MBOA5_RAT
ID MBOA5_RAT Reviewed; 487 AA.
AC Q5FVN0;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Lysophospholipid acyltransferase 5;
DE Short=LPLAT 5;
DE EC=2.3.1.- {ECO:0000250|UniProtKB:Q6P1A2};
DE AltName: Full=1-acylglycerophosphocholine O-acyltransferase;
DE EC=2.3.1.23 {ECO:0000250|UniProtKB:Q6P1A2};
DE AltName: Full=1-acylglycerophosphoethanolamine O-acyltransferase;
DE EC=2.3.1.n7 {ECO:0000250|UniProtKB:Q6P1A2};
DE AltName: Full=1-acylglycerophosphoserine O-acyltransferase;
DE EC=2.3.1.n6 {ECO:0000250|UniProtKB:Q6P1A2};
DE AltName: Full=Lysophosphatidylcholine acyltransferase 3;
DE Short=Lyso-PC acyltransferase 3;
DE AltName: Full=Membrane-bound O-acyltransferase domain-containing protein 5;
DE Short=O-acyltransferase domain-containing protein 5;
GN Name=Lpcat3; Synonyms=Grcc3f {ECO:0000312|EMBL:AAH89869.1}, Mboat5, Oact5;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver;
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).
CC -!- FUNCTION: Lysophospholipid O-acyltransferase (LPLAT) that catalyzes the
CC reacylation step of the phospholipid remodeling process also known as
CC the Lands cycle. Catalyzes transfer of the fatty acyl chain from fatty
CC acyl-CoA to 1-acyl lysophospholipid to form various classes of
CC phospholipids. Converts 1-acyl lysophosphatidylcholine (LPC) into
CC phosphatidylcholine (PC) (LPCAT activity), 1-acyl
CC lysophosphatidylserine (LPS) into phosphatidylserine (PS) (LPSAT
CC activity) and 1-acyl lysophosphatidylethanolamine (LPE) into
CC phosphatidylethanolamine (PE) (LPEAT activity). Favors polyunsaturated
CC fatty acyl-CoAs as acyl donors compared to saturated fatty acyl-CoAs
CC (By similarity). Has higher activity for LPC acyl acceptors compared to
CC LPEs and LPSs. Can also transfer the fatty acyl chain from fatty acyl-
CC CoA to 1-O-alkyl lysophospholipid or 1-O-alkenyl lysophospholipid with
CC lower efficiency. Acts as a major LPC O-acyltransferase in liver and
CC intestine. As a component of the liver X receptor/NR1H3 or NR1H2
CC signaling pathway, mainly catalyzes the incorporation of arachidonate
CC into PCs of endoplasmic reticulum (ER) membranes, increasing membrane
CC dynamics and enabling triacylglycerols transfer to nascent very low-
CC density lipoprotein (VLDL) particles. Promotes processing of sterol
CC regulatory protein SREBF1 in hepatocytes, likely by facilitating the
CC translocation of SREBF1-SCAP complex from ER to the Golgi apparatus.
CC Participates in mechanisms by which the liver X receptor/NR1H3 or NR1H2
CC signaling pathway counteracts lipid-induced ER stress response and
CC inflammation. Down-regulates hepatic inflammation by limiting
CC arachidonic acid availability for synthesis of inflammatory
CC eicosanoids, such as prostaglandins. In enterocytes, acts as a
CC component of a gut-brain feedback loop that coordinates dietary lipid
CC absorption and food intake. Regulates the abundance of PCs containing
CC linoleate and arachidonate in enterocyte membranes, enabling passive
CC diffusion of fatty acids and cholesterol across the membrane for
CC efficient chylomicron assembly. In the intestinal crypt, acts as a
CC component of dietary-responsive phospholipid-cholesterol axis,
CC regulating the biosynthesis of cholesterol and its mitogenic effects on
CC intestinal stem cells (By similarity). {ECO:0000250|UniProtKB:Q6P1A2,
CC ECO:0000250|UniProtKB:Q91V01}.
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:Q6P1A2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12938;
CC Evidence={ECO:0000250|UniProtKB:Q6P1A2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-acyl-sn-glycero-3-phosphoethanolamine + an acyl-CoA = a
CC 1,2-diacyl-sn-glycero-3-phosphoethanolamine + CoA;
CC Xref=Rhea:RHEA:32995, ChEBI:CHEBI:57287, ChEBI:CHEBI:58342,
CC ChEBI:CHEBI:64381, ChEBI:CHEBI:64612; EC=2.3.1.n7;
CC Evidence={ECO:0000250|UniProtKB:Q6P1A2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32996;
CC Evidence={ECO:0000250|UniProtKB:Q6P1A2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-acyl-sn-glycero-3-phospho-L-serine + an acyl-CoA = a 1,2-
CC diacyl-sn-glycero-3-phospho-L-serine + CoA; Xref=Rhea:RHEA:33191,
CC ChEBI:CHEBI:57262, ChEBI:CHEBI:57287, ChEBI:CHEBI:58342,
CC ChEBI:CHEBI:64379; EC=2.3.1.n6;
CC Evidence={ECO:0000250|UniProtKB:Q6P1A2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33192;
CC Evidence={ECO:0000250|UniProtKB:Q6P1A2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z)-octadecadienoyl-CoA + a 1-acyl-sn-glycero-3-
CC phosphocholine = 1-acyl-2-(9Z,12Z)-octadecadienoyl-sn-glycero-3-
CC phosphocholine + CoA; Xref=Rhea:RHEA:37563, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57383, ChEBI:CHEBI:58168, ChEBI:CHEBI:60000;
CC Evidence={ECO:0000250|UniProtKB:Q6P1A2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37564;
CC Evidence={ECO:0000250|UniProtKB:Q6P1A2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + a 1-acyl-sn-glycero-3-
CC phosphocholine = 1-acyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-
CC glycero-3-phosphocholine + CoA; Xref=Rhea:RHEA:37559,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57368, ChEBI:CHEBI:58168,
CC ChEBI:CHEBI:75063; Evidence={ECO:0000250|UniProtKB:Q6P1A2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37560;
CC Evidence={ECO:0000250|UniProtKB:Q6P1A2};
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:Q6P1A2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37516;
CC Evidence={ECO:0000250|UniProtKB:Q6P1A2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-sn-glycero-3-phosphocholine + octadecanoyl-CoA
CC = 1-hexadecanoyl-2-octadecanoyl-sn-glycero-3-phosphocholine + CoA;
CC Xref=Rhea:RHEA:35987, ChEBI:CHEBI:57287, ChEBI:CHEBI:57394,
CC ChEBI:CHEBI:72998, ChEBI:CHEBI:73000;
CC Evidence={ECO:0000250|UniProtKB:Q6P1A2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35988;
CC Evidence={ECO:0000250|UniProtKB:Q6P1A2};
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:Q6P1A2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37512;
CC Evidence={ECO:0000250|UniProtKB:Q6P1A2};
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:Q6P1A2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37656;
CC Evidence={ECO:0000250|UniProtKB:Q6P1A2};
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:Q6P1A2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35984;
CC Evidence={ECO:0000250|UniProtKB:Q6P1A2};
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:Q6P1A2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37528;
CC Evidence={ECO:0000250|UniProtKB:Q6P1A2};
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:Q6P1A2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37384;
CC Evidence={ECO:0000250|UniProtKB:Q6P1A2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-hexadecenoyl-CoA + 1-hexadecanoyl-sn-glycero-3-
CC phosphocholine = 1-hexadecanoyl-2-(9Z-hexadecenoyl)-sn-glycero-3-
CC phosphocholine + CoA; Xref=Rhea:RHEA:37207, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:61540, ChEBI:CHEBI:72998, ChEBI:CHEBI:74000;
CC Evidence={ECO:0000250|UniProtKB:Q6P1A2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37208;
CC Evidence={ECO:0000250|UniProtKB:Q6P1A2};
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:Q6P1A2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35992;
CC Evidence={ECO:0000250|UniProtKB:Q6P1A2};
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:Q6P1A2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35996;
CC Evidence={ECO:0000250|UniProtKB:Q6P1A2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + 1-dodecanoyl-sn-
CC glycero-3-phosphocholine = 1-dodecanoyl-2-(5Z,8Z,11Z,14Z)-
CC eicosatetraenoyl-sn-glycero-3-phosphocholine + CoA;
CC Xref=Rhea:RHEA:37483, ChEBI:CHEBI:57287, ChEBI:CHEBI:57368,
CC ChEBI:CHEBI:74966, ChEBI:CHEBI:74967;
CC Evidence={ECO:0000250|UniProtKB:Q91V01};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37484;
CC Evidence={ECO:0000250|UniProtKB:Q91V01};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + 1-hexadecanoyl-sn-
CC glycero-3-phosphocholine = 1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-
CC eicosatetraenoyl)-sn-glycero-3-phosphocholine + CoA;
CC Xref=Rhea:RHEA:35999, ChEBI:CHEBI:57287, ChEBI:CHEBI:57368,
CC ChEBI:CHEBI:72998, ChEBI:CHEBI:73003;
CC Evidence={ECO:0000250|UniProtKB:Q6P1A2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36000;
CC Evidence={ECO:0000250|UniProtKB:Q6P1A2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + 1-octadecanoyl-sn-
CC glycero-3-phosphocholine = 1-octadecanoyl-2-(5Z,8Z,11Z,14Z-
CC eicosatetraenoyl)-sn-glycero-3-phosphocholine + CoA;
CC Xref=Rhea:RHEA:37479, ChEBI:CHEBI:57287, ChEBI:CHEBI:57368,
CC ChEBI:CHEBI:73858, ChEBI:CHEBI:74965;
CC Evidence={ECO:0000250|UniProtKB:Q91V01};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37480;
CC Evidence={ECO:0000250|UniProtKB:Q91V01};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + 1-eicosanoyl-sn-
CC glycero-3-phosphocholine = 1-eicosanoyl-2-(5Z,8Z,11Z,14Z)-
CC eicosatetraenoyl-sn-glycero-3-phosphocholine + CoA;
CC Xref=Rhea:RHEA:37487, ChEBI:CHEBI:57287, ChEBI:CHEBI:57368,
CC ChEBI:CHEBI:74968, ChEBI:CHEBI:74970;
CC Evidence={ECO:0000250|UniProtKB:Q91V01};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37488;
CC Evidence={ECO:0000250|UniProtKB:Q91V01};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 1-(9Z-octadecenoyl)-sn-glycero-3-
CC phosphocholine = 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine
CC + CoA; Xref=Rhea:RHEA:37387, ChEBI:CHEBI:28610, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57387, ChEBI:CHEBI:74669;
CC Evidence={ECO:0000250|UniProtKB:Q6P1A2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37388;
CC Evidence={ECO:0000250|UniProtKB:Q6P1A2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z)-octadecadienoyl-CoA + 1-(9Z-octadecenoyl)-sn-glycero-
CC 3-phosphocholine = 1-(9Z)-octadecenoyl-2-(9Z,12Z)-octadecadienoyl-sn-
CC glycero-3-phosphocholine + CoA; Xref=Rhea:RHEA:37391,
CC ChEBI:CHEBI:28610, ChEBI:CHEBI:57287, ChEBI:CHEBI:57383,
CC ChEBI:CHEBI:74670; Evidence={ECO:0000250|UniProtKB:Q6P1A2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37392;
CC Evidence={ECO:0000250|UniProtKB:Q6P1A2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + 1-(9Z-octadecenoyl)-sn-
CC glycero-3-phosphocholine = 1-(9Z)-octadecenoyl-2-(5Z,8Z,11Z,14Z)-
CC icosatetraenoyl-sn-glycero-3-phosphocholine + CoA;
CC Xref=Rhea:RHEA:37395, ChEBI:CHEBI:28610, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57368, ChEBI:CHEBI:74671;
CC Evidence={ECO:0000250|UniProtKB:Q6P1A2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37396;
CC Evidence={ECO:0000250|UniProtKB:Q6P1A2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z)-octadecadienoyl-CoA + a 1-acyl-sn-glycero-3-
CC phosphoethanolamine = 1-acyl-2-(9Z,12Z)-octadecadienoyl-sn-glycero-3-
CC phosphoethanolamine + CoA; Xref=Rhea:RHEA:37579, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57383, ChEBI:CHEBI:64381, ChEBI:CHEBI:75069;
CC Evidence={ECO:0000250|UniProtKB:Q6P1A2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37580;
CC Evidence={ECO:0000250|UniProtKB:Q6P1A2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z)-octadecadienoyl-CoA + 1-(9Z-octadecenoyl)-sn-glycero-
CC 3-phosphoethanolamine = 1-(9Z)-octadecenoyl-2-(9Z,12Z)-
CC octadecadienoyl-sn-glycero-3-phosphoethanolamine + CoA;
CC Xref=Rhea:RHEA:37503, ChEBI:CHEBI:57287, ChEBI:CHEBI:57383,
CC ChEBI:CHEBI:74971, ChEBI:CHEBI:74977;
CC Evidence={ECO:0000250|UniProtKB:Q91V01};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37504;
CC Evidence={ECO:0000250|UniProtKB:Q91V01};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z)-octadecadienoyl-CoA + 1-(10Z-heptadecenoyl)-sn-
CC glycero-3-phosphoethanolamine = 1-(10Z-heptadecenoyl)-2-(9Z,12Z-
CC octadecadienoyl)-sn-glycero-3-phosphoethanolamine + CoA;
CC Xref=Rhea:RHEA:64228, ChEBI:CHEBI:57287, ChEBI:CHEBI:57383,
CC ChEBI:CHEBI:149768, ChEBI:CHEBI:149770;
CC Evidence={ECO:0000250|UniProtKB:Q91V01};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64229;
CC Evidence={ECO:0000250|UniProtKB:Q91V01};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + a 1-acyl-sn-glycero-3-
CC phosphoethanolamine = 1-acyl-2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-
CC glycero-3-phosphoethanolamine + CoA; Xref=Rhea:RHEA:37575,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57368, ChEBI:CHEBI:64381,
CC ChEBI:CHEBI:75067; Evidence={ECO:0000250|UniProtKB:Q6P1A2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37576;
CC Evidence={ECO:0000250|UniProtKB:Q6P1A2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + 1-hexadecanoyl-sn-
CC glycero-3-phosphoethanolamine = 1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-
CC eicosatetraenoyl)-sn-glycero-3-phosphoethanolamine + CoA;
CC Xref=Rhea:RHEA:36023, ChEBI:CHEBI:57287, ChEBI:CHEBI:57368,
CC ChEBI:CHEBI:73004, ChEBI:CHEBI:73009;
CC Evidence={ECO:0000250|UniProtKB:Q6P1A2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36024;
CC Evidence={ECO:0000250|UniProtKB:Q6P1A2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + 1-(9Z-octadecenoyl)-sn-
CC glycero-3-phosphoethanolamine = 1-(9Z)-octadecenoyl-2-
CC (5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero-3-phosphoethanolamine +
CC CoA; Xref=Rhea:RHEA:37495, ChEBI:CHEBI:57287, ChEBI:CHEBI:57368,
CC ChEBI:CHEBI:74971, ChEBI:CHEBI:74975;
CC Evidence={ECO:0000250|UniProtKB:Q91V01};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37496;
CC Evidence={ECO:0000250|UniProtKB:Q91V01};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + 1-(10Z-heptadecenoyl)-
CC sn-glycero-3-phosphoethanolamine = 1-(10Z-heptadecenoyl)-2-
CC (5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphoethanolamine +
CC CoA; Xref=Rhea:RHEA:64204, ChEBI:CHEBI:57287, ChEBI:CHEBI:57368,
CC ChEBI:CHEBI:149768, ChEBI:CHEBI:149769;
CC Evidence={ECO:0000250|UniProtKB:Q91V01};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64205;
CC Evidence={ECO:0000250|UniProtKB:Q91V01};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + 1-O-(1Z-alkenyl)-sn-
CC glycero-3-phosphoethanolamine = 1-O-(1Z)-alkenyl-2-(5Z,8Z,11Z,14Z)-
CC eicosatetraenoyl-sn-glycero-3-phosphoethanolamine + CoA;
CC Xref=Rhea:RHEA:37635, ChEBI:CHEBI:57287, ChEBI:CHEBI:57368,
CC ChEBI:CHEBI:77288, ChEBI:CHEBI:77295;
CC Evidence={ECO:0000250|UniProtKB:Q91V01};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37636;
CC Evidence={ECO:0000250|UniProtKB:Q91V01};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z)-octadecadienoyl-CoA + a 1-acyl-sn-glycero-3-phospho-
CC L-serine = 1-acyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phospho-L-
CC serine + CoA; Xref=Rhea:RHEA:37567, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57383, ChEBI:CHEBI:64379, ChEBI:CHEBI:75066;
CC Evidence={ECO:0000250|UniProtKB:Q6P1A2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37568;
CC Evidence={ECO:0000250|UniProtKB:Q6P1A2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + a 1-acyl-sn-glycero-3-
CC phospho-L-serine = 1-acyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-
CC glycero-3-phospho-L-serine + CoA; Xref=Rhea:RHEA:37571,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57368, ChEBI:CHEBI:64379,
CC ChEBI:CHEBI:75065; Evidence={ECO:0000250|UniProtKB:Q6P1A2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37572;
CC Evidence={ECO:0000250|UniProtKB:Q6P1A2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 1-hexadecanoyl-sn-glycero-3-phospho-L-
CC serine = 1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phospho-L-
CC serine + CoA; Xref=Rhea:RHEA:37531, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57387, ChEBI:CHEBI:75020, ChEBI:CHEBI:75029;
CC Evidence={ECO:0000250|UniProtKB:Q6P1A2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37532;
CC Evidence={ECO:0000250|UniProtKB:Q6P1A2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 1-(9Z-octadecenoyl)-sn-glycero-3-
CC phospho-L-serine = 1,2-di-(9Z)-octadecenoyl-sn-glycero-3-phospho-L-
CC serine + CoA; Xref=Rhea:RHEA:37407, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57387, ChEBI:CHEBI:74617, ChEBI:CHEBI:74905;
CC Evidence={ECO:0000250|UniProtKB:Q91V01};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37408;
CC Evidence={ECO:0000250|UniProtKB:Q91V01};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z)-octadecadienoyl-CoA + 1-hexadecanoyl-sn-glycero-3-
CC phospho-L-serine = 1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-
CC glycero-3-phospho-L-serine + CoA; Xref=Rhea:RHEA:37535,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57383, ChEBI:CHEBI:75020,
CC ChEBI:CHEBI:75031; Evidence={ECO:0000250|UniProtKB:Q6P1A2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37536;
CC Evidence={ECO:0000250|UniProtKB:Q6P1A2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z)-octadecadienoyl-CoA + 1-(9Z-octadecenoyl)-sn-glycero-
CC 3-phospho-L-serine = 1-(9Z-octadecenoyl)-2-(9Z,12Z-octadienoyl)-sn-
CC glycero-3-phospho-L-serine + CoA; Xref=Rhea:RHEA:37375,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57383, ChEBI:CHEBI:74617,
CC ChEBI:CHEBI:74892; Evidence={ECO:0000250|UniProtKB:Q6P1A2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37376;
CC Evidence={ECO:0000250|UniProtKB:Q6P1A2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + 1-hexadecanoyl-sn-
CC glycero-3-phospho-L-serine = 1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-
CC eicosatetraenoyl)-sn-glycero-3-phospho-L-serine + CoA;
CC Xref=Rhea:RHEA:37539, ChEBI:CHEBI:57287, ChEBI:CHEBI:57368,
CC ChEBI:CHEBI:75020, ChEBI:CHEBI:75032;
CC Evidence={ECO:0000250|UniProtKB:Q6P1A2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37540;
CC Evidence={ECO:0000250|UniProtKB:Q6P1A2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + 1-(9Z-octadecenoyl)-sn-
CC glycero-3-phospho-L-serine = 1-(9Z-octadecenoyl)-2-(5Z,8Z,11Z,14Z-
CC eicosatetraenoyl)-sn-glycero-3-phospho-L-serine + CoA;
CC Xref=Rhea:RHEA:37379, ChEBI:CHEBI:57287, ChEBI:CHEBI:57368,
CC ChEBI:CHEBI:74617, ChEBI:CHEBI:74897;
CC Evidence={ECO:0000250|UniProtKB:Q6P1A2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37380;
CC Evidence={ECO:0000250|UniProtKB:Q6P1A2};
CC -!- PATHWAY: Lipid metabolism; phospholipid metabolism.
CC {ECO:0000250|UniProtKB:Q6P1A2}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q6P1A2}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- DOMAIN: The di-lysine motif confers endoplasmic reticulum localization.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the membrane-bound acyltransferase family.
CC {ECO:0000255}.
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DR EMBL; BC089869; AAH89869.1; -; mRNA.
DR RefSeq; NP_001012189.1; NM_001012189.1.
DR RefSeq; XP_017448194.1; XM_017592705.1.
DR AlphaFoldDB; Q5FVN0; -.
DR SMR; Q5FVN0; -.
DR STRING; 10116.ENSRNOP00000017090; -.
DR GlyGen; Q5FVN0; 1 site.
DR iPTMnet; Q5FVN0; -.
DR PhosphoSitePlus; Q5FVN0; -.
DR jPOST; Q5FVN0; -.
DR PaxDb; Q5FVN0; -.
DR PRIDE; Q5FVN0; -.
DR Ensembl; ENSRNOT00000017090; ENSRNOP00000017090; ENSRNOG00000012269.
DR GeneID; 362434; -.
DR KEGG; rno:362434; -.
DR UCSC; RGD:1310223; rat.
DR CTD; 10162; -.
DR RGD; 1310223; Lpcat3.
DR eggNOG; KOG2705; Eukaryota.
DR GeneTree; ENSGT01030000234564; -.
DR HOGENOM; CLU_011340_6_1_1; -.
DR InParanoid; Q5FVN0; -.
DR OMA; CILVLRM; -.
DR OrthoDB; 881262at2759; -.
DR PhylomeDB; Q5FVN0; -.
DR TreeFam; TF106143; -.
DR Reactome; R-RNO-1482788; Acyl chain remodelling of PC.
DR Reactome; R-RNO-1482801; Acyl chain remodelling of PS.
DR Reactome; R-RNO-1482839; Acyl chain remodelling of PE.
DR UniPathway; UPA00085; -.
DR PRO; PR:Q5FVN0; -.
DR Proteomes; UP000002494; Chromosome 4.
DR Bgee; ENSRNOG00000012269; Expressed in ovary and 19 other tissues.
DR Genevisible; Q5FVN0; RN.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0047184; F:1-acylglycerophosphocholine O-acyltransferase activity; ISS:UniProtKB.
DR GO; GO:0106262; F:1-acylglycerophosphoethanolamine O-acyltransferase activity; ISS:UniProtKB.
DR GO; GO:0106263; F:1-acylglycerophosphoserine O-acyltransferase activity; ISS:UniProtKB.
DR GO; GO:0016746; F:acyltransferase activity; IBA:GO_Central.
DR GO; GO:0071617; F:lysophospholipid acyltransferase activity; IBA:GO_Central.
DR GO; GO:0034378; P:chylomicron assembly; ISS:UniProtKB.
DR GO; GO:0090158; P:endoplasmic reticulum membrane organization; ISS:UniProtKB.
DR GO; GO:0036335; P:intestinal stem cell homeostasis; ISS:UniProtKB.
DR GO; GO:0030258; P:lipid modification; IBA:GO_Central.
DR GO; GO:0050728; P:negative regulation of inflammatory response; ISS:UniProtKB.
DR GO; GO:1903573; P:negative regulation of response to endoplasmic reticulum stress; ISS:UniProtKB.
DR GO; GO:0036151; P:phosphatidylcholine acyl-chain remodeling; ISS:UniProtKB.
DR GO; GO:0006656; P:phosphatidylcholine biosynthetic process; IBA:GO_Central.
DR GO; GO:0036152; P:phosphatidylethanolamine acyl-chain remodeling; ISS:UniProtKB.
DR GO; GO:0036150; P:phosphatidylserine acyl-chain remodeling; ISS:UniProtKB.
DR GO; GO:0045797; P:positive regulation of intestinal cholesterol absorption; ISS:UniProtKB.
DR GO; GO:1901310; P:positive regulation of sterol regulatory element binding protein cleavage; ISS:UniProtKB.
DR GO; GO:1905885; P:positive regulation of triglyceride transport; ISS:UniProtKB.
DR GO; GO:0045540; P:regulation of cholesterol biosynthetic process; ISS:UniProtKB.
DR GO; GO:0097006; P:regulation of plasma lipoprotein particle levels; ISO:RGD.
DR GO; GO:0034379; P:very-low-density lipoprotein particle assembly; ISS:UniProtKB.
DR InterPro; IPR004299; MBOAT_fam.
DR Pfam; PF03062; MBOAT; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Acyltransferase; Endoplasmic reticulum; Glycoprotein;
KW Lipid biosynthesis; Lipid metabolism; Membrane; Phospholipid biosynthesis;
KW Phospholipid metabolism; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q6P1A2"
FT CHAIN 2..487
FT /note="Lysophospholipid acyltransferase 5"
FT /id="PRO_0000233384"
FT TRANSMEM 44..64
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 67..87
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 111..131
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 178..198
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 236..256
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 285..305
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 364..384
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 422..442
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 453..473
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOTIF 484..487
FT /note="Di-lysine motif"
FT ACT_SITE 338
FT /evidence="ECO:0000250"
FT ACT_SITE 374
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q6P1A2"
FT CARBOHYD 308
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 487 AA; 56018 MW; 29F44D92190957A2 CRC64;
MASTADGDVG ETLGQMRGLW PGVEDLSLNK LATSLGASEQ ALRLIFSIFL GYPLALFYRH
YLFYKDSYLI HLFHAFSGLS IAYFNFGHQF YHSLLCVVLQ FLILRLMGRT ITAVFTTLCF
QMAYLLAGYY YTATGDYDIK WTMPHCVLTL KLIGLSIDYY DGGKDRNSLS SEQQKYAILG
VPSLLEVAGF SYFYGAFLVG PQFSMNHYMK LVKGQLTDVP GKMPNSTIPA LKRLSLGLVY
LVGYTLLSPH ITEDYLLTED YDTRPFWFRC MYMLIWGKFV LYKYVTCWLV TEGVCILSGL
GFNGFEENGT VKWDACANMK VWLFETTPRF TGTIASFNIN TNAWVARYIF KRLKFLGNKE
LSQGLSLLFL ALWHGLHSGY LICFQMEFLI VIVEKQATNL IRDSPALSSL ASITALQPFY
YLVQQTIHWL FMGYSMTAFC LFTWDKWLKV YRSIYFLGHV FFLSLLFTLP YVYKAMVPRK
EKLKKRE
