305|PubMed:21173190};
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:21173190};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33188;
CC Evidence={ECO:0000305|PubMed:21173190};
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:21173190};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35916;
CC Evidence={ECO:0000305|PubMed:21173190};
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:0000269|PubMed:21173190};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42221;
CC Evidence={ECO:0000305|PubMed:21173190};
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:0000269|PubMed:21173190};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37164;
CC Evidence={ECO:0000305|PubMed:21173190};
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:21173190};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42589;
CC Evidence={ECO:0000305|PubMed:21173190};
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:0000269|PubMed:21173190};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42593;
CC Evidence={ECO:0000305|PubMed:21173190};
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:0000250|UniProtKB:Q9D517};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45405;
CC Evidence={ECO:0000250|UniProtKB:Q9D517};
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:0000250|UniProtKB:Q9D517};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37016;
CC Evidence={ECO:0000250|UniProtKB:Q9D517};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=4.78 uM for LPA sn-1 C18:1 {ECO:0000269|PubMed:21173190};
CC KM=21.53 uM for C18:1-CoA {ECO:0000269|PubMed:21173190};
CC Vmax=6.35 nmol/min/mg enzyme toward LPA sn-1 C18:1
CC {ECO:0000269|PubMed:21173190};
CC Vmax=0.74 nmol/min/mg enzyme toward C18:1-CoA
CC {ECO:0000269|PubMed:21173190};
CC -!- PATHWAY: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-
CC diacylglycerol from sn-glycerol 3-phosphate: step 2/3.
CC -!- INTERACTION:
CC Q9NRZ7; O95870: ABHD16A; NbExp=3; IntAct=EBI-2803601, EBI-348517;
CC Q9NRZ7; Q13520: AQP6; NbExp=3; IntAct=EBI-2803601, EBI-13059134;
CC Q9NRZ7; Q12982: BNIP2; NbExp=3; IntAct=EBI-2803601, EBI-752094;
CC Q9NRZ7; Q96BA8: CREB3L1; NbExp=3; IntAct=EBI-2803601, EBI-6942903;
CC Q9NRZ7; Q8N9E0: FAM133A; NbExp=3; IntAct=EBI-2803601, EBI-10268158;
CC Q9NRZ7; Q6ZVE7: GOLT1A; NbExp=3; IntAct=EBI-2803601, EBI-17231387;
CC Q9NRZ7; Q8NBQ5: HSD17B11; NbExp=3; IntAct=EBI-2803601, EBI-1052304;
CC Q9NRZ7; Q7Z5P4: HSD17B13; NbExp=3; IntAct=EBI-2803601, EBI-18053395;
CC Q9NRZ7; Q5SR56: MFSD14B; NbExp=3; IntAct=EBI-2803601, EBI-373355;
CC Q9NRZ7; Q00013: MPP1; NbExp=3; IntAct=EBI-2803601, EBI-711788;
CC Q9NRZ7; Q6ZUT1: NKAPD1; NbExp=3; IntAct=EBI-2803601, EBI-3920396;
CC Q9NRZ7; Q14973: SLC10A1; NbExp=3; IntAct=EBI-2803601, EBI-3923031;
CC Q9NRZ7; Q9NQQ7-3: SLC35C2; NbExp=3; IntAct=EBI-2803601, EBI-17295964;
CC Q9NRZ7; Q8N9Q2: SREK1IP1; NbExp=3; IntAct=EBI-2803601, EBI-10268630;
CC Q9NRZ7; Q9NUH8: TMEM14B; NbExp=3; IntAct=EBI-2803601, EBI-8638294;
CC Q9NRZ7; Q9NRX6: TMEM167B; NbExp=3; IntAct=EBI-2803601, EBI-17684533;
CC Q9NRZ7; Q9Y320: TMX2; NbExp=3; IntAct=EBI-2803601, EBI-6447886;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:20537980, ECO:0000269|PubMed:21173190}; Multi-pass
CC membrane protein {ECO:0000255}. Nucleus envelope
CC {ECO:0000269|PubMed:21173190}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=Gamma-1;
CC IsoId=Q9NRZ7-1; Sequence=Displayed;
CC Name=2; Synonyms=Gamma-2;
CC IsoId=Q9NRZ7-2; Sequence=VSP_005072;
CC Name=3;
CC IsoId=Q9NRZ7-3; Sequence=VSP_013144;
CC -!- TISSUE SPECIFICITY: Widely expressed with highest levels in testis,
CC pancreas and kidney, followed by spleen, lung, adipose tissue and
CC liver. {ECO:0000269|PubMed:21173190}.
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; AF156774; AAF80336.1; -; mRNA.
DR EMBL; AF156775; AAF80337.1; -; mRNA.
DR EMBL; AB040138; BAB18943.1; -; mRNA.
DR EMBL; AY358704; AAQ89067.1; -; mRNA.
DR EMBL; AP001054; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471079; EAX09461.1; -; Genomic_DNA.
DR EMBL; CH471079; EAX09463.1; -; Genomic_DNA.
DR EMBL; CH471079; EAX09464.1; -; Genomic_DNA.
DR EMBL; CH471079; EAX09465.1; -; Genomic_DNA.
DR EMBL; BC011971; AAH11971.1; -; mRNA.
DR EMBL; BC040603; AAH40603.1; -; mRNA.
DR EMBL; BC063552; AAH63552.1; -; mRNA.
DR EMBL; AK125804; BAC86299.1; -; mRNA.
DR EMBL; AL832919; CAD38635.2; -; mRNA.
DR CCDS; CCDS13703.1; -. [Q9NRZ7-1]
DR RefSeq; NP_001032642.1; NM_001037553.1. [Q9NRZ7-1]
DR RefSeq; NP_064517.1; NM_020132.4. [Q9NRZ7-1]
DR RefSeq; XP_005261217.1; XM_005261160.4. [Q9NRZ7-1]
DR RefSeq; XP_006724092.1; XM_006724029.3. [Q9NRZ7-1]
DR RefSeq; XP_006724093.1; XM_006724030.3. [Q9NRZ7-1]
DR RefSeq; XP_006724094.1; XM_006724031.3. [Q9NRZ7-2]
DR RefSeq; XP_011527967.1; XM_011529665.2. [Q9NRZ7-1]
DR RefSeq; XP_016883898.1; XM_017028409.1.
DR RefSeq; XP_016883899.1; XM_017028410.1.
DR RefSeq; XP_016883900.1; XM_017028411.1. [Q9NRZ7-2]
DR RefSeq; XP_016883901.1; XM_017028412.1. [Q9NRZ7-2]
DR RefSeq; XP_016883902.1; XM_017028413.1.
DR AlphaFoldDB; Q9NRZ7; -.
DR BioGRID; 121224; 98.
DR IntAct; Q9NRZ7; 32.
DR MINT; Q9NRZ7; -.
DR STRING; 9606.ENSP00000381140; -.
DR SwissLipids; SLP:000000823; -.
DR iPTMnet; Q9NRZ7; -.
DR PhosphoSitePlus; Q9NRZ7; -.
DR SwissPalm; Q9NRZ7; -.
DR BioMuta; AGPAT3; -.
DR DMDM; 12643817; -.
DR EPD; Q9NRZ7; -.
DR jPOST; Q9NRZ7; -.
DR MassIVE; Q9NRZ7; -.
DR MaxQB; Q9NRZ7; -.
DR PaxDb; Q9NRZ7; -.
DR PeptideAtlas; Q9NRZ7; -.
DR PRIDE; Q9NRZ7; -.
DR ProteomicsDB; 82447; -. [Q9NRZ7-1]
DR ProteomicsDB; 82448; -. [Q9NRZ7-2]
DR ProteomicsDB; 82449; -. [Q9NRZ7-3]
DR Antibodypedia; 24081; 171 antibodies from 26 providers.
DR DNASU; 56894; -.
DR Ensembl; ENST00000291572.13; ENSP00000291572.8; ENSG00000160216.21. [Q9NRZ7-1]
DR Ensembl; ENST00000327505.6; ENSP00000332989.2; ENSG00000160216.21. [Q9NRZ7-1]
DR Ensembl; ENST00000398058.5; ENSP00000381135.1; ENSG00000160216.21. [Q9NRZ7-1]
DR Ensembl; ENST00000398061.5; ENSP00000381138.1; ENSG00000160216.21. [Q9NRZ7-1]
DR Ensembl; ENST00000398063.6; ENSP00000381140.2; ENSG00000160216.21. [Q9NRZ7-1]
DR Ensembl; ENST00000546158.1; ENSP00000443510.1; ENSG00000160216.21. [Q9NRZ7-1]
DR GeneID; 56894; -.
DR KEGG; hsa:56894; -.
DR MANE-Select; ENST00000291572.13; ENSP00000291572.8; NM_020132.5; NP_064517.1.
DR UCSC; uc002zdv.4; human. [Q9NRZ7-1]
DR CTD; 56894; -.
DR DisGeNET; 56894; -.
DR GeneCards; AGPAT3; -.
DR HGNC; HGNC:326; AGPAT3.
DR HPA; ENSG00000160216; Low tissue specificity.
DR MIM; 614794; gene.
DR neXtProt; NX_Q9NRZ7; -.
DR OpenTargets; ENSG00000160216; -.
DR PharmGKB; PA24623; -.
DR VEuPathDB; HostDB:ENSG00000160216; -.
DR eggNOG; KOG1505; Eukaryota.
DR GeneTree; ENSGT00950000182836; -.
DR InParanoid; Q9NRZ7; -.
DR OMA; WPTWLIS; -.
DR OrthoDB; 959325at2759; -.
DR PhylomeDB; Q9NRZ7; -.
DR TreeFam; TF314065; -.
DR BioCyc; MetaCyc:HS08470-MON; -.
DR BRENDA; 2.3.1.51; 2681.
DR PathwayCommons; Q9NRZ7; -.
DR Reactome; R-HSA-1483166; Synthesis of PA.
DR Reactome; R-HSA-6811436; COPI-independent Golgi-to-ER retrograde traffic.
DR SABIO-RK; Q9NRZ7; -.
DR SignaLink; Q9NRZ7; -.
DR SIGNOR; Q9NRZ7; -.
DR UniPathway; UPA00557; UER00613.
DR BioGRID-ORCS; 56894; 17 hits in 1083 CRISPR screens.
DR ChiTaRS; AGPAT3; human.
DR GeneWiki; AGPAT3; -.
DR GenomeRNAi; 56894; -.
DR Pharos; Q9NRZ7; Tbio.
DR PRO; PR:Q9NRZ7; -.
DR Proteomes; UP000005640; Chromosome 21.
DR RNAct; Q9NRZ7; protein.
DR Bgee; ENSG00000160216; Expressed in lateral globus pallidus and 181 other tissues.
DR ExpressionAtlas; Q9NRZ7; baseline and differential.
DR Genevisible; Q9NRZ7; HS.
DR GO; GO:0012505; C:endomembrane system; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005635; C:nuclear envelope; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; HDA:UniProtKB.
DR GO; GO:0003841; F:1-acylglycerol-3-phosphate O-acyltransferase activity; IDA:UniProtKB.
DR GO; GO:0016746; F:acyltransferase activity; IBA:GO_Central.
DR GO; GO:0016024; P:CDP-diacylglycerol biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006654; P:phosphatidic acid biosynthetic process; TAS:Reactome.
DR GO; GO:0008654; P:phospholipid biosynthetic process; NAS:UniProtKB.
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; Alternative splicing; 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_0000208194"
FT TOPO_DOM 1..124
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:20537980"
FT TRANSMEM 125..145
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 146..316
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:20537980"
FT TRANSMEM 317..339
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 340..376
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:20537980"
FT MOTIF 96..101
FT /note="HXXXXD motif"
FT /evidence="ECO:0000250|UniProtKB:Q9D517"
FT VAR_SEQ 1..62
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11487472"
FT /id="VSP_005072"
FT VAR_SEQ 1..60
FT /note="MGLLAFLKTQFVLHLLVGFVFVVSGLVINFVQLCTLALWPVSKQLYRRLNCR
FT LAYSLWSQ -> MQSGGSLPFCCYLPSVSSQLLLRESYCNFIKRTQCKSSKLMFSRDFL
FT SGQKYCRCLLWALPDHPRRRGPTSANALPLSAE (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_013144"
FT CONFLICT 74
FT /note="T -> P (in Ref. 7; CAD38635)"
FT /evidence="ECO:0000305"
FT CONFLICT 358..376
FT /note="VTEIEKGSSYGNQEFKKKE -> ESLEPGRWRLQ (in Ref. 3;
FT AAQ89067)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 376 AA; 43381 MW; C12CDBB7CC363852 CRC64;
MGLLAFLKTQ FVLHLLVGFV FVVSGLVINF VQLCTLALWP VSKQLYRRLN CRLAYSLWSQ
LVMLLEWWSC TECTLFTDQA TVERFGKEHA VIILNHNFEI DFLCGWTMCE RFGVLGSSKV
LAKKELLYVP LIGWTWYFLE IVFCKRKWEE DRDTVVEGLR RLSDYPEYMW FLLYCEGTRF
TETKHRVSME VAAAKGLPVL KYHLLPRTKG FTTAVKCLRG TVAAVYDVTL NFRGNKNPSL
LGILYGKKYE ADMCVRRFPL EDIPLDEKEA AQWLHKLYQE KDALQEIYNQ KGMFPGEQFK
PARRPWTLLN FLSWATILLS PLFSFVLGVF ASGSPLLILT FLGFVGAASF GVRRLIGVTE
IEKGSSYGNQ EFKKKE
