LGAT1_MOUSE
ID LGAT1_MOUSE Reviewed; 370 AA.
AC Q91YX5;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Acyl-CoA:lysophosphatidylglycerol acyltransferase 1 {ECO:0000305};
DE AltName: Full=Acyl-CoA:monoacylglycerol acyltransferase LPGAT1 {ECO:0000305};
DE EC=2.3.1.22 {ECO:0000269|PubMed:20018982};
DE AltName: Full=Lysophospholipid acyltransferase 7 {ECO:0000303|PubMed:34890643};
DE Short=LPLAT7 {ECO:0000303|PubMed:34890643};
DE EC=2.3.1.- {ECO:0000269|PubMed:35131264};
DE AltName: Full=Stearoyl-CoA:1-lyso-2-acyl-PE acyltransferase {ECO:0000303|PubMed:35131264};
GN Name=Lpgat1 {ECO:0000312|MGI:MGI:2446186}; Synonyms=Fam34a;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND CATALYTIC
RP ACTIVITY.
RX PubMed=20018982; DOI=10.1194/jlr.m002584;
RA Hiramine Y., Emoto H., Takasuga S., Hiramatsu R.;
RT "Novel acyl-coenzyme A:monoacylglycerol acyltransferase plays an important
RT role in hepatic triacylglycerol secretion.";
RL J. Lipid Res. 51:1424-1431(2010).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Lung, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=35131264; DOI=10.1016/j.jbc.2022.101685;
RA Xu Y., Miller P.C., Phoon C.K.L., Ren M., Nargis T., Rajan S.,
RA Hussain M.M., Schlame M.;
RT "LPGAT1 controls the stearate/palmitate ratio of phosphatidylethanolamine
RT and phosphatidylcholine in sn-1 specific remodeling.";
RL J. Biol. Chem. 299:101685-101685(2022).
RN [5]
RP NOMENCLATURE.
RX PubMed=34890643; DOI=10.1016/j.jbc.2021.101470;
RA Valentine W.J., Yanagida K., Kawana H., Kono N., Noda N.N., Aoki J.,
RA Shindou H.;
RT "Update and nomenclature proposal for mammalian lysophospholipid
RT acyltransferases, which create membrane phospholipid diversity.";
RL J. Biol. Chem. 298:101470-101470(2022).
CC -!- FUNCTION: Lysophospholipid acyltransferase involved in fatty acyl chain
CC remodeling of glycerophospholipids in the endoplasmic reticulum
CC membrane (PubMed:35131264). Selectively catalyzes the transfer and
CC esterification of saturated long-chain fatty acids from acyl-CoA to the
CC sn-1 position of 1-lyso-2-acyl phosphatidylethanolamines (1-lyso-PE,
CC LPE), with a preference for stearoyl CoA over palmitoyl CoA as acyl
CC donor. Acts in concert with an unknown phospholipase A1 to convert
CC palmitate PE species into stearate ones. Provides substrates to the PE
CC methylation pathway, controlling stearate/palmitate composition of PE
CC and phosphatidylcholine (PC) species with an overall impact on de novo
CC hepatic lipid synthesis, body fat content and life span
CC (PubMed:35131264). Can acylate lysophosphatidylglycerols (LPG) using
CC various saturated fatty acyl-CoAs as acyl donors (By similarity). Can
CC also acylate monoacylglycerols with a preference for 2-
CC monoacylglycerols over 1-monoacylglycerols (PubMed:20018982,
CC PubMed:35131264). Has no activity toward lysophosphatidic acids (LPA)
CC and lysophosphatidylcholines (LPC) (PubMed:35131264).
CC {ECO:0000250|UniProtKB:Q92604, ECO:0000269|PubMed:20018982,
CC ECO:0000269|PubMed:35131264}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2-acyl-sn-glycero-3-phosphoethanolamine + octadecanoyl-CoA =
CC 1-octadecanoyl-2-acyl-sn-glycero-3-phosphoethanolamine + CoA;
CC Xref=Rhea:RHEA:70583, ChEBI:CHEBI:57287, ChEBI:CHEBI:57394,
CC ChEBI:CHEBI:65213, ChEBI:CHEBI:189703;
CC Evidence={ECO:0000269|PubMed:35131264};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70584;
CC Evidence={ECO:0000305|PubMed:35131264};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine +
CC octadecanoyl-CoA = 1-octadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-
CC phosphoethanolamine + CoA; Xref=Rhea:RHEA:70579, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57394, ChEBI:CHEBI:75038, ChEBI:CHEBI:76088;
CC Evidence={ECO:0000269|PubMed:35131264};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70580;
CC Evidence={ECO:0000305|PubMed:35131264};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2-acyl-sn-glycero-3-phosphoethanolamine + hexadecanoyl-CoA =
CC 1-hexadecanoyl-2-acyl-sn-glycero-3-phosphoethanolamine + CoA;
CC Xref=Rhea:RHEA:70595, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379,
CC ChEBI:CHEBI:65213, ChEBI:CHEBI:77370;
CC Evidence={ECO:0000269|PubMed:35131264};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70596;
CC Evidence={ECO:0000305|PubMed:35131264};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine +
CC hexadecanoyl-CoA = 1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-
CC phosphoethanolamine + CoA; Xref=Rhea:RHEA:70591, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57379, ChEBI:CHEBI:73007, ChEBI:CHEBI:76088;
CC Evidence={ECO:0000269|PubMed:35131264};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70592;
CC Evidence={ECO:0000305|PubMed:35131264};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-tetradecanoyl-sn-glycero-3-phospho-(1'-sn-glycerol) +
CC hexadecanoyl-CoA = 1-tetradecanoyl-2-hexadecanoyl-sn-glycero-3-
CC phospho-(1'-sn-glycerol) + CoA; Xref=Rhea:RHEA:35855,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57379, ChEBI:CHEBI:72826,
CC ChEBI:CHEBI:72830; Evidence={ECO:0000250|UniProtKB:Q92604};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35856;
CC Evidence={ECO:0000250|UniProtKB:Q92604};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-sn-glycero-3-phospho-(1'-sn-glycerol) +
CC dodecanoyl-CoA = 1-hexadecanoyl-2-dodecanoyl-sn-glycero-3-phospho-
CC (1'-sn-glycerol) + CoA; Xref=Rhea:RHEA:40107, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57375, ChEBI:CHEBI:75158, ChEBI:CHEBI:77001;
CC Evidence={ECO:0000250|UniProtKB:Q92604};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40108;
CC Evidence={ECO:0000250|UniProtKB:Q92604};
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:Q92604};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35852;
CC Evidence={ECO:0000250|UniProtKB:Q92604};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-sn-glycero-3-phospho-(1'-sn-glycerol) +
CC octadecanoyl-CoA = 1-hexadecanoyl-2-octadecanoyl-sn-glycero-3-
CC phospho-(1'-sn-glycerol) + CoA; Xref=Rhea:RHEA:35887,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57394, ChEBI:CHEBI:72839,
CC ChEBI:CHEBI:75158; Evidence={ECO:0000250|UniProtKB:Q92604};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35888;
CC Evidence={ECO:0000250|UniProtKB:Q92604};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-octadecanoyl-sn-glycero-3-phospho-(1'-sn-glycerol) +
CC hexadecanoyl-CoA = 1-octadecanoyl-2-hexadecanoyl-sn-glycero-3-
CC phospho-(1'-sn-glycerol) + CoA; Xref=Rhea:RHEA:35859,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57379, ChEBI:CHEBI:72827,
CC ChEBI:CHEBI:72831; Evidence={ECO:0000250|UniProtKB:Q92604};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35860;
CC Evidence={ECO:0000250|UniProtKB:Q92604};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phospho-(1'-sn-glycerol) +
CC dodecanoyl-CoA = 1-(9Z-octadecenoyl)-2-dodecanoyl-sn-glycero-3-
CC phospho-(1'-sn-glycerol) + CoA; Xref=Rhea:RHEA:40099,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57375, ChEBI:CHEBI:72828,
CC ChEBI:CHEBI:77000; Evidence={ECO:0000250|UniProtKB:Q92604};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40100;
CC Evidence={ECO:0000250|UniProtKB:Q92604};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 1-hexadecanoyl-sn-glycero-3-phospho-
CC (1'-sn-glycerol) = 1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-
CC phospho-(1'-sn-glycerol) + CoA; Xref=Rhea:RHEA:35891,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57387, ChEBI:CHEBI:72841,
CC ChEBI:CHEBI:75158; Evidence={ECO:0000250|UniProtKB:Q92604};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35892;
CC Evidence={ECO:0000250|UniProtKB:Q92604};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phospho-(1'-sn-glycerol) +
CC hexadecanoyl-CoA = 1-(9Z-octadecenoyl)-2-hexadecanoyl-sn-glycero-3-
CC phospho-(1'-sn-glycerol) + CoA; Xref=Rhea:RHEA:35863,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57379, ChEBI:CHEBI:72828,
CC ChEBI:CHEBI:72832; Evidence={ECO:0000250|UniProtKB:Q92604};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35864;
CC Evidence={ECO:0000250|UniProtKB:Q92604};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 1-(9Z-octadecenoyl)-sn-glycero-3-
CC phospho-(1'-sn-glycerol) = 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-
CC phospho-(1'-sn-glycerol) + CoA; Xref=Rhea:RHEA:37651,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57387, ChEBI:CHEBI:72828,
CC ChEBI:CHEBI:75163; Evidence={ECO:0000250|UniProtKB:Q92604};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37652;
CC Evidence={ECO:0000250|UniProtKB:Q92604};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2-acylglycerol + an acyl-CoA = a 1,2-diacyl-sn-glycerol +
CC CoA; Xref=Rhea:RHEA:32947, ChEBI:CHEBI:17389, ChEBI:CHEBI:17815,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:58342; EC=2.3.1.22;
CC Evidence={ECO:0000269|PubMed:20018982};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32948;
CC Evidence={ECO:0000305|PubMed:20018982};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2-acylglycerol + hexadecanoyl-CoA = a 1-hexadecanoyl-2-
CC acylglycerol + CoA; Xref=Rhea:RHEA:65096, ChEBI:CHEBI:17389,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57379, ChEBI:CHEBI:156324;
CC Evidence={ECO:0000269|PubMed:20018982};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65097;
CC Evidence={ECO:0000305|PubMed:20018982};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-acylglycerol + hexadecanoyl-CoA = an hexadecanoyl-
CC acylglycerol + CoA; Xref=Rhea:RHEA:65100, ChEBI:CHEBI:35759,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57379, ChEBI:CHEBI:156325;
CC Evidence={ECO:0000269|PubMed:20018982};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65101;
CC Evidence={ECO:0000305|PubMed:20018982};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q92604}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q92604}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. Expressed in heart, kidney, liver,
CC skin, intestine, and thymus. Highest expression is detected in brain
CC and testis. {ECO:0000269|PubMed:20018982, ECO:0000269|PubMed:35131264}.
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-phosphate. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Mice are born at the expected Mendelian
CC frequency. They show reduced body fat and increased mortality during
CC early adulthood with an average life span of about 5 months. Mutant
CC mice produce poorly nutritional milk and are unable to nourish their
CC litters leading in high pre-weaning mortality.
CC {ECO:0000269|PubMed:35131264}.
CC -!- SIMILARITY: Belongs to the 1-acyl-sn-glycerol-3-phosphate
CC acyltransferase family. {ECO:0000305}.
CC -!- CAUTION: The role in phosphatidylglycerols remodeling and cardiolipin
CC synthesis is questioned as both processes occur in mitochondria. The
CC monoacylglycerol acyltransferase activity is also weak and a direct
CC role in triacylglycerol synthesis appears unlikely.
CC {ECO:0000269|PubMed:35131264}.
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DR EMBL; BC013667; AAH13667.1; -; mRNA.
DR CCDS; CCDS15622.1; -.
DR RefSeq; NP_758470.1; NM_172266.3.
DR RefSeq; XP_006497218.1; XM_006497155.3.
DR RefSeq; XP_006497219.1; XM_006497156.3.
DR AlphaFoldDB; Q91YX5; -.
DR BioGRID; 230563; 3.
DR STRING; 10090.ENSMUSP00000106480; -.
DR iPTMnet; Q91YX5; -.
DR PhosphoSitePlus; Q91YX5; -.
DR SwissPalm; Q91YX5; -.
DR EPD; Q91YX5; -.
DR jPOST; Q91YX5; -.
DR MaxQB; Q91YX5; -.
DR PaxDb; Q91YX5; -.
DR PRIDE; Q91YX5; -.
DR ProteomicsDB; 265065; -.
DR Antibodypedia; 1888; 97 antibodies from 22 providers.
DR DNASU; 226856; -.
DR Ensembl; ENSMUST00000110855; ENSMUSP00000106479; ENSMUSG00000026623.
DR GeneID; 226856; -.
DR KEGG; mmu:226856; -.
DR UCSC; uc007ecs.3; mouse.
DR CTD; 9926; -.
DR MGI; MGI:2446186; Lpgat1.
DR VEuPathDB; HostDB:ENSMUSG00000026623; -.
DR eggNOG; KOG1505; Eukaryota.
DR GeneTree; ENSGT00950000182836; -.
DR HOGENOM; CLU_046804_2_0_1; -.
DR InParanoid; Q91YX5; -.
DR PhylomeDB; Q91YX5; -.
DR Reactome; R-MMU-1482925; Acyl chain remodelling of PG.
DR BioGRID-ORCS; 226856; 4 hits in 74 CRISPR screens.
DR ChiTaRS; Lpgat1; mouse.
DR PRO; PR:Q91YX5; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q91YX5; protein.
DR Bgee; ENSMUSG00000026623; Expressed in rostral migratory stream and 255 other tissues.
DR ExpressionAtlas; Q91YX5; baseline and differential.
DR Genevisible; Q91YX5; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0012505; C:endomembrane system; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
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:0003846; F:2-acylglycerol O-acyltransferase activity; IDA:UniProtKB.
DR GO; GO:0016746; F:acyltransferase activity; IBA:GO_Central.
DR GO; GO:0071618; F:lysophosphatidylethanolamine acyltransferase activity; IDA:UniProtKB.
DR GO; GO:0071617; F:lysophospholipid acyltransferase activity; ISS:UniProtKB.
DR GO; GO:0036152; P:phosphatidylethanolamine acyl-chain remodeling; IDA:UniProtKB.
DR GO; GO:0036149; P:phosphatidylinositol acyl-chain remodeling; IBA:GO_Central.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0045723; P:positive regulation of fatty acid biosynthetic process; ISO:MGI.
DR GO; GO:0019432; P:triglyceride biosynthetic process; IMP:UniProtKB.
DR InterPro; IPR032098; Acyltransf_C.
DR InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR Pfam; PF16076; Acyltransf_C; 1.
DR Pfam; PF01553; Acyltransferase; 1.
DR SMART; SM00563; PlsC; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Endoplasmic reticulum; Lipid biosynthesis;
KW Lipid metabolism; Membrane; Phospholipid biosynthesis;
KW Phospholipid metabolism; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..370
FT /note="Acyl-CoA:lysophosphatidylglycerol acyltransferase 1"
FT /id="PRO_0000208205"
FT TRANSMEM 22..42
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 342..362
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOTIF 101..106
FT /note="HXXXXD motif"
SQ SEQUENCE 370 AA; 43088 MW; EE746F9AAD3073EE CRC64;
MAVTVEEAPW LGWIVAKALM RFAFMVANNL VAIPSYICYV IILQPLRVLD SKRFWYIEGL
MYKWLLGMVA SWGWYAGYTV MEWGEDIKAI AKDEAVMLVN HQATGDVCTL MMCLQDKGPV
VAQMMWLMDH IFKYTNFGIV SLIHGDFFIR QGRAYRDQQL LVLKKHLEHN YRSRDRKWIV
LFPEGGFLRK RRETSQAFAK KNNLPFLTHV TLPRFGATNI ILKALVARQE NGSPAGGDAR
GLECKSRGLQ WIIDTTIAYP KAEPIDIQTW ILGYRKPTVT HVHYRIFPIG DVPLETEDLT
SWLYQRFIEK EDLLSHFYKT GAFPPPQGQK EAVCREMTLS NMWIFLIQSF AFLSGYLWYH
IIQYFYHCLF
