PLCB_MOUSE
ID PLCB_MOUSE Reviewed; 278 AA.
AC Q8K3K7;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=1-acyl-sn-glycerol-3-phosphate acyltransferase beta;
DE EC=2.3.1.51 {ECO:0000269|PubMed:15367102};
DE AltName: Full=1-acylglycerol-3-phosphate O-acyltransferase 2;
DE Short=1-AGP acyltransferase 2;
DE Short=1-AGPAT 2;
DE AltName: Full=Lysophosphatidic acid acyltransferase beta {ECO:0000250|UniProtKB:O15120};
DE Short=LPAAT-beta;
DE Flags: Precursor;
GN Name=Agpat2;
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 STRAIN=BALB/cJ; TISSUE=Liver;
RX PubMed=11967537; DOI=10.1038/ng880;
RA Agarwal A.K., Arioglu E., de Almeida S., Akkoc N., Taylor S.I.,
RA Bowcock A.M., Barnes R.I., Garg A.;
RT "AGPAT2 is mutated in congenital generalized lipodystrophy linked to
RT chromosome 9q34.";
RL Nat. Genet. 31:21-23(2002).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, AND INDUCTION.
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, and Spleen;
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:0000269|PubMed:15367102}.
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:0000269|PubMed:15367102};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19710;
CC Evidence={ECO:0000305|PubMed:15367102};
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:O15120};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37132;
CC Evidence={ECO:0000250|UniProtKB:O15120};
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:O15120};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37144;
CC Evidence={ECO:0000250|UniProtKB:O15120};
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:O15120};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37156;
CC Evidence={ECO:0000250|UniProtKB:O15120};
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:O15120};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37160;
CC Evidence={ECO:0000250|UniProtKB:O15120};
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:O15120};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37172;
CC Evidence={ECO:0000250|UniProtKB:O15120};
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:O15120};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37176;
CC Evidence={ECO:0000250|UniProtKB:O15120};
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:O15120};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33188;
CC Evidence={ECO:0000250|UniProtKB:O15120};
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:O15120};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37188;
CC Evidence={ECO:0000250|UniProtKB:O15120};
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:O15120};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37140;
CC Evidence={ECO:0000250|UniProtKB:O15120};
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:O15120};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37180;
CC Evidence={ECO:0000250|UniProtKB:O15120};
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:O15120};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37184;
CC Evidence={ECO:0000250|UniProtKB:O15120};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-sn-glycero-3-phosphate + octadecanoyl-CoA = 1-
CC hexadecanoyl-2-octadecanoyl-sn-glycero-3-phosphate + CoA;
CC Xref=Rhea:RHEA:35907, ChEBI:CHEBI:57287, ChEBI:CHEBI:57394,
CC ChEBI:CHEBI:57518, ChEBI:CHEBI:72857;
CC Evidence={ECO:0000250|UniProtKB:O15120};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35908;
CC Evidence={ECO:0000250|UniProtKB:O15120};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + 1-hexadecanoyl-sn-
CC glycero-3-phosphate = 1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-
CC eicosatetraenoyl)-sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:35915,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57368, ChEBI:CHEBI:57518,
CC ChEBI:CHEBI:72864; Evidence={ECO:0000250|UniProtKB:O15120};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35916;
CC Evidence={ECO:0000250|UniProtKB:O15120};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-sn-glycero-3-phosphate + hexadecanoyl-CoA =
CC 1,2-dihexadecanoyl-sn-glycero-3-phosphate + CoA;
CC Xref=Rhea:RHEA:35903, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379,
CC ChEBI:CHEBI:57518, ChEBI:CHEBI:72859;
CC Evidence={ECO:0000250|UniProtKB:O15120};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35904;
CC Evidence={ECO:0000250|UniProtKB:O15120};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-sn-glycero-3-phosphate + tetradecanoyl-CoA = 1-
CC hexadecanoyl-2-tetradecanoyl-sn-glycero-3-phosphate + CoA;
CC Xref=Rhea:RHEA:35899, ChEBI:CHEBI:57287, ChEBI:CHEBI:57385,
CC ChEBI:CHEBI:57518, ChEBI:CHEBI:72858;
CC Evidence={ECO:0000250|UniProtKB:O15120};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35900;
CC Evidence={ECO:0000250|UniProtKB:O15120};
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:O15120};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37604;
CC Evidence={ECO:0000250|UniProtKB:O15120};
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:O15120}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed at high levels in the liver, at
CC intermediate levels in the kidney, gut, heart and skeletal muscles.
CC Undetectable in brain and spleen. {ECO:0000269|PubMed:15367102}.
CC -!- INDUCTION: Down-regulated in the heart by clofibrate, a PPAR-alpha
CC agonist. {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; AY072769; AAL62337.1; -; mRNA.
DR CCDS; CCDS15809.1; -.
DR RefSeq; NP_080488.1; NM_026212.2.
DR AlphaFoldDB; Q8K3K7; -.
DR SMR; Q8K3K7; -.
DR IntAct; Q8K3K7; 1.
DR MINT; Q8K3K7; -.
DR STRING; 10090.ENSMUSP00000028286; -.
DR iPTMnet; Q8K3K7; -.
DR PhosphoSitePlus; Q8K3K7; -.
DR SwissPalm; Q8K3K7; -.
DR jPOST; Q8K3K7; -.
DR MaxQB; Q8K3K7; -.
DR PaxDb; Q8K3K7; -.
DR PRIDE; Q8K3K7; -.
DR ProteomicsDB; 289921; -.
DR Antibodypedia; 18762; 175 antibodies from 27 providers.
DR Ensembl; ENSMUST00000028286; ENSMUSP00000028286; ENSMUSG00000026922.
DR GeneID; 67512; -.
DR KEGG; mmu:67512; -.
DR UCSC; uc008ivt.2; mouse.
DR CTD; 10555; -.
DR MGI; MGI:1914762; Agpat2.
DR VEuPathDB; HostDB:ENSMUSG00000026922; -.
DR eggNOG; KOG2848; Eukaryota.
DR GeneTree; ENSGT00390000008726; -.
DR HOGENOM; CLU_027938_10_1_1; -.
DR InParanoid; Q8K3K7; -.
DR OMA; WVMRYTT; -.
DR OrthoDB; 1623097at2759; -.
DR PhylomeDB; Q8K3K7; -.
DR TreeFam; TF314867; -.
DR BRENDA; 2.3.1.51; 3474.
DR Reactome; R-MMU-1483166; Synthesis of PA.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR UniPathway; UPA00557; UER00613.
DR BioGRID-ORCS; 67512; 3 hits in 73 CRISPR screens.
DR PRO; PR:Q8K3K7; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q8K3K7; protein.
DR Bgee; ENSMUSG00000026922; Expressed in brown adipose tissue and 187 other tissues.
DR ExpressionAtlas; Q8K3K7; baseline and differential.
DR Genevisible; Q8K3K7; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA: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:UniProtKB.
DR GO; GO:0016024; P:CDP-diacylglycerol biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0008544; P:epidermis development; IEA:Ensembl.
DR GO; GO:0006654; P:phosphatidic acid biosynthetic process; ISO:MGI.
DR GO; GO:0008654; P:phospholipid biosynthetic process; NAS:UniProtKB.
DR GO; GO:0001819; P:positive regulation of cytokine production; ISO:MGI.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl.
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..23
FT /evidence="ECO:0000255"
FT CHAIN 24..278
FT /note="1-acyl-sn-glycerol-3-phosphate acyltransferase beta"
FT /id="PRO_0000208193"
FT TOPO_DOM 24..29
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 30..50
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 51..121
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 122..142
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 143..278
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT MOTIF 98..103
FT /note="HXXXXD motif"
FT /evidence="ECO:0000250|UniProtKB:Q9D517"
FT MOTIF 172..175
FT /note="EGTR motif"
FT /evidence="ECO:0000250|UniProtKB:O15120"
SQ SEQUENCE 278 AA; 31011 MW; 57A54BFB1A0EFF56 CRC64;
MDPWPWLTAA LLLLLLLVQL SRTARFYAKV GLYCVLCLSF SAAASIVCLL RHGGRTVDNM
SIISWFVRSF KYVYGLRFEV SGQKKLEVDG PCVIISNHQS ILDMMGLMEI LPKRCVQIAK
RELMFTGPVG LIMYLGGVYF INRQQARTAM SVMADLGDLM VKENLKVWIY PEGTRNDNGD
LLPFKKGAFY LAIQAQVPII PVVYSSFSSF YNVKTKLFTS GTIKVQVLDA VPTNGLTDAD
VTKLVDTCYQ SMRATFLQIS QIPQENSAIK EPGVLPAQ
