PLCA_MOUSE
ID PLCA_MOUSE Reviewed; 285 AA.
AC O35083; O35446;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 25-MAY-2022, entry version 146.
DE RecName: Full=1-acyl-sn-glycerol-3-phosphate acyltransferase alpha;
DE EC=2.3.1.51 {ECO:0000250|UniProtKB:Q99943};
DE AltName: Full=1-acylglycerol-3-phosphate O-acyltransferase 1;
DE Short=1-AGP acyltransferase 1;
DE Short=1-AGPAT 1;
DE AltName: Full=Lysophosphatidic acid acyltransferase alpha {ECO:0000250|UniProtKB:Q99943};
DE Short=LPAAT-alpha;
DE Flags: Precursor;
GN Name=Agpat1;
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].
RC TISSUE=Embryo;
RX PubMed=9299423; DOI=10.1006/bbrc.1997.7214;
RA Kume K., Shimizu T.;
RT "cDNA cloning and expression of murine 1-acyl-sn-glycerol-3-phosphate
RT acyltransferase.";
RL Biochem. Biophys. Res. Commun. 237:663-666(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=129;
RX PubMed=14656967; DOI=10.1101/gr.1736803;
RA Xie T., Rowen L., Aguado B., Ahearn M.E., Madan A., Qin S., Campbell R.D.,
RA Hood L.;
RT "Analysis of the gene-dense major histocompatibility complex class III
RT region and its comparison to mouse.";
RL Genome Res. 13:2621-2636(2003).
RN [3]
RP TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J;
RX PubMed=15367102; DOI=10.1042/bj20041348;
RA Lu B., Jiang Y.J., Zhou Y., Xu F.Y., Hatch G.M., Choy P.C.;
RT "Cloning and characterization of murine 1-acyl-sn-glycerol 3-phosphate
RT acyltransferases and their regulation by PPARalpha in murine heart.";
RL Biochem. J. 385:469-477(2005).
RN [4]
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).
CC -!- FUNCTION: Converts 1-acyl-sn-glycerol-3-phosphate (lysophosphatidic
CC acid or LPA) into 1,2-diacyl-sn-glycerol-3-phosphate (phosphatidic acid
CC or PA) by incorporating an acyl moiety at the sn-2 position of the
CC glycerol backbone. {ECO:0000250|UniProtKB:Q99943}.
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:Q99943};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19710;
CC Evidence={ECO:0000250|UniProtKB:Q99943};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 1-(9Z-octadecenoyl)-sn-glycero-3-
CC phosphate = 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphate + CoA;
CC Xref=Rhea:RHEA:37131, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387,
CC ChEBI:CHEBI:74544, ChEBI:CHEBI:74546;
CC Evidence={ECO:0000250|UniProtKB:Q99943};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37132;
CC Evidence={ECO:0000250|UniProtKB:Q99943};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphate + hexadecanoyl-CoA
CC = 1-(9Z)-octadecenoyl-2-hexadecanoyl-sn-glycero-3-phosphate + CoA;
CC Xref=Rhea:RHEA:37143, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379,
CC ChEBI:CHEBI:74544, ChEBI:CHEBI:74551;
CC Evidence={ECO:0000250|UniProtKB:Q99943};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37144;
CC Evidence={ECO:0000250|UniProtKB:Q99943};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphate + heptadecanoyl-CoA
CC = 1-(9Z)-octadecenoyl-2-heptadecanoyl-sn-glycero-3-phosphate + CoA;
CC Xref=Rhea:RHEA:37155, ChEBI:CHEBI:57287, ChEBI:CHEBI:74307,
CC ChEBI:CHEBI:74544, ChEBI:CHEBI:74558;
CC Evidence={ECO:0000250|UniProtKB:Q99943};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37156;
CC Evidence={ECO:0000250|UniProtKB:Q99943};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphate + octadecanoyl-CoA
CC = 1-(9Z-octadecenoyl)-2-octadecanoyl-sn-glycero-3-phosphate + CoA;
CC Xref=Rhea:RHEA:37147, ChEBI:CHEBI:57287, ChEBI:CHEBI:57394,
CC ChEBI:CHEBI:74544, ChEBI:CHEBI:74552;
CC Evidence={ECO:0000250|UniProtKB:Q99943};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37148;
CC Evidence={ECO:0000250|UniProtKB:Q99943};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z)-octadecadienoyl-CoA + 1-(9Z-octadecenoyl)-sn-glycero-
CC 3-phosphate = 1-(9Z)-octadecenoyl-2-(9Z,12Z)-octadecadienoyl-sn-
CC glycero-3-phosphate + CoA; Xref=Rhea:RHEA:37159, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57383, ChEBI:CHEBI:74544, ChEBI:CHEBI:74563;
CC Evidence={ECO:0000250|UniProtKB:Q99943};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37160;
CC Evidence={ECO:0000250|UniProtKB:Q99943};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphate + tetradecanoyl-CoA
CC = 1-(9Z)-octadecenoyl-2-tetradecanoyl-sn-glycero-3-phosphate + CoA;
CC Xref=Rhea:RHEA:37171, ChEBI:CHEBI:57287, ChEBI:CHEBI:57385,
CC ChEBI:CHEBI:74544, ChEBI:CHEBI:74579;
CC Evidence={ECO:0000250|UniProtKB:Q99943};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37172;
CC Evidence={ECO:0000250|UniProtKB:Q99943};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphate + pentadecanoyl-CoA
CC = 1-(9Z)-octadecenoyl-2-pentadecanoyl-sn-glycero-3-phosphate + CoA;
CC Xref=Rhea:RHEA:37175, ChEBI:CHEBI:57287, ChEBI:CHEBI:74309,
CC ChEBI:CHEBI:74544, ChEBI:CHEBI:74578;
CC Evidence={ECO:0000250|UniProtKB:Q99943};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37176;
CC Evidence={ECO:0000250|UniProtKB:Q99943};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 1-hexadecanoyl-sn-glycero-3-phosphate
CC = 1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphate + CoA;
CC Xref=Rhea:RHEA:33187, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387,
CC ChEBI:CHEBI:57518, ChEBI:CHEBI:64839;
CC Evidence={ECO:0000250|UniProtKB:Q99943};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33188;
CC Evidence={ECO:0000250|UniProtKB:Q99943};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 1-(9Z,12Z,15Z)-octadecatrienoyl-sn-
CC glycero-3-phosphate = 1-(9Z,12Z,15Z)-octadecatrienoyl-2-(9Z)-
CC octadecenoyl-sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:37139,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57387, ChEBI:CHEBI:74549,
CC ChEBI:CHEBI:74550; Evidence={ECO:0000250|UniProtKB:Q99943};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37140;
CC Evidence={ECO:0000250|UniProtKB:Q99943};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 1-(6Z,9Z,12Z-octadecatrienoyl)-sn-
CC glycero-3-phosphate = (6Z,9Z,12Z)-octadecatrienoyl-2-(9Z)-
CC octadecenoyl-sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:37179,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57387, ChEBI:CHEBI:74581,
CC ChEBI:CHEBI:74582; Evidence={ECO:0000250|UniProtKB:Q99943};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37180;
CC Evidence={ECO:0000250|UniProtKB:Q99943};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 1-eicosanoyl-sn-glycero-3-phosphate =
CC 1-eicosanoyl-2-(9Z)-octadecenoyl-sn-glycero-3-phosphate + CoA;
CC Xref=Rhea:RHEA:37183, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387,
CC ChEBI:CHEBI:74583, ChEBI:CHEBI:74584;
CC Evidence={ECO:0000250|UniProtKB:Q99943};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37184;
CC Evidence={ECO:0000250|UniProtKB:Q99943};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 1-tetradecanoyl-sn-glycerol 3-
CC phosphate = 1-tetradecanoyl-2-(9Z)-octadecenoyl-sn-glycero-3-
CC phosphate + CoA; Xref=Rhea:RHEA:37187, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57387, ChEBI:CHEBI:72683, ChEBI:CHEBI:74586;
CC Evidence={ECO:0000250|UniProtKB:Q99943};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37188;
CC Evidence={ECO:0000250|UniProtKB:Q99943};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + 1-(9Z-octadecenoyl)-sn-
CC glycero-3-phosphate = 1-(9Z)-octadecenoyl-2-(5Z,8Z,11Z,14Z)-
CC eicosatetraenoyl-sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:37443,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57368, ChEBI:CHEBI:74544,
CC ChEBI:CHEBI:74928; Evidence={ECO:0000250|UniProtKB:Q99943};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37444;
CC Evidence={ECO:0000250|UniProtKB:Q99943};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphate + dodecanoyl-CoA =
CC 1-(9Z)-octadecenoyl-2-dodecanoyl-sn-glycero-3-phosphate + CoA;
CC Xref=Rhea:RHEA:37591, ChEBI:CHEBI:57287, ChEBI:CHEBI:57375,
CC ChEBI:CHEBI:74544, ChEBI:CHEBI:75076;
CC Evidence={ECO:0000250|UniProtKB:Q99943};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37592;
CC Evidence={ECO:0000250|UniProtKB:Q99943};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6Z)-octadecenoyl-CoA + 1-(9Z-octadecenoyl)-sn-glycero-3-
CC phosphate = 1-(9Z)-octadecenoyl-2-(6Z)-octadecenoyl-sn-glycero-3-
CC phosphate + CoA; Xref=Rhea:RHEA:37607, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:74544, ChEBI:CHEBI:75123, ChEBI:CHEBI:75124;
CC Evidence={ECO:0000250|UniProtKB:Q99943};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37608;
CC Evidence={ECO:0000250|UniProtKB:Q99943};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(11Z)-octadecenoyl-CoA + 1-(9Z-octadecenoyl)-sn-glycero-3-
CC phosphate = 1-(9Z)-octadecenoyl-2-(11Z)-octadecenoyl-sn-glycero-3-
CC phosphate + CoA; Xref=Rhea:RHEA:37603, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:74544, ChEBI:CHEBI:75121, ChEBI:CHEBI:75122;
CC Evidence={ECO:0000250|UniProtKB:Q99943};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37604;
CC Evidence={ECO:0000250|UniProtKB:Q99943};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-hexadecenoyl-CoA + 1-(9Z-octadecenoyl)-sn-glycero-3-
CC phosphate = 1-(9Z-octadecenoyl)-2-(9Z-hexadecenoyl)-sn-glycero-3-
CC phosphate + CoA; Xref=Rhea:RHEA:40195, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:61540, ChEBI:CHEBI:74544, ChEBI:CHEBI:74697;
CC Evidence={ECO:0000250|UniProtKB:Q99943};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40196;
CC Evidence={ECO:0000250|UniProtKB:Q99943};
CC -!- PATHWAY: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-
CC diacylglycerol from sn-glycerol 3-phosphate: step 2/3.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q99943}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:15367102}.
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|UniProtKB:Q9D517}.
CC -!- SIMILARITY: Belongs to the 1-acyl-sn-glycerol-3-phosphate
CC acyltransferase family. {ECO:0000305}.
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DR EMBL; AB005623; BAA22599.1; -; mRNA.
DR EMBL; AF030001; AAB82009.1; -; Genomic_DNA.
DR CCDS; CCDS37590.1; -.
DR PIR; JC5639; JC5639.
DR RefSeq; NP_001156851.1; NM_001163379.1.
DR RefSeq; NP_061350.3; NM_018862.3.
DR RefSeq; XP_006524710.1; XM_006524647.2.
DR RefSeq; XP_006524711.1; XM_006524648.1.
DR AlphaFoldDB; O35083; -.
DR SMR; O35083; -.
DR BioGRID; 207751; 5.
DR IntAct; O35083; 1.
DR MINT; O35083; -.
DR STRING; 10090.ENSMUSP00000048573; -.
DR ChEMBL; CHEMBL2844; -.
DR PhosphoSitePlus; O35083; -.
DR SwissPalm; O35083; -.
DR EPD; O35083; -.
DR jPOST; O35083; -.
DR MaxQB; O35083; -.
DR PaxDb; O35083; -.
DR PeptideAtlas; O35083; -.
DR PRIDE; O35083; -.
DR ProteomicsDB; 289917; -.
DR DNASU; 55979; -.
DR GeneID; 55979; -.
DR KEGG; mmu:55979; -.
DR UCSC; uc008ccz.2; mouse.
DR CTD; 10554; -.
DR MGI; MGI:1932075; Agpat1.
DR eggNOG; KOG2848; Eukaryota.
DR InParanoid; O35083; -.
DR OrthoDB; 1623097at2759; -.
DR PhylomeDB; O35083; -.
DR TreeFam; TF314867; -.
DR BRENDA; 2.3.1.51; 3474.
DR Reactome; R-MMU-1483166; Synthesis of PA.
DR Reactome; R-MMU-163765; ChREBP activates metabolic gene expression.
DR UniPathway; UPA00557; UER00613.
DR BioGRID-ORCS; 55979; 2 hits in 76 CRISPR screens.
DR ChiTaRS; Agpat1; mouse.
DR PRO; PR:O35083; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; O35083; protein.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
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:0003841; F:1-acylglycerol-3-phosphate O-acyltransferase activity; IDA:MGI.
DR GO; GO:0016024; P:CDP-diacylglycerol biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006654; P:phosphatidic acid biosynthetic process; IDA:MGI.
DR GO; GO:0001819; P:positive regulation of cytokine production; ISO:MGI.
DR InterPro; IPR004552; AGP_acyltrans.
DR InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR Pfam; PF01553; Acyltransferase; 1.
DR SMART; SM00563; PlsC; 1.
DR TIGRFAMs; TIGR00530; AGP_acyltrn; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Endoplasmic reticulum; Lipid biosynthesis;
KW Lipid metabolism; Membrane; Phospholipid biosynthesis;
KW Phospholipid metabolism; Reference proteome; Signal; Transferase;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT CHAIN 29..285
FT /note="1-acyl-sn-glycerol-3-phosphate acyltransferase
FT alpha"
FT /id="PRO_0000208191"
FT TOPO_DOM 29..34
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q99943"
FT TRANSMEM 35..55
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 56..124
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q99943"
FT TRANSMEM 125..145
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 146..189
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q99943"
FT MOTIF 101..106
FT /note="HXXXXD motif"
FT /evidence="ECO:0000250|UniProtKB:Q9D517"
FT MOTIF 175..178
FT /note="EGTR motif"
FT /evidence="ECO:0000250|UniProtKB:Q99943"
FT CONFLICT 73
FT /note="A -> V (in Ref. 2; AAB82009)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 285 AA; 31709 MW; 6227A2C3A09009C1 CRC64;
MELWPGAWTA LLLLLLLLLS TLWFCSSSAK YFFKMAFYNG WILFLAILAI PVCAVRGRNV
ENMKILRLLL LHAKYLYGIR VEVRGAHHFP PTQPYVVVSN HQSSLDLLGM MEVLPDRCVP
IAKRELLWAG SAGLACWLAG IIFIDRKRTG DAISVMSEVA QTLLTQDVRV WVFPEGTRNH
NGSMLPFKRG AFHLAVQAQV PIIPIVMSSY QDFYSKKERR FTSPGRCQVR VLPPVSTEGL
TPDDVPALAD SVRHSMLTIF REISTDGLGG GDCLKKPGGA GEARL
