PCAT2_MOUSE
ID PCAT2_MOUSE Reviewed; 544 AA.
AC Q8BYI6; A3KBM0; A9Q1G2; A9Q1G3;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 145.
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:17182612, ECO:0000269|PubMed:18156367};
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:0000250|UniProtKB:Q7L5N7};
DE AltName: Full=1-acylglycerophosphocholine O-acyltransferase;
DE AltName: Full=1-alkenylglycerophosphocholine O-acyltransferase;
DE EC=2.3.1.25 {ECO:0000269|PubMed:17182612};
DE AltName: Full=1-alkylglycerophosphocholine O-acetyltransferase;
DE EC=2.3.1.67 {ECO:0000269|PubMed:17182612, ECO:0000269|PubMed:18285344};
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;
GN Name=Lpcat2; Synonyms=Aytl1, Aytl1a, Lpcat2a;
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] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY,
RP ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, AND INDUCTION.
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 STRAIN=C57BL/6J; TISSUE=Spinal cord;
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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 175-299 (ISOFORM 2), NUCLEOTIDE SEQUENCE
RP [MRNA] OF 175-544 (ISOFORM 3), FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=18156367; DOI=10.1073/pnas.0709737104;
RA Soupene E., Fyrst H., Kuypers F.A.;
RT "Mammalian acyl-CoA:lysophosphatidylcholine acyltransferase enzymes.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:88-93(2008).
RN [4]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=18285344; DOI=10.1074/jbc.m708909200;
RA Harayama T., Shindou H., Ogasawara R., Suwabe A., Shimizu T.;
RT "Identification of a novel noninflammatory biosynthetic pathway of
RT platelet-activating factor.";
RL J. Biol. Chem. 283:11097-11106(2008).
CC -!- FUNCTION: Exhibits both acyltransferase and acetyltransferase
CC activities (PubMed:17182612, PubMed:18156367, PubMed:18285344).
CC Activity is calcium-dependent (PubMed:17182612). Catalyzes the
CC conversion of lysophosphatidylcholine (1-acyl-sn-glycero-3-
CC phosphocholine or LPC) into phosphatidylcholine (1,2-diacyl-sn-glycero-
CC 3-phosphocholine or PC) (PubMed:17182612, PubMed:18156367). Catalyzes
CC the 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 (By similarity). Involved in platelet-activating factor (PAF)
CC biosynthesis by catalyzing the conversion of the PAF precursor, 1-O-
CC alkyl-sn-glycero-3-phosphocholine (lyso-PAF) into 1-O-alkyl-2-acetyl-
CC sn-glycero-3-phosphocholine (PAF) (PubMed:17182612, PubMed:18285344).
CC Also converts lyso-PAF to 1-O-alkyl-2-acyl-sn-glycero-3-phosphocholine
CC (PC), a major component of cell membranes and a PAF precursor
CC (PubMed:17182612). Under resting conditions, acyltransferase activity
CC is preferred (PubMed:17182612). Upon acute inflammatory stimulus,
CC acetyltransferase activity is enhanced and PAF synthesis increases
CC (PubMed:17182612). Involved in the regulation of lipid droplet number
CC and size (By similarity). {ECO:0000250|UniProtKB:Q8NF37,
CC ECO:0000269|PubMed:17182612, ECO:0000269|PubMed:18156367,
CC ECO:0000269|PubMed:18285344}.
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:17182612, ECO:0000269|PubMed:18156367};
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, ECO:0000269|PubMed:18285344};
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:0000250|UniProtKB:Q7L5N7};
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:0000269|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:0000269|PubMed:17182612};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37700;
CC Evidence={ECO:0000305|PubMed:17182612};
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:0000269|PubMed:17182612};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37704;
CC Evidence={ECO:0000305|PubMed:17182612};
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:0000269|PubMed:17182612};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37708;
CC Evidence={ECO:0000305|PubMed:17182612};
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:0000269|PubMed:17182612};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37712;
CC Evidence={ECO:0000305|PubMed:17182612};
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, ECO:0000269|PubMed:18285344};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37720;
CC Evidence={ECO:0000305|PubMed:17182612};
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:0000269|PubMed:17182612};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37748;
CC Evidence={ECO:0000305|PubMed:17182612};
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:0000250|UniProtKB:Q7L5N7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33188;
CC Evidence={ECO:0000250|UniProtKB:Q7L5N7};
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:Q7L5N7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37132;
CC Evidence={ECO:0000250|UniProtKB:Q7L5N7};
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:0000250|UniProtKB:Q7L5N7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37144;
CC Evidence={ECO:0000250|UniProtKB:Q7L5N7};
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:0000250|UniProtKB:Q7L5N7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37152;
CC Evidence={ECO:0000250|UniProtKB:Q7L5N7};
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:Q7L5N7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37164;
CC Evidence={ECO:0000250|UniProtKB:Q7L5N7};
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:Q7L5N7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37156;
CC Evidence={ECO:0000250|UniProtKB:Q7L5N7};
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:Q7L5N7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37160;
CC Evidence={ECO:0000250|UniProtKB:Q7L5N7};
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:0000250|UniProtKB:Q7L5N7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37172;
CC Evidence={ECO:0000250|UniProtKB:Q7L5N7};
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:Q7L5N7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37176;
CC Evidence={ECO:0000250|UniProtKB:Q7L5N7};
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:Q7L5N7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37596;
CC Evidence={ECO:0000250|UniProtKB:Q7L5N7};
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:0000250|UniProtKB:Q7L5N7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35992;
CC Evidence={ECO:0000250|UniProtKB:Q7L5N7};
CC -!- ACTIVITY REGULATION: Acetyltransferase activity is increased following
CC acute inflammatory stimulation by lipopolysaccharide (LPS).
CC Acyltransferase activity is unchanged. {ECO:0000269|PubMed:17182612}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=50.4 uM for acetyl-CoA {ECO:0000269|PubMed:17182612};
CC KM=21.1 uM for arachidonoyl-CoA {ECO:0000269|PubMed:17182612};
CC Temperature dependence:
CC Optimum temperature is 7.4 degrees Celsius.
CC {ECO:0000269|PubMed:17182612};
CC -!- PATHWAY: Lipid metabolism; phospholipid metabolism.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:17182612}; Single-pass type II membrane protein
CC {ECO:0000250|UniProtKB:Q7L5N7}. Golgi apparatus membrane
CC {ECO:0000269|PubMed:17182612}; Single-pass type II membrane protein
CC {ECO:0000250|UniProtKB:Q7L5N7}. Cell membrane
CC {ECO:0000305|PubMed:18156367}; Single-pass type II membrane protein
CC {ECO:0000250|UniProtKB:Q7L5N7}. Lipid droplet
CC {ECO:0000250|UniProtKB:Q7L5N7}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=a, Aytl1_v1;
CC IsoId=Q8BYI6-1; Sequence=Displayed;
CC Name=2; Synonyms=b, Aytl1_v2;
CC IsoId=Q8BYI6-2; Sequence=VSP_037079;
CC Name=3; Synonyms=c, Aytl1_v3;
CC IsoId=Q8BYI6-3; Sequence=VSP_037080, VSP_037081;
CC -!- TISSUE SPECIFICITY: Highest expression is found in resident macrophages
CC and casein-induced neutrophils followed by skin, colon, spleen and
CC thioglycollate-induced macrophages. Detected in erythroleukemic cells
CC but not in reticulocytes. {ECO:0000269|PubMed:17182612,
CC ECO:0000269|PubMed:18156367}.
CC -!- INDUCTION: By inflammatory stimulation by LPS and by ODN1826, a TLR9
CC ligand, but not by poly(I:C), a TLR3 ligand.
CC {ECO:0000269|PubMed:17182612}.
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}.
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DR EMBL; AB244716; BAF47695.1; -; mRNA.
DR EMBL; AK039431; BAC30345.1; -; mRNA.
DR EMBL; EF442783; ABR20912.1; -; mRNA.
DR EMBL; EF442784; ABR20913.1; -; mRNA.
DR CCDS; CCDS22524.1; -. [Q8BYI6-1]
DR CCDS; CCDS90434.1; -. [Q8BYI6-2]
DR RefSeq; NP_766602.1; NM_173014.1. [Q8BYI6-1]
DR AlphaFoldDB; Q8BYI6; -.
DR SMR; Q8BYI6; -.
DR BioGRID; 234756; 1.
DR STRING; 10090.ENSMUSP00000049252; -.
DR SwissLipids; SLP:000000293; -.
DR iPTMnet; Q8BYI6; -.
DR PhosphoSitePlus; Q8BYI6; -.
DR SwissPalm; Q8BYI6; -.
DR MaxQB; Q8BYI6; -.
DR PaxDb; Q8BYI6; -.
DR PeptideAtlas; Q8BYI6; -.
DR PRIDE; Q8BYI6; -.
DR ProteomicsDB; 287796; -. [Q8BYI6-1]
DR ProteomicsDB; 287797; -. [Q8BYI6-2]
DR ProteomicsDB; 287798; -. [Q8BYI6-3]
DR Antibodypedia; 2010; 206 antibodies from 27 providers.
DR DNASU; 270084; -.
DR Ensembl; ENSMUST00000046290; ENSMUSP00000049252; ENSMUSG00000033192. [Q8BYI6-1]
DR Ensembl; ENSMUST00000209265; ENSMUSP00000148089; ENSMUSG00000033192. [Q8BYI6-3]
DR Ensembl; ENSMUST00000210099; ENSMUSP00000147941; ENSMUSG00000033192. [Q8BYI6-2]
DR GeneID; 270084; -.
DR KEGG; mmu:270084; -.
DR UCSC; uc009muf.1; mouse. [Q8BYI6-3]
DR UCSC; uc009mug.1; mouse. [Q8BYI6-1]
DR UCSC; uc012gij.1; mouse. [Q8BYI6-2]
DR CTD; 54947; -.
DR MGI; MGI:3606214; Lpcat2.
DR VEuPathDB; HostDB:ENSMUSG00000033192; -.
DR eggNOG; KOG4666; Eukaryota.
DR GeneTree; ENSGT01030000234574; -.
DR HOGENOM; CLU_025017_0_0_1; -.
DR InParanoid; Q8BYI6; -.
DR OMA; VQQTRMG; -.
DR OrthoDB; 1266853at2759; -.
DR PhylomeDB; Q8BYI6; -.
DR TreeFam; TF323244; -.
DR BRENDA; 2.3.1.23; 3474.
DR BRENDA; 2.3.1.67; 3474.
DR Reactome; R-MMU-1482788; Acyl chain remodelling of PC.
DR UniPathway; UPA00085; -.
DR BioGRID-ORCS; 270084; 3 hits in 76 CRISPR screens.
DR ChiTaRS; Lpcat2; mouse.
DR PRO; PR:Q8BYI6; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q8BYI6; protein.
DR Bgee; ENSMUSG00000033192; Expressed in granulocyte and 155 other tissues.
DR Genevisible; Q8BYI6; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005795; C:Golgi stack; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005811; C:lipid droplet; ISO:MGI.
DR GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0003841; F:1-acylglycerol-3-phosphate O-acyltransferase activity; ISS: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; IDA:UniProtKB.
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; IDA:UniProtKB.
DR GO; GO:0036151; P:phosphatidylcholine acyl-chain remodeling; ISO:MGI.
DR GO; GO:0006663; P:platelet activating factor biosynthetic process; IDA:UniProtKB.
DR CDD; cd00051; EFh; 1.
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; PF13499; EF-hand_7; 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_0000247059"
FT TOPO_DOM 1..58
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 59..79
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 80..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 520..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 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 215..254
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:18156367"
FT /id="VSP_037079"
FT VAR_SEQ 215..236
FT /note="ILVFPEGTCTNRSCLITFKPGA -> EPSSQEFQCSPSSSDTQTSWIL (in
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:18156367"
FT /id="VSP_037080"
FT VAR_SEQ 237..544
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:18156367"
FT /id="VSP_037081"
SQ SEQUENCE 544 AA; 60254 MW; 8A790A4C71BB8898 CRC64;
MNRCAEAAAV AATVPGSGVG DAGLRPPMVP RQASFFPPPV PNPFVQQTTI SASRRLQMFL
LGIILLPVRA LLVGIILLLA WPFAVISTAC CPEKLTHPIS NWRRKITRPA LTFLARAMFF
SMGFTVTVKG KVASPLEAPI FVVAPHSTFF DGIACVVAGL PSLVSRNENA QTPLVGRLLR
ALQPVLVSRV DPDSRKNTIN EIKKRATSGG EWPQILVFPE GTCTNRSCLI TFKPGAFIPG
VPVQPVLLRY PNKLDTVTWT WQGYTFLQLC VLTFCQLFTK VEIEFMPVQA PSEEEKNDPV
LFASRIRNLM AEALEIPVTD HTYEDCRLMI SAGQLTLPME AGLVEFSKIS RKLKLDWDGI
RKHLDEYASI ASSSKGGRIG IEEFAEYLKL PVSDVLRQLF ALFDRNNDGS IDFREYVIGL
AVLCNPANTE EIIQVAFKLF DVDEDGYITE EEFCTILQAS LGVPDLNVSG LFREIAQRDS
VSYEEFKSFA LKHPEYAKIF TTYLDLQTCH VFSLPEEVQT APSVASNKVS PESQEEGTSD
KKVD
