LPCT4_MOUSE
ID LPCT4_MOUSE Reviewed; 524 AA.
AC Q6NVG1; Q66JP7;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Lysophospholipid acyltransferase LPCAT4;
DE AltName: Full=1-acylglycerol-3-phosphate O-acyltransferase 7;
DE Short=1-AGP acyltransferase 7;
DE Short=1-AGPAT 7;
DE AltName: Full=1-acylglycerophosphocholine O-acyltransferase;
DE EC=2.3.1.23 {ECO:0000269|PubMed:18156367};
DE AltName: Full=1-acylglycerophosphoserine O-acyltransferase;
DE EC=2.3.1.n6 {ECO:0000250|UniProtKB:Q643R3};
DE AltName: Full=1-alkenylglycerophosphoethanolamine O-acyltransferase;
DE EC=2.3.1.121 {ECO:0000250|UniProtKB:Q643R3};
DE AltName: Full=1-alkylglycerophosphocholine O-acetyltransferase;
DE EC=2.3.1.67 {ECO:0000250|UniProtKB:Q643R3};
DE AltName: Full=Acyltransferase-like 3;
DE AltName: Full=Lysophosphatidylcholine acyltransferase 4;
DE AltName: Full=Lysophosphatidylethanolamine acyltransferase 2;
DE EC=2.3.1.n7 {ECO:0000250|UniProtKB:Q643R3};
DE AltName: Full=Plasmalogen synthase;
GN Name=Lpcat4; Synonyms=Agpat7, Aytl3;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain, and Embryo;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, 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 [3]
RP TISSUE SPECIFICITY.
RX PubMed=18458083; DOI=10.1074/jbc.m800364200;
RA Cao J., Shan D., Revett T., Li D., Wu L., Liu W., Tobin J.F., Gimeno R.E.;
RT "Molecular identification of a novel mammalian brain isoform of acyl-
RT CoA:lysophospholipid acyltransferase with prominent ethanolamine
RT lysophospholipid acylating activity, LPEAT2.";
RL J. Biol. Chem. 283:19049-19057(2008).
CC -!- FUNCTION: Displays acyl-CoA-dependent lysophospholipid acyltransferase
CC activity with a subset of lysophospholipids as substrates; converts
CC lysophosphatidylethanolamine to phosphatidylethanolamine, 1-alkenyl-
CC lysophatidylethanolamine to 1-alkenyl-phosphatidylethanolamine,
CC lysophosphatidylglycerol and alkyl-lysophosphatidylcholine to
CC phosphatidylglycerol and alkyl-phosphatidylcholine, respectively. In
CC contrast, has no lysophosphatidylinositol, glycerol-3-phosphate,
CC diacylglycerol or lysophosphatidic acid acyltransferase activity.
CC Prefers long chain acyl-CoAs (C16, C18) as acyl donors (By similarity).
CC Converts lysophosphatidylcholine to phosphatidycholine
CC (PubMed:18156367). {ECO:0000250, ECO:0000250|UniProtKB:Q643R3,
CC ECO:0000269|PubMed:18156367}.
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:Q643R3};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-O-(1Z-alkenyl)-sn-glycero-3-phosphoethanolamine + an acyl-
CC CoA = 1-O-(1Z-alkenyl)-2-acyl-sn-glycero-3-phosphoethanolamine + CoA;
CC Xref=Rhea:RHEA:16245, ChEBI:CHEBI:57287, ChEBI:CHEBI:58342,
CC ChEBI:CHEBI:77288, ChEBI:CHEBI:77290; EC=2.3.1.121;
CC Evidence={ECO:0000250|UniProtKB:Q643R3};
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: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:0000250|UniProtKB:Q643R3};
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:Q643R3};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-acyl-sn-glycero-3-phosphoethanolamine + octanoyl-CoA = 1-
CC acyl-2-octanoyl-sn-glycero-3-phosphoethanolamine + CoA;
CC Xref=Rhea:RHEA:37775, ChEBI:CHEBI:57287, ChEBI:CHEBI:57386,
CC ChEBI:CHEBI:64381, ChEBI:CHEBI:75263;
CC Evidence={ECO:0000250|UniProtKB:Q643R3};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37776;
CC Evidence={ECO:0000250|UniProtKB:Q643R3};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-acyl-sn-glycero-3-phosphoethanolamine + hexadecanoyl-CoA =
CC 1-acyl-2-hexadecanoyl-sn-glycero-3-phosphoethanolamine + CoA;
CC Xref=Rhea:RHEA:37767, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379,
CC ChEBI:CHEBI:64381, ChEBI:CHEBI:75265;
CC Evidence={ECO:0000250|UniProtKB:Q643R3};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37768;
CC Evidence={ECO:0000250|UniProtKB:Q643R3};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-acyl-sn-glycero-3-phosphoethanolamine + octadecanoyl-CoA =
CC 1-acyl-2-octadecanoyl-sn-glycero-3-phosphoethanolamine + CoA;
CC Xref=Rhea:RHEA:37771, ChEBI:CHEBI:57287, ChEBI:CHEBI:57394,
CC ChEBI:CHEBI:64381, ChEBI:CHEBI:75264;
CC Evidence={ECO:0000250|UniProtKB:Q643R3};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37772;
CC Evidence={ECO:0000250|UniProtKB:Q643R3};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + a 1-acyl-sn-glycero-3-
CC phosphoethanolamine = 1-acyl-2-(9Z)-octadecenoyl-sn-glycero-3-
CC phosphoethanolamine + CoA; Xref=Rhea:RHEA:37731, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57387, ChEBI:CHEBI:64381, ChEBI:CHEBI:75238;
CC Evidence={ECO:0000250|UniProtKB:Q643R3};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37732;
CC Evidence={ECO:0000250|UniProtKB:Q643R3};
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:Q643R3};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37576;
CC Evidence={ECO:0000250|UniProtKB:Q643R3};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-O-(1Z-alkenyl)-sn-glycero-3-phosphoethanolamine + octanoyl-
CC CoA = 1-O-(1Z)-alkenyl-2-octanoyl-sn-glycero-3-phosphoethanolamine +
CC CoA; Xref=Rhea:RHEA:37763, ChEBI:CHEBI:57287, ChEBI:CHEBI:57386,
CC ChEBI:CHEBI:77288, ChEBI:CHEBI:77301;
CC Evidence={ECO:0000250|UniProtKB:Q643R3};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37764;
CC Evidence={ECO:0000250|UniProtKB:Q643R3};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-O-(1Z-alkenyl)-sn-glycero-3-phosphoethanolamine +
CC hexadecanoyl-CoA = 1-O-(1Z)-alkenyl-2-hexadecanoyl-sn-glycero-3-
CC phosphoethanolamine + CoA; Xref=Rhea:RHEA:37755, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57379, ChEBI:CHEBI:77288, ChEBI:CHEBI:77303;
CC Evidence={ECO:0000250|UniProtKB:Q643R3};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37756;
CC Evidence={ECO:0000250|UniProtKB:Q643R3};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-O-(1Z-alkenyl)-sn-glycero-3-phosphoethanolamine +
CC octadecanoyl-CoA = 1-O-(1Z)-alkenyl-2-octadecanoyl-sn-glycero-3-
CC phosphoethanolamine + CoA; Xref=Rhea:RHEA:37759, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57394, ChEBI:CHEBI:77288, ChEBI:CHEBI:77302;
CC Evidence={ECO:0000250|UniProtKB:Q643R3};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37760;
CC Evidence={ECO:0000250|UniProtKB:Q643R3};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 1-O-(1Z-alkenyl)-sn-glycero-3-
CC phosphoethanolamine = 1-O-(1Z)-alkenyl-2-(9Z)-octadecenoyl-sn-
CC glycero-3-phosphoethanolamine + CoA; Xref=Rhea:RHEA:37631,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57387, ChEBI:CHEBI:77288,
CC ChEBI:CHEBI:77291; Evidence={ECO:0000250|UniProtKB:Q643R3};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37632;
CC Evidence={ECO:0000250|UniProtKB:Q643R3};
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:Q643R3};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37636;
CC Evidence={ECO:0000250|UniProtKB:Q643R3};
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:0000269|PubMed:18156367};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37804;
CC Evidence={ECO:0000305|PubMed:18156367};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + a 1-acyl-sn-glycero-3-phosphocholine =
CC 1-acyl-2-(9Z)-octadecenoyl-sn-glycero-3-phosphocholine + CoA;
CC Xref=Rhea:RHEA:33359, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387,
CC ChEBI:CHEBI:58168, ChEBI:CHEBI:58293;
CC Evidence={ECO:0000269|PubMed:18156367};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33360;
CC Evidence={ECO:0000305|PubMed:18156367};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 1-O-hexadecyl-sn-glycero-3-
CC phosphocholine = 1-O-hexadecyl-2-(9Z)-octadecenoyl-sn-glycero-3-
CC phosphocholine + CoA; Xref=Rhea:RHEA:37783, ChEBI:CHEBI:34112,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57387, ChEBI:CHEBI:64496;
CC Evidence={ECO:0000250|UniProtKB:Q643R3};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37784;
CC Evidence={ECO:0000250|UniProtKB:Q643R3};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + 1-O-hexadecyl-sn-
CC glycero-3-phosphocholine = 1-O-hexadecyl-2-(5Z,8Z,11Z,14Z)-
CC eicosatetraenoyl-sn-glycero-3-phosphocholine + CoA;
CC Xref=Rhea:RHEA:37787, ChEBI:CHEBI:55430, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57368, ChEBI:CHEBI:64496;
CC Evidence={ECO:0000250|UniProtKB:Q643R3};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37788;
CC Evidence={ECO:0000250|UniProtKB:Q643R3};
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:Q643R3};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37532;
CC Evidence={ECO:0000250|UniProtKB:Q643R3};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 1-octadecanoyl-sn-glycero-3-phospho-
CC (1'-sn-glycerol) = 1-octadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-
CC phospho-(1'-sn-glycerol) + CoA; Xref=Rhea:RHEA:37647,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57387, ChEBI:CHEBI:72827,
CC ChEBI:CHEBI:72845; Evidence={ECO:0000250|UniProtKB:Q643R3};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37648;
CC Evidence={ECO:0000250|UniProtKB:Q643R3};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + 1-octadecanoyl-sn-
CC glycero-3-phospho-(1'-sn-glycerol) = 1-octadecanoyl-2-(5Z,8Z,11Z,14Z-
CC eicosatetraenoyl)-sn-glycero-3-phospho-(1'-sn-glycerol) + CoA;
CC Xref=Rhea:RHEA:37779, ChEBI:CHEBI:57287, ChEBI:CHEBI:57368,
CC ChEBI:CHEBI:72827, ChEBI:CHEBI:75266;
CC Evidence={ECO:0000250|UniProtKB:Q643R3};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37780;
CC Evidence={ECO:0000250|UniProtKB:Q643R3};
CC -!- PATHWAY: Lipid metabolism; phospholipid metabolism.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q643R3}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Widely expressed with much higher level in brain.
CC Expressed in erythroleukemic cells but not in reticulocytes.
CC {ECO:0000269|PubMed:18156367, ECO:0000269|PubMed:18458083}.
CC -!- SIMILARITY: Belongs to the 1-acyl-sn-glycerol-3-phosphate
CC acyltransferase family. {ECO:0000305}.
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DR EMBL; BC068131; AAH68131.1; -; mRNA.
DR EMBL; BC080829; AAH80829.1; -; mRNA.
DR CCDS; CCDS16548.1; -.
DR RefSeq; NP_997089.1; NM_207206.2.
DR AlphaFoldDB; Q6NVG1; -.
DR SMR; Q6NVG1; -.
DR BioGRID; 221169; 1.
DR STRING; 10090.ENSMUSP00000028554; -.
DR GlyGen; Q6NVG1; 1 site.
DR iPTMnet; Q6NVG1; -.
DR PhosphoSitePlus; Q6NVG1; -.
DR SwissPalm; Q6NVG1; -.
DR EPD; Q6NVG1; -.
DR MaxQB; Q6NVG1; -.
DR PaxDb; Q6NVG1; -.
DR PeptideAtlas; Q6NVG1; -.
DR PRIDE; Q6NVG1; -.
DR ProteomicsDB; 290143; -.
DR Antibodypedia; 22726; 65 antibodies from 22 providers.
DR DNASU; 99010; -.
DR Ensembl; ENSMUST00000028554; ENSMUSP00000028554; ENSMUSG00000027134.
DR GeneID; 99010; -.
DR KEGG; mmu:99010; -.
DR UCSC; uc008loo.1; mouse.
DR CTD; 254531; -.
DR MGI; MGI:2138993; Lpcat4.
DR VEuPathDB; HostDB:ENSMUSG00000027134; -.
DR eggNOG; KOG4666; Eukaryota.
DR GeneTree; ENSGT01030000234574; -.
DR HOGENOM; CLU_025017_1_0_1; -.
DR InParanoid; Q6NVG1; -.
DR OMA; PGRLLYQ; -.
DR OrthoDB; 1266853at2759; -.
DR PhylomeDB; Q6NVG1; -.
DR TreeFam; TF323244; -.
DR BRENDA; 2.3.1.23; 3474.
DR Reactome; R-MMU-1482788; Acyl chain remodelling of PC.
DR Reactome; R-MMU-1482801; Acyl chain remodelling of PS.
DR Reactome; R-MMU-1482839; Acyl chain remodelling of PE.
DR Reactome; R-MMU-1482925; Acyl chain remodelling of PG.
DR Reactome; R-MMU-1483166; Synthesis of PA.
DR UniPathway; UPA00085; -.
DR BioGRID-ORCS; 99010; 3 hits in 75 CRISPR screens.
DR ChiTaRS; Lpcat4; mouse.
DR PRO; PR:Q6NVG1; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q6NVG1; protein.
DR Bgee; ENSMUSG00000027134; Expressed in superior frontal gyrus and 106 other tissues.
DR Genevisible; Q6NVG1; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0047184; F:1-acylglycerophosphocholine O-acyltransferase activity; IDA: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:0047166; F:1-alkenylglycerophosphoethanolamine O-acyltransferase activity; ISS:UniProtKB.
DR GO; GO:0047192; F:1-alkylglycerophosphocholine O-acetyltransferase activity; ISS:UniProtKB.
DR GO; GO:0071617; F:lysophospholipid acyltransferase activity; ISO:MGI.
DR GO; GO:0036151; P:phosphatidylcholine acyl-chain remodeling; IDA:UniProtKB.
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:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006644; P:phospholipid metabolic process; ISO:MGI.
DR CDD; cd07991; LPLAT_LPCAT1-like; 1.
DR InterPro; IPR045252; LPCAT1-like.
DR InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR Pfam; PF01553; Acyltransferase; 1.
DR SMART; SM00563; PlsC; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Endoplasmic reticulum; Glycoprotein; Lipid biosynthesis;
KW Lipid metabolism; Membrane; Phospholipid biosynthesis;
KW Phospholipid metabolism; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..524
FT /note="Lysophospholipid acyltransferase LPCAT4"
FT /id="PRO_0000247055"
FT TRANSMEM 40..62
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 87..107
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 490..524
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 129..134
FT /note="HXXXXD motif"
FT COMPBIAS 494..516
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 152
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 301
FT /note="A -> T (in Ref. 1; AAH80829)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 524 AA; 57143 MW; 2EB97E811ED9C0E6 CRC64;
MSQGSPGAWA PLDPTSGSSA SPNPFVHELH LSGLQRVKFC LLGVLLAPIR VLLAFIVLFL
LWPFAWLQVA GLTEEQLQEP ITGWRKTVCH NGVLGLSRLL FFLLGFLRIR VRGQRASRLE
APVLVAAPHS TFFDPIVLLP CDLPKVVSRA ENLSVPVIGA LLRFNQAILV SRHDPASRRR
VVEEVRRRAT SGGKWPQVLF FPEGTCSNKK ALLKFKPGAF IAGVPVQPVL IRYPNSLDTT
SWAWRGPGVL KVLWLTASQP CSIVDVEFLP VYQPSLEESK DPTLYANNVQ RVMAQALGIP
ATECEFVGSL PVIVVGQLKV ALEPQLWELA KVLQKAGLSP GFVDMGAEPG RSRMISQEAF
AQQLQLSDPQ TVAGAFSYFQ QDAKGLVDFR NVALALAALD GGRSLEELTR LAFELFAEEQ
AEGSDRLLYK DGFSTILHLL LGSPRPAATT LHAELCQPGC SQGLSLCQFQ NFSLHDPLYG
KLFSAYLRPP HKPRSTSQIP NASSPSSPTA LANGTVQAPK QKGD
