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MBOA5_BOVIN
ID   MBOA5_BOVIN             Reviewed;         485 AA.
AC   Q3SZL3; Q58CS9;
DT   02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   03-AUG-2022, entry version 88.
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=MBOAT5, OACT5;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA   Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA   Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT   "Characterization of 954 bovine full-CDS cDNA sequences.";
RL   BMC Genomics 6:166-166(2005).
RN   [2] {ECO:0000312|EMBL:AAX46715.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Crossbred X Angus {ECO:0000312|EMBL:AAI02803.1};
RC   TISSUE=Ileum {ECO:0000312|EMBL:AAI02803.1};
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAX46715.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; BT021868; AAX46715.1; ALT_FRAME; mRNA.
DR   EMBL; BC102802; AAI02803.1; -; mRNA.
DR   RefSeq; NP_001019717.2; NM_001024546.2.
DR   AlphaFoldDB; Q3SZL3; -.
DR   SMR; Q3SZL3; -.
DR   STRING; 9913.ENSBTAP00000052356; -.
DR   PaxDb; Q3SZL3; -.
DR   PRIDE; Q3SZL3; -.
DR   GeneID; 515361; -.
DR   KEGG; bta:515361; -.
DR   CTD; 10162; -.
DR   eggNOG; KOG2705; Eukaryota.
DR   InParanoid; Q3SZL3; -.
DR   OrthoDB; 881262at2759; -.
DR   UniPathway; UPA00085; -.
DR   Proteomes; UP000009136; Unplaced.
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: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; Lipid biosynthesis;
KW   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..485
FT                   /note="Lysophospholipid acyltransferase 5"
FT                   /id="PRO_0000233381"
FT   TRANSMEM        35..55
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        82..102
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        108..128
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        139..158
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        176..196
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        232..252
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        283..303
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        362..382
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        420..440
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        448..468
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   MOTIF           482..485
FT                   /note="Di-lysine motif"
FT   ACT_SITE        336
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        372
FT                   /evidence="ECO:0000250"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6P1A2"
SQ   SEQUENCE   485 AA;  55834 MW;  4C9EAFBDBF7D2F2E CRC64;
     MASAAEGDME AELTRGLLWG FQDLSLNKLA TSLGASEQAL RLIISIFLGY PFALFYRRYL
     FYKDSYLIHL FHTFTGLSIA YYNFGTQLYH SLLCIVLQFL ILRLMGRTIT AVLTTFCVQM
     GYLLAGYYNT ATGTYDIKWT MPHCVLTLKL IGLAMDYYDG GKDQKSLTSE QQIYAIWGVP
     SLLEISGFSY FYGAFLVGPQ FSMNHYMKLV RGELTDVPGK IPNSTIPALR RLALGLVYLV
     GYTLLSPHIT EDYLLSDDYE NGSFWFRCMY MLIWGKFVLY KYVTCWLVTE GVCILTGLGF
     NGLDEYGTAK WDACANMKVW LFETTPRFTG TIASFNINTN AWVARYFFKR LKFLGNKVLS
     QGLSLLFLAL WHGLHSGYLV CFQMEFLIVI VERQAASLIR DSPVLSRLAS ITVLQPLYYL
     AQQTIHWLFM GYSMTAFCLF TWDKWMKVYK SIYFLGHVFF LSLLFILPYV RKVMVPRKEK
     LKKME
 
 
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