PCAT2_HUMAN
ID PCAT2_HUMAN Reviewed; 544 AA.
AC Q7L5N7; A3KBM1; Q6MZJ6; Q9NX23;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Lysophosphatidylcholine acyltransferase 2;
DE Short=LPC acyltransferase 2;
DE Short=LPCAT-2;
DE Short=LysoPC acyltransferase 2;
DE EC=2.3.1.23 {ECO:0000269|PubMed:21498505};
DE AltName: Full=1-acylglycerol-3-phosphate O-acyltransferase 11;
DE Short=1-AGP acyltransferase 11;
DE Short=1-AGPAT 11;
DE EC=2.3.1.51 {ECO:0000269|PubMed:20363836};
DE AltName: Full=1-acylglycerophosphocholine O-acyltransferase;
DE AltName: Full=1-alkenylglycerophosphocholine O-acyltransferase;
DE EC=2.3.1.25 {ECO:0000250|UniProtKB:Q8BYI6};
DE AltName: Full=1-alkylglycerophosphocholine O-acetyltransferase;
DE EC=2.3.1.67 {ECO:0000269|PubMed:17182612};
DE AltName: Full=Acetyl-CoA:lyso-platelet-activating factor acetyltransferase;
DE Short=Acetyl-CoA:lyso-PAF acetyltransferase;
DE Short=Lyso-PAF acetyltransferase;
DE Short=LysoPAFAT;
DE AltName: Full=Acyltransferase-like 1;
DE AltName: Full=Lysophosphatidic acid acyltransferase alpha;
DE Short=LPAAT-alpha;
GN Name=LPCAT2; Synonyms=AGPAT11, AYTL1;
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] (ISOFORM 1), FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=17182612; DOI=10.1074/jbc.m609641200;
RA Shindou H., Hishikawa D., Nakanishi H., Harayama T., Ishii S., Taguchi R.,
RA Shimizu T.;
RT "A single enzyme catalyzes both platelet-activating factor production and
RT membrane biogenesis of inflammatory cells. Cloning and characterization of
RT acetyl-CoA:lyso-PAF acetyltransferase.";
RL J. Biol. Chem. 282:6532-6539(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Carcinoma;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Fetal kidney;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Kidney;
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 [5]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RX PubMed=20363836; DOI=10.1194/jlr.m004762;
RA Agarwal A.K., Garg A.;
RT "Enzymatic activity of the human 1-acylglycerol-3-phosphate-O-
RT acyltransferase isoform 11: upregulated in breast and cervical cancers.";
RL J. Lipid Res. 51:2143-2152(2010).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND TOPOLOGY.
RX PubMed=21498505; DOI=10.1074/jbc.m110.202424;
RA Moessinger C., Kuerschner L., Spandl J., Shevchenko A., Thiele C.;
RT "Human lysophosphatidylcholine acyltransferases 1 and 2 are located in
RT lipid droplets where they catalyze the formation of phosphatidylcholine.";
RL J. Biol. Chem. 286:21330-21339(2011).
RN [8]
RP FUNCTION.
RX PubMed=25491198; DOI=10.1186/s12860-014-0043-3;
RA Moessinger C., Klizaite K., Steinhagen A., Philippou-Massier J.,
RA Shevchenko A., Hoch M., Ejsing C.S., Thiele C.;
RT "Two different pathways of phosphatidylcholine synthesis, the Kennedy
RT Pathway and the Lands Cycle, differentially regulate cellular
RT triacylglycerol storage.";
RL BMC Cell Biol. 15:43-43(2014).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
CC -!- FUNCTION: Exhibits both acyltransferase and acetyltransferase
CC activities (PubMed:17182612, PubMed:20363836, PubMed:21498505).
CC Catalyzes the conversion of lysophosphatidylcholine (1-acyl-sn-glycero-
CC 3-phosphocholine or LPC) into phosphatidylcholine (1,2-diacyl-sn-
CC glycero-3-phosphocholine or PC) (PubMed:21498505). Catalyzes the
CC conversion 1-acyl-sn-glycerol-3-phosphate (lysophosphatidic acid or
CC LPA) into 1,2-diacyl-sn-glycerol-3-phosphate (phosphatidic acid or PA)
CC by incorporating an acyl moiety at the sn-2 position of the glycerol
CC backbone (PubMed:20363836). Involved in platelet-activating factor
CC (PAF) biosynthesis by catalyzing the conversion of the PAF precursor,
CC 1-O-alkyl-sn-glycero-3-phosphocholine (lyso-PAF) into 1-O-alkyl-2-
CC acetyl-sn-glycero-3-phosphocholine (PAF) (PubMed:17182612). Also
CC converts lyso-PAF to 1-O-alkyl-2-acyl-sn-glycero-3-phosphocholine (PC),
CC a major component of cell membranes and a PAF precursor (By
CC similarity). Under resting conditions, acyltransferase activity is
CC preferred (By similarity). Upon acute inflammatory stimulus,
CC acetyltransferase activity is enhanced and PAF synthesis increases (By
CC similarity). Involved in the regulation of lipid droplet number and
CC size (PubMed:25491198). {ECO:0000250|UniProtKB:Q8BYI6,
CC ECO:0000269|PubMed:17182612, ECO:0000269|PubMed:20363836,
CC ECO:0000269|PubMed:21498505, ECO:0000269|PubMed:25491198}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-acyl-sn-glycero-3-phosphocholine + an acyl-CoA = a 1,2-
CC diacyl-sn-glycero-3-phosphocholine + CoA; Xref=Rhea:RHEA:12937,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168,
CC ChEBI:CHEBI:58342; EC=2.3.1.23;
CC Evidence={ECO:0000269|PubMed:21498505};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-O-alkyl-sn-glycero-3-phosphocholine + acetyl-CoA = a 1-O-
CC alkyl-2-acetyl-sn-glycero-3-phosphocholine + CoA;
CC Xref=Rhea:RHEA:18461, ChEBI:CHEBI:30909, ChEBI:CHEBI:36707,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=2.3.1.67;
CC Evidence={ECO:0000269|PubMed:17182612};
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:20363836};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-O-(1Z-alkenyl)-sn-glycero-3-phosphocholine + an acyl-CoA =
CC 1-O-(1Z-alkenyl)-2-acyl-sn-glycero-3-phosphocholine + CoA;
CC Xref=Rhea:RHEA:10344, ChEBI:CHEBI:57287, ChEBI:CHEBI:58342,
CC ChEBI:CHEBI:77286, ChEBI:CHEBI:77287; EC=2.3.1.25;
CC Evidence={ECO:0000250|UniProtKB:Q8BYI6};
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:20363836};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33188;
CC Evidence={ECO:0000305|PubMed:20363836};
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:20363836};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37132;
CC Evidence={ECO:0000305|PubMed:20363836};
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:20363836};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37144;
CC Evidence={ECO:0000305|PubMed:20363836};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 1-heptadecanoyl-sn-glycero-3-phosphate
CC = 1-heptadecanoyl-2-(9Z)-octadecenoyl-sn-glycero-3-phosphate + CoA;
CC Xref=Rhea:RHEA:37151, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387,
CC ChEBI:CHEBI:74554, ChEBI:CHEBI:74556;
CC Evidence={ECO:0000269|PubMed:20363836};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37152;
CC Evidence={ECO:0000305|PubMed:20363836};
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:20363836};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37164;
CC Evidence={ECO:0000305|PubMed:20363836};
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:20363836};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37156;
CC Evidence={ECO:0000305|PubMed:20363836};
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:20363836};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37160;
CC Evidence={ECO:0000305|PubMed:20363836};
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:20363836};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37172;
CC Evidence={ECO:0000305|PubMed:20363836};
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:20363836};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37176;
CC Evidence={ECO:0000305|PubMed:20363836};
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:20363836};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37596;
CC Evidence={ECO:0000305|PubMed:20363836};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 1-hexadecanoyl-sn-glycero-3-
CC phosphocholine = 1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-
CC phosphocholine + CoA; Xref=Rhea:RHEA:35991, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57387, ChEBI:CHEBI:72998, ChEBI:CHEBI:73001;
CC Evidence={ECO:0000269|PubMed:21498505};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35992;
CC Evidence={ECO:0000305|PubMed:21498505};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-O-hexadecyl-sn-glycero-3-phosphocholine + acetyl-CoA = 1-O-
CC hexadecyl-2-acetyl-sn-glycero-3-phosphocholine + CoA;
CC Xref=Rhea:RHEA:37719, ChEBI:CHEBI:44811, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57288, ChEBI:CHEBI:64496;
CC Evidence={ECO:0000269|PubMed:17182612};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37720;
CC Evidence={ECO:0000305|PubMed:17182612};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-O-octadecyl-sn-glycero-3-phosphocholine + acetyl-CoA = 1-O-
CC octadecyl-2-acetyl-sn-glycero-3-phosphocholine + CoA;
CC Xref=Rhea:RHEA:37699, ChEBI:CHEBI:52450, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57288, ChEBI:CHEBI:75216;
CC Evidence={ECO:0000250|UniProtKB:Q8BYI6};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37700;
CC Evidence={ECO:0000250|UniProtKB:Q8BYI6};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-sn-glycero-3-phosphocholine + acetyl-CoA = 1-
CC hexadecanoyl-2-acetyl-sn-glycero-3-phosphocholine + CoA;
CC Xref=Rhea:RHEA:37703, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:72998, ChEBI:CHEBI:75219;
CC Evidence={ECO:0000250|UniProtKB:Q8BYI6};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37704;
CC Evidence={ECO:0000250|UniProtKB:Q8BYI6};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-octadecanoyl-sn-glycero-3-phosphocholine + acetyl-CoA = 1-
CC octadecanoyl-2-acetyl-sn-glycero-3-phosphocholine + CoA;
CC Xref=Rhea:RHEA:37707, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:73858, ChEBI:CHEBI:75220;
CC Evidence={ECO:0000250|UniProtKB:Q8BYI6};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37708;
CC Evidence={ECO:0000250|UniProtKB:Q8BYI6};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-O-(1Z-alkenyl)-sn-glycero-3-phosphocholine + acetyl-CoA = 1-
CC O-(1Z)-alkenyl-2-acetyl-sn-glycero-3-phosphocholine + CoA;
CC Xref=Rhea:RHEA:37711, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:77287, ChEBI:CHEBI:78566;
CC Evidence={ECO:0000250|UniProtKB:Q8BYI6};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37712;
CC Evidence={ECO:0000250|UniProtKB:Q8BYI6};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + 1-O-octadecyl-sn-
CC glycero-3-phosphocholine = 1-O-octadecyl-2-(5Z,8Z,11Z,14Z)-
CC eicosatetraenoyl-sn-glycero-3-phosphocholine + CoA;
CC Xref=Rhea:RHEA:37747, ChEBI:CHEBI:57287, ChEBI:CHEBI:57368,
CC ChEBI:CHEBI:75216, ChEBI:CHEBI:75245;
CC Evidence={ECO:0000250|UniProtKB:Q8BYI6};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37748;
CC Evidence={ECO:0000250|UniProtKB:Q8BYI6};
CC -!- PATHWAY: Lipid metabolism; phospholipid metabolism.
CC -!- INTERACTION:
CC Q7L5N7; Q15125: EBP; NbExp=3; IntAct=EBI-4280011, EBI-3915253;
CC Q7L5N7; Q9Y282: ERGIC3; NbExp=3; IntAct=EBI-4280011, EBI-781551;
CC Q7L5N7; Q7Z5P4: HSD17B13; NbExp=3; IntAct=EBI-4280011, EBI-18053395;
CC Q7L5N7; P48051: KCNJ6; NbExp=3; IntAct=EBI-4280011, EBI-12017638;
CC Q7L5N7; Q5SR56: MFSD14B; NbExp=3; IntAct=EBI-4280011, EBI-373355;
CC Q7L5N7; Q86VR2: RETREG3; NbExp=3; IntAct=EBI-4280011, EBI-10192441;
CC Q7L5N7; Q8TEB9: RHBDD1; NbExp=3; IntAct=EBI-4280011, EBI-9916444;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:20363836, ECO:0000269|PubMed:21498505}; Single-pass
CC type II membrane protein {ECO:0000269|PubMed:21498505}. Golgi apparatus
CC membrane {ECO:0000250|UniProtKB:Q8BYI6}; Single-pass type II membrane
CC protein {ECO:0000305|PubMed:21498505}. Cell membrane
CC {ECO:0000250|UniProtKB:Q8BYI6}; Single-pass type II membrane protein
CC {ECO:0000305|PubMed:21498505}. Lipid droplet
CC {ECO:0000269|PubMed:21498505}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q7L5N7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q7L5N7-2; Sequence=VSP_019912;
CC -!- DOMAIN: The HXXXXD motif is essential for acyltransferase activity.
CC {ECO:0000250|UniProtKB:Q3TFD2}.
CC -!- SIMILARITY: Belongs to the 1-acyl-sn-glycerol-3-phosphate
CC acyltransferase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA91199.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAE46034.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AB244718; BAF47696.1; -; mRNA.
DR EMBL; AK000488; BAA91199.1; ALT_FRAME; mRNA.
DR EMBL; BX641069; CAE46034.1; ALT_FRAME; mRNA.
DR EMBL; BC002472; AAH02472.2; -; mRNA.
DR CCDS; CCDS10753.1; -. [Q7L5N7-1]
DR RefSeq; NP_060309.2; NM_017839.4. [Q7L5N7-1]
DR RefSeq; XP_011521471.1; XM_011523169.2. [Q7L5N7-2]
DR AlphaFoldDB; Q7L5N7; -.
DR SMR; Q7L5N7; -.
DR BioGRID; 120286; 109.
DR IntAct; Q7L5N7; 11.
DR MINT; Q7L5N7; -.
DR STRING; 9606.ENSP00000262134; -.
DR SwissLipids; SLP:000000279; -.
DR GlyGen; Q7L5N7; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q7L5N7; -.
DR PhosphoSitePlus; Q7L5N7; -.
DR SwissPalm; Q7L5N7; -.
DR BioMuta; LPCAT2; -.
DR DMDM; 74738601; -.
DR EPD; Q7L5N7; -.
DR jPOST; Q7L5N7; -.
DR MassIVE; Q7L5N7; -.
DR MaxQB; Q7L5N7; -.
DR PaxDb; Q7L5N7; -.
DR PeptideAtlas; Q7L5N7; -.
DR PRIDE; Q7L5N7; -.
DR ProteomicsDB; 68812; -. [Q7L5N7-1]
DR ProteomicsDB; 68813; -. [Q7L5N7-2]
DR Antibodypedia; 2010; 206 antibodies from 27 providers.
DR DNASU; 54947; -.
DR Ensembl; ENST00000262134.10; ENSP00000262134.5; ENSG00000087253.13. [Q7L5N7-1]
DR GeneID; 54947; -.
DR KEGG; hsa:54947; -.
DR MANE-Select; ENST00000262134.10; ENSP00000262134.5; NM_017839.5; NP_060309.2.
DR UCSC; uc002eie.5; human. [Q7L5N7-1]
DR CTD; 54947; -.
DR DisGeNET; 54947; -.
DR GeneCards; LPCAT2; -.
DR HGNC; HGNC:26032; LPCAT2.
DR HPA; ENSG00000087253; Tissue enhanced (bone marrow, thyroid gland).
DR MalaCards; LPCAT2; -.
DR MIM; 612040; gene.
DR neXtProt; NX_Q7L5N7; -.
DR OpenTargets; ENSG00000087253; -.
DR PharmGKB; PA162394265; -.
DR VEuPathDB; HostDB:ENSG00000087253; -.
DR eggNOG; KOG4666; Eukaryota.
DR GeneTree; ENSGT01030000234574; -.
DR HOGENOM; CLU_025017_0_0_1; -.
DR InParanoid; Q7L5N7; -.
DR OMA; VQQTRMG; -.
DR OrthoDB; 1266853at2759; -.
DR PhylomeDB; Q7L5N7; -.
DR TreeFam; TF323244; -.
DR BRENDA; 2.3.1.23; 2681.
DR BRENDA; 2.3.1.51; 2681.
DR BRENDA; 2.3.1.67; 2681.
DR PathwayCommons; Q7L5N7; -.
DR Reactome; R-HSA-1482788; Acyl chain remodelling of PC.
DR SignaLink; Q7L5N7; -.
DR SIGNOR; Q7L5N7; -.
DR UniPathway; UPA00085; -.
DR BioGRID-ORCS; 54947; 7 hits in 1078 CRISPR screens.
DR ChiTaRS; LPCAT2; human.
DR GenomeRNAi; 54947; -.
DR Pharos; Q7L5N7; Tbio.
DR PRO; PR:Q7L5N7; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q7L5N7; protein.
DR Bgee; ENSG00000087253; Expressed in caput epididymis and 165 other tissues.
DR ExpressionAtlas; Q7L5N7; baseline and differential.
DR Genevisible; Q7L5N7; HS.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005795; C:Golgi stack; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005811; C:lipid droplet; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0003841; F:1-acylglycerol-3-phosphate O-acyltransferase activity; IDA:UniProtKB.
DR GO; GO:0047184; F:1-acylglycerophosphocholine O-acyltransferase activity; IDA:UniProtKB.
DR GO; GO:0047159; F:1-alkenylglycerophosphocholine O-acyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0047192; F:1-alkylglycerophosphocholine O-acetyltransferase activity; ISS:UniProtKB.
DR GO; GO:0047144; F:2-acylglycerol-3-phosphate O-acyltransferase activity; TAS:Reactome.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0050200; F:plasmalogen synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0061024; P:membrane organization; ISS:UniProtKB.
DR GO; GO:0036151; P:phosphatidylcholine acyl-chain remodeling; IDA:UniProtKB.
DR GO; GO:0006663; P:platelet activating factor biosynthetic process; ISS:UniProtKB.
DR CDD; cd00051; EFh; 2.
DR CDD; cd07991; LPLAT_LPCAT1-like; 1.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR045252; LPCAT1-like.
DR InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR Pfam; PF01553; Acyltransferase; 1.
DR Pfam; PF00036; EF-hand_1; 1.
DR Pfam; PF13202; EF-hand_5; 1.
DR SMART; SM00054; EFh; 2.
DR SMART; SM00563; PlsC; 1.
DR SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS00018; EF_HAND_1; 2.
DR PROSITE; PS50222; EF_HAND_2; 2.
PE 1: Evidence at protein level;
KW Acyltransferase; Alternative splicing; Calcium; Cell membrane;
KW Endoplasmic reticulum; Golgi apparatus; Lipid biosynthesis; Lipid droplet;
KW Lipid metabolism; Membrane; Metal-binding; Phospholipid biosynthesis;
KW Phospholipid metabolism; Reference proteome; Repeat; Signal-anchor;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..544
FT /note="Lysophosphatidylcholine acyltransferase 2"
FT /id="PRO_0000247058"
FT TOPO_DOM 1..57
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 58..78
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 79..544
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT DOMAIN 391..426
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 428..463
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 518..544
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 146..151
FT /note="HXXXXD motif"
FT /evidence="ECO:0000250|UniProtKB:Q3TFD2"
FT MOTIF 220..223
FT /note="EGTC motif"
FT COMPBIAS 529..544
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 404
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 406
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 408
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 410
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 415
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 441
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 443
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 445
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 447
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 452
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT VAR_SEQ 1..270
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_019912"
FT VARIANT 163
FT /note="M -> I (in dbSNP:rs837550)"
FT /id="VAR_027058"
SQ SEQUENCE 544 AA; 60208 MW; B823D86272A739C0 CRC64;
MSRCAQAAEV AATVPGAGVG NVGLRPPMVP RQASFFPPPV PNPFVQQTQI GSARRVQIVL
LGIILLPIRV LLVALILLLA WPFAAISTVC CPEKLTHPIT GWRRKITQTA LKFLGRAMFF
SMGFIVAVKG KIASPLEAPV FVAAPHSTFF DGIACVVAGL PSMVSRNENA QVPLIGRLLR
AVQPVLVSRV DPDSRKNTIN EIIKRTTSGG EWPQILVFPE GTCTNRSCLI TFKPGAFIPG
VPVQPVLLRY PNKLDTVTWT WQGYTFIQLC MLTFCQLFTK VEVEFMPVQV PNDEEKNDPV
LFANKVRNLM AEALGIPVTD HTYEDCRLMI SAGQLTLPME AGLVEFTKIS RKLKLDWDGV
RKHLDEYASI ASSSKGGRIG IEEFAKYLKL PVSDVLRQLF ALFDRNHDGS IDFREYVIGL
AVLCNPSNTE EIIQVAFKLF DVDEDGYITE EEFSTILQAS LGVPDLDVSG LFKEIAQGDS
ISYEEFKSFA LKHPEYAKIF TTYLDLQTCH VFSLPKEVQT TPSTASNKVS PEKHEESTSD
KKDD
