PCAT1_DANRE
ID PCAT1_DANRE Reviewed; 517 AA.
AC Q1LWG4; A1L1Q0;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Lysophosphatidylcholine acyltransferase 1;
DE Short=LPC acyltransferase 1;
DE Short=LPCAT-1;
DE Short=LysoPC acyltransferase 1;
DE EC=2.3.1.23 {ECO:0000250|UniProtKB:Q3TFD2};
DE AltName: Full=1-acylglycerol-3-phosphate O-acyltransferase;
DE EC=2.3.1.51 {ECO:0000250|UniProtKB:Q1HAQ0};
DE AltName: Full=1-acylglycerophosphocholine O-acyltransferase;
DE AltName: Full=1-alkenylglycerophosphocholine O-acyltransferase;
DE EC=2.3.1.25 {ECO:0000250|UniProtKB:Q3TFD2};
DE AltName: Full=1-alkylglycerophosphocholine O-acetyltransferase;
DE EC=2.3.1.67 {ECO:0000250|UniProtKB:Q3TFD2};
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 2;
GN Name=lpcat1; Synonyms=aytl2; ORFNames=si:dkey-261i16.4, zgc:158232;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Exhibits both acyltransferase and acetyltransferase
CC activities (By similarity). Activity is calcium-independent (By
CC similarity). Catalyzes the conversion of lysophosphatidylcholine (1-
CC acyl-sn-glycero-3-phosphocholine or LPC) into phosphatidylcholine (1,2-
CC diacyl-sn-glycero-3-phosphocholine or PC) (By similarity). 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). {ECO:0000250|UniProtKB:Q1HAQ0,
CC ECO:0000250|UniProtKB:Q3TFD2}.
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:0000250|UniProtKB:Q3TFD2};
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:0000250|UniProtKB:Q3TFD2};
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:Q1HAQ0};
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:Q3TFD2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-acyl-sn-glycero-3-phospho-(1'-sn-glycerol) + an acyl-CoA =
CC 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol) + CoA;
CC Xref=Rhea:RHEA:33203, ChEBI:CHEBI:57287, ChEBI:CHEBI:58342,
CC ChEBI:CHEBI:64716, ChEBI:CHEBI:64840;
CC Evidence={ECO:0000250|UniProtKB:Q1HAQ0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33204;
CC Evidence={ECO:0000250|UniProtKB:Q1HAQ0};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-sn-glycero-3-phosphocholine + hexadecanoyl-CoA
CC = 1,2-dihexadecanoyl-sn-glycero-3-phosphocholine + CoA;
CC Xref=Rhea:RHEA:35983, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379,
CC ChEBI:CHEBI:72998, ChEBI:CHEBI:72999;
CC Evidence={ECO:0000250|UniProtKB:Q3TFD2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35984;
CC Evidence={ECO:0000250|UniProtKB:Q3TFD2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-O-hexadecyl-sn-glycero-3-phosphocholine + hexadecanoyl-CoA =
CC 1-O-hexadecyl-2-hexadecanoyl-sn-glycero-3-phosphocholine + CoA;
CC Xref=Rhea:RHEA:37811, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379,
CC ChEBI:CHEBI:64496, ChEBI:CHEBI:72744;
CC Evidence={ECO:0000250|UniProtKB:Q3TFD2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37812;
CC Evidence={ECO:0000250|UniProtKB:Q3TFD2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-O-(1Z-alkenyl)-sn-glycero-3-phosphocholine + hexadecanoyl-
CC CoA = 1-O-(1Z)-alkenyl-2-hexadecanoyl-sn-glycero-3-phosphocholine +
CC CoA; Xref=Rhea:RHEA:37819, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379,
CC ChEBI:CHEBI:77287, ChEBI:CHEBI:77304;
CC Evidence={ECO:0000250|UniProtKB:Q3TFD2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37820;
CC Evidence={ECO:0000250|UniProtKB:Q3TFD2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-sn-glycero-3-phospho-(1'-sn-glycerol) +
CC hexadecanoyl-CoA = 1,2-dihexadecanoyl-sn-glycero-3-phospho-(1'-sn-
CC glycerol) + CoA; Xref=Rhea:RHEA:35851, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57379, ChEBI:CHEBI:72829, ChEBI:CHEBI:75158;
CC Evidence={ECO:0000250|UniProtKB:Q3TFD2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35852;
CC Evidence={ECO:0000250|UniProtKB:Q3TFD2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-dodecanoyl-sn-glycero-3-phosphocholine + hexadecanoyl-CoA =
CC 1-dodecanoyl-2-hexadecanoyl-sn-glycero-3-phosphocholine + CoA;
CC Xref=Rhea:RHEA:37511, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379,
CC ChEBI:CHEBI:74966, ChEBI:CHEBI:75017;
CC Evidence={ECO:0000250|UniProtKB:Q3TFD2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37512;
CC Evidence={ECO:0000250|UniProtKB:Q3TFD2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-tetradecanoyl-sn-glycero-3-phosphocholine + hexadecanoyl-CoA
CC = 1-tetradecanoyl-2-hexadecanoyl-sn-glycero-3-phosphocholine + CoA;
CC Xref=Rhea:RHEA:37655, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379,
CC ChEBI:CHEBI:64489, ChEBI:CHEBI:75062;
CC Evidence={ECO:0000250|UniProtKB:Q3TFD2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37656;
CC Evidence={ECO:0000250|UniProtKB:Q3TFD2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-O-octadecyl-sn-glycero-3-phosphocholine + hexadecanoyl-CoA =
CC 1-O-octadecyl-2-hexadecanoyl-sn-glycero-3-phosphocholine + CoA;
CC Xref=Rhea:RHEA:37839, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379,
CC ChEBI:CHEBI:75216, ChEBI:CHEBI:75290;
CC Evidence={ECO:0000250|UniProtKB:Q3TFD2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37840;
CC Evidence={ECO:0000250|UniProtKB:Q3TFD2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-octadecanoyl-sn-glycero-3-phosphocholine + hexadecanoyl-CoA
CC = 1-octadecanoyl-2-hexadecanoyl-sn-glycero-3-phosphocholine + CoA;
CC Xref=Rhea:RHEA:37527, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379,
CC ChEBI:CHEBI:73858, ChEBI:CHEBI:75026;
CC Evidence={ECO:0000250|UniProtKB:Q3TFD2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37528;
CC Evidence={ECO:0000250|UniProtKB:Q3TFD2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine +
CC hexadecanoyl-CoA = 1-(9Z-octadecenoyl)-2-hexadecanoyl-sn-glycero-3-
CC phosphocholine + CoA; Xref=Rhea:RHEA:37383, ChEBI:CHEBI:28610,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57379, ChEBI:CHEBI:74667;
CC Evidence={ECO:0000250|UniProtKB:Q3TFD2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37384;
CC Evidence={ECO:0000250|UniProtKB:Q3TFD2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-eicosanoyl-sn-glycero-3-phosphocholine + hexadecanoyl-CoA =
CC 1-eicosanoyl-2-hexadecanoyl-sn-glycero-3-phosphocholine + CoA;
CC Xref=Rhea:RHEA:37843, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379,
CC ChEBI:CHEBI:74968, ChEBI:CHEBI:75294;
CC Evidence={ECO:0000250|UniProtKB:Q3TFD2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37844;
CC Evidence={ECO:0000250|UniProtKB:Q3TFD2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-sn-glycero-3-phosphocholine + hexanoyl-CoA = 1-
CC hexadecanoyl-2-hexanoyl-sn-glycero-3-phosphocholine + CoA;
CC Xref=Rhea:RHEA:37855, ChEBI:CHEBI:57287, ChEBI:CHEBI:62620,
CC ChEBI:CHEBI:72998, ChEBI:CHEBI:75301;
CC Evidence={ECO:0000250|UniProtKB:Q3TFD2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37856;
CC Evidence={ECO:0000250|UniProtKB:Q3TFD2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-sn-glycero-3-phosphocholine + octanoyl-CoA = 1-
CC hexadecanoyl-2-octanoyl-sn-glycero-3-phosphocholine + CoA;
CC Xref=Rhea:RHEA:37859, ChEBI:CHEBI:57287, ChEBI:CHEBI:57386,
CC ChEBI:CHEBI:72998, ChEBI:CHEBI:75302;
CC Evidence={ECO:0000250|UniProtKB:Q3TFD2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37860;
CC Evidence={ECO:0000250|UniProtKB:Q3TFD2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-sn-glycero-3-phosphocholine + decanoyl-CoA = 1-
CC hexadecanoyl-2-decanoyl-sn-glycero-3-phosphocholine + CoA;
CC Xref=Rhea:RHEA:37863, ChEBI:CHEBI:57287, ChEBI:CHEBI:61430,
CC ChEBI:CHEBI:72998, ChEBI:CHEBI:75300;
CC Evidence={ECO:0000250|UniProtKB:Q3TFD2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37864;
CC Evidence={ECO:0000250|UniProtKB:Q3TFD2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-sn-glycero-3-phosphocholine + dodecanoyl-CoA =
CC 1-hexadecanoyl-2-dodecanoyl-sn-glycero-3-phosphocholine + CoA;
CC Xref=Rhea:RHEA:37515, ChEBI:CHEBI:57287, ChEBI:CHEBI:57375,
CC ChEBI:CHEBI:72998, ChEBI:CHEBI:75018;
CC Evidence={ECO:0000250|UniProtKB:Q3TFD2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37516;
CC Evidence={ECO:0000250|UniProtKB:Q3TFD2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-sn-glycero-3-phosphocholine + tetradecanoyl-CoA
CC = 1-hexadecanoyl-2-tetradecanoyl-sn-glycero-3-phosphocholine + CoA;
CC Xref=Rhea:RHEA:37867, ChEBI:CHEBI:57287, ChEBI:CHEBI:57385,
CC ChEBI:CHEBI:72998, ChEBI:CHEBI:75304;
CC Evidence={ECO:0000250|UniProtKB:Q3TFD2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37868;
CC Evidence={ECO:0000250|UniProtKB:Q3TFD2};
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:Q3TFD2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35992;
CC Evidence={ECO:0000250|UniProtKB:Q3TFD2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z)-octadecadienoyl-CoA + 1-hexadecanoyl-sn-glycero-3-
CC phosphocholine = 1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-
CC glycero-3-phosphocholine + CoA; Xref=Rhea:RHEA:35995,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57383, ChEBI:CHEBI:72998,
CC ChEBI:CHEBI:73002; Evidence={ECO:0000250|UniProtKB:Q3TFD2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35996;
CC Evidence={ECO:0000250|UniProtKB:Q3TFD2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoyl-CoA + 1-hexadecanoyl-
CC sn-glycero-3-phosphocholine = 1-hexadecanoyl-2-
CC (4Z,7Z,10Z,13Z,16Z,19Z-docosahexaenoyl)-sn-glycero-3-phosphocholine +
CC CoA; Xref=Rhea:RHEA:37475, ChEBI:CHEBI:57287, ChEBI:CHEBI:72998,
CC ChEBI:CHEBI:74298, ChEBI:CHEBI:74963;
CC Evidence={ECO:0000250|UniProtKB:Q3TFD2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37476;
CC Evidence={ECO:0000250|UniProtKB:Q3TFD2};
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:Q3TFD2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37704;
CC Evidence={ECO:0000250|UniProtKB:Q3TFD2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-sn-glycero-3-phosphocholine + eicosanoyl-CoA =
CC 1-hexadecanoyl-2-eicosanoyl-sn-glycero-3-phosphocholine + CoA;
CC Xref=Rhea:RHEA:43264, ChEBI:CHEBI:57287, ChEBI:CHEBI:57380,
CC ChEBI:CHEBI:72998, ChEBI:CHEBI:82943;
CC Evidence={ECO:0000250|UniProtKB:Q3TFD2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43265;
CC Evidence={ECO:0000250|UniProtKB:Q3TFD2};
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:0000250|UniProtKB:Q3TFD2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37720;
CC Evidence={ECO:0000250|UniProtKB:Q3TFD2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-acyl-sn-glycero-3-phosphocholine + hexadecanoyl-CoA = 1-
CC acyl-2-hexadecanoyl-sn-glycero-3-phosphocholine + CoA;
CC Xref=Rhea:RHEA:37803, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379,
CC ChEBI:CHEBI:58168, ChEBI:CHEBI:75279;
CC Evidence={ECO:0000250|UniProtKB:Q1HAQ0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37804;
CC Evidence={ECO:0000250|UniProtKB:Q1HAQ0};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-acyl-sn-glycero-3-phosphate + hexadecanoyl-CoA = 1-acyl-2-
CC hexadecanoyl-sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:33315,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57379, ChEBI:CHEBI:57970,
CC ChEBI:CHEBI:64862; Evidence={ECO:0000250|UniProtKB:Q1HAQ0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33316;
CC Evidence={ECO:0000250|UniProtKB:Q1HAQ0};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-acyl-sn-glycero-3-phospho-(1'-sn-glycerol) + hexadecanoyl-
CC CoA = 1-acyl-2-hexadecanoyl-sn-glycero-3-phospho-(1'-sn-glycerol) +
CC CoA; Xref=Rhea:RHEA:37807, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379,
CC ChEBI:CHEBI:64840, ChEBI:CHEBI:75280;
CC Evidence={ECO:0000250|UniProtKB:Q1HAQ0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37808;
CC Evidence={ECO:0000250|UniProtKB:Q1HAQ0};
CC -!- PATHWAY: Lipid metabolism; phospholipid metabolism.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q8NF37}; Single-pass type II membrane protein
CC {ECO:0000250|UniProtKB:Q8NF37}. Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:Q3TFD2}; Single-pass type II membrane protein
CC {ECO:0000250|UniProtKB:Q8NF37}. Cell membrane
CC {ECO:0000250|UniProtKB:Q8NF37}; Single-pass type II membrane protein
CC {ECO:0000250|UniProtKB:Q8NF37}. Lipid droplet
CC {ECO:0000250|UniProtKB:Q8NF37}. Note=May adopt a monotopic topology
CC when embedded in the lipid monolayer of the lipid droplet, with both
CC termini exposed to the cytoplasm. {ECO:0000250|UniProtKB:Q8NF37}.
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-phosphocholine. {ECO:0000250|UniProtKB:Q3TFD2}.
CC -!- DOMAIN: The di-lysine motif may confer endoplasmic reticulum
CC localization. {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; BX571830; CAK10868.1; -; Genomic_DNA.
DR EMBL; BC129167; AAI29168.1; -; mRNA.
DR RefSeq; NP_001037806.2; NM_001044341.2.
DR RefSeq; XP_005170093.1; XM_005170036.3.
DR AlphaFoldDB; Q1LWG4; -.
DR SMR; Q1LWG4; -.
DR STRING; 7955.ENSDARP00000094631; -.
DR PaxDb; Q1LWG4; -.
DR Ensembl; ENSDART00000103855; ENSDARP00000094631; ENSDARG00000011506.
DR Ensembl; ENSDART00000163382; ENSDARP00000133893; ENSDARG00000011506.
DR GeneID; 555969; -.
DR KEGG; dre:555969; -.
DR CTD; 79888; -.
DR ZFIN; ZDB-GENE-060503-915; lpcat1.
DR eggNOG; KOG4666; Eukaryota.
DR GeneTree; ENSGT01030000234574; -.
DR InParanoid; Q1LWG4; -.
DR OMA; SHDIAKM; -.
DR OrthoDB; 1266853at2759; -.
DR PhylomeDB; Q1LWG4; -.
DR TreeFam; TF323244; -.
DR Reactome; R-DRE-1482788; Acyl chain remodelling of PC.
DR Reactome; R-DRE-1482925; Acyl chain remodelling of PG.
DR Reactome; R-DRE-1483166; Synthesis of PA.
DR Reactome; R-DRE-1483191; Synthesis of PC.
DR Reactome; R-DRE-6798695; Neutrophil degranulation.
DR UniPathway; UPA00085; -.
DR PRO; PR:Q1LWG4; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 19.
DR Bgee; ENSDARG00000011506; Expressed in mature ovarian follicle and 25 other tissues.
DR ExpressionAtlas; Q1LWG4; baseline.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005811; C:lipid droplet; IEA:UniProtKB-SubCell.
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; ISS:UniProtKB.
DR GO; GO:0047159; F:1-alkenylglycerophosphocholine O-acyltransferase activity; ISS:UniProtKB.
DR GO; GO:0047192; F:1-alkylglycerophosphocholine O-acetyltransferase activity; ISS: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:0008654; P:phospholipid biosynthetic process; ISS:UniProtKB.
DR CDD; cd00051; EFh; 1.
DR CDD; cd07991; LPLAT_LPCAT1-like; 1.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR045252; LPCAT1-like.
DR InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR Pfam; PF01553; Acyltransferase; 1.
DR Pfam; PF13833; EF-hand_8; 1.
DR SMART; SM00563; PlsC; 1.
DR SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS50222; EF_HAND_2; 1.
PE 2: Evidence at transcript level;
KW Acyltransferase; Calcium; Cell membrane; Endoplasmic reticulum;
KW Glycoprotein; Golgi apparatus; Lipid biosynthesis; Lipid droplet;
KW Lipid metabolism; Membrane; Phospholipid biosynthesis;
KW Phospholipid metabolism; Reference proteome; Repeat; Signal-anchor;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..517
FT /note="Lysophosphatidylcholine acyltransferase 1"
FT /id="PRO_0000247067"
FT TOPO_DOM 1..52
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 53..73
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 74..517
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT DOMAIN 443..478
FT /note="EF-hand"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT MOTIF 129..134
FT /note="HXXXXD motif"
FT /evidence="ECO:0000250|UniProtKB:Q3TFD2"
FT MOTIF 514..517
FT /note="Di-lysine motif"
FT /evidence="ECO:0000250|UniProtKB:Q3TFD2"
FT CARBOHYD 207
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 511
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 347
FT /note="Q -> R (in Ref. 2; AAI29168)"
FT /evidence="ECO:0000305"
FT CONFLICT 351
FT /note="C -> S (in Ref. 2; AAI29168)"
FT /evidence="ECO:0000305"
FT CONFLICT 467
FT /note="E -> D (in Ref. 2; AAI29168)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 517 AA; 58727 MW; DA4A17F30B6D39CD CRC64;
MRFPNRKLHT AVNGGDSGVS THFRNPFVHE LRFTTLQKLK IAVMTVTLFP VRLLFAAFMM
LLAWPFAFVA TVGRSENAVE PLSWWRWLVD LALKAIMRAM WFSGGFHWVR VKGRPALPSE
APILTMAPHS SYFDAIPVTM TMASIVMKAE SKDIPVWGTL IKFIRPVFVS RSDQDSRRKT
VEEIKRRASS NGEWPQIMIF PEGTCTNRSC LIAFKPGAFI PGVPVQPVVL RYPNELDTIS
WTWQGPGAFK ILWLTLCQLH NFVEIEYLPT YTPSEEEKKD PALFASNVRR IMAKALGLPI
IDYSFEDCQL AMAKGPLRLP KHTCLLEFAR LVRLLGLKTK VTDEVLQEEA CSARQLCGRR
LDMEGFAQYL HQPMTEAVQD IFSLFEEHGM MDVREYVIAL SVVCRPFRYL DTVKLAFRMF
EAQEDGAIVE DELTVILKTA LGVGDLAVSE LFRAIDSQDK GKITFDELCS FMEKCPDLVE
QYHCLCESIS QHSRESTSSS NGFCADFSPR NHSKKQD
