PLCD_RAT
ID PLCD_RAT Reviewed; 378 AA.
AC Q924S1;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=1-acyl-sn-glycerol-3-phosphate acyltransferase delta;
DE EC=2.3.1.51 {ECO:0000250|UniProtKB:Q8K4X7};
DE AltName: Full=1-acylglycerol-3-phosphate O-acyltransferase 4;
DE Short=1-AGP acyltransferase 4;
DE Short=1-AGPAT 4;
DE AltName: Full=Lysophosphatidic acid acyltransferase delta;
DE Short=LPAAT-delta;
GN Name=Agpat4;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Li W., Suzuki T.;
RT "Rattus norvegicus mRNA for lysophosphatidic acid acyltransferase-delta,
RT complete cds.";
RL Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
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).
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 (By similarity). Exhibits high acyl-CoA specificity
CC for polyunsaturated fatty acyl-CoA, especially docosahexaenoyl-CoA
CC (22:6-CoA, DHA-CoA) (By similarity). {ECO:0000250|UniProtKB:Q8K4X7}.
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:Q8K4X7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19710;
CC Evidence={ECO:0000250|UniProtKB:Q8K4X7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoyl-CoA + 1-hexadecanoyl-
CC sn-glycero-3-phosphate = 1-hexadecanoyl-2-(4Z,7Z,10Z,13Z,16Z,19Z-
CC docosahexaenoyl)-sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:55300,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57518, ChEBI:CHEBI:74298,
CC ChEBI:CHEBI:82928; Evidence={ECO:0000250|UniProtKB:Q8K4X7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55301;
CC Evidence={ECO:0000250|UniProtKB:Q8K4X7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z)-octadecadienoyl-CoA + 1-octadecanoyl-sn-glycero-3-
CC phosphate = 1-octadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-
CC phosphate + CoA; Xref=Rhea:RHEA:55304, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57383, ChEBI:CHEBI:74565, ChEBI:CHEBI:77098;
CC Evidence={ECO:0000250|UniProtKB:Q8K4X7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55305;
CC Evidence={ECO:0000250|UniProtKB:Q8K4X7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoyl-CoA + 1-octadecanoyl-
CC sn-glycero-3-phosphate = 1-octadecanoyl-2-(4Z,7Z,10Z,13Z,16Z,19Z-
CC docosahexaenoyl)-sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:55308,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:74298, ChEBI:CHEBI:74565,
CC ChEBI:CHEBI:77130; Evidence={ECO:0000250|UniProtKB:Q8K4X7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55309;
CC Evidence={ECO:0000250|UniProtKB:Q8K4X7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoyl-CoA + 1-(9Z-
CC octadecenoyl)-sn-glycero-3-phosphate = 1-(9Z-octadecenoyl)-2-
CC (4Z,7Z,10Z,13Z,16Z,19Z-docosahexaenoyl)-sn-glycero-3-phosphate + CoA;
CC Xref=Rhea:RHEA:55312, ChEBI:CHEBI:57287, ChEBI:CHEBI:74298,
CC ChEBI:CHEBI:74544, ChEBI:CHEBI:138723;
CC Evidence={ECO:0000250|UniProtKB:Q8K4X7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55313;
CC Evidence={ECO:0000250|UniProtKB:Q8K4X7};
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:Q8K4X7}; Multi-pass membrane protein
CC {ECO:0000255}.
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; AB067572; BAB62290.1; -; mRNA.
DR EMBL; BC086992; AAH86992.1; -; mRNA.
DR RefSeq; NP_596897.1; NM_133406.1.
DR RefSeq; XP_006227919.1; XM_006227857.3.
DR AlphaFoldDB; Q924S1; -.
DR STRING; 10116.ENSRNOP00000024213; -.
DR PaxDb; Q924S1; -.
DR PRIDE; Q924S1; -.
DR Ensembl; ENSRNOT00000024213; ENSRNOP00000024213; ENSRNOG00000017731.
DR GeneID; 170919; -.
DR KEGG; rno:170919; -.
DR CTD; 56895; -.
DR RGD; 619916; Agpat4.
DR eggNOG; KOG1505; Eukaryota.
DR GeneTree; ENSGT00950000182836; -.
DR InParanoid; Q924S1; -.
DR PhylomeDB; Q924S1; -.
DR TreeFam; TF314065; -.
DR Reactome; R-RNO-1483166; Synthesis of PA.
DR UniPathway; UPA00557; UER00613.
DR PRO; PR:Q924S1; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000017731; Expressed in cerebellum and 20 other tissues.
DR ExpressionAtlas; Q924S1; baseline and differential.
DR Genevisible; Q924S1; RN.
DR GO; GO:0012505; C:endomembrane system; IBA:GO_Central.
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:0005741; C:mitochondrial outer membrane; ISO:RGD.
DR GO; GO:0003841; F:1-acylglycerol-3-phosphate O-acyltransferase activity; ISS:UniProtKB.
DR GO; GO:0016746; F:acyltransferase activity; IBA:GO_Central.
DR GO; GO:0042171; F:lysophosphatidic acid acyltransferase activity; ISO:RGD.
DR GO; GO:0016024; P:CDP-diacylglycerol biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006644; P:phospholipid metabolic process; ISO:RGD.
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 2: Evidence at transcript 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..378
FT /note="1-acyl-sn-glycerol-3-phosphate acyltransferase
FT delta"
FT /id="PRO_0000208199"
FT TRANSMEM 11..31
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 125..145
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 311..331
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 338..358
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOTIF 96..101
FT /note="HXXXXD motif"
FT /evidence="ECO:0000250|UniProtKB:Q9D517"
SQ SEQUENCE 378 AA; 43794 MW; 389AA01B7327AE2B CRC64;
MDLIGLLKSQ FLCHLVFCYV FIASGLIVNA IQLCTLVIWP INKQLFRKIN ARLCYCVSSQ
LVMLLEWWSG TECTIYTDPK ASPHYGKENA IVVLNHKFEI DFLCGWSLAE RLGILGNSKV
LAKKELAYVP IIGWMWYFVE MIFCTRKWEQ DRQTVAKSLL HLRDYPEKYL FLIHCEGTRF
TEKKHQISMQ VAQAKGLPSL KHHLLPRTKG FAITVKCLRD VVPAVYDCTL NFRNNENPTL
LGVLNGKKYH ADCYVRRIPM EDIPEDEDKC SAWLHKLYQE KDAFQEEYYR TGVFPETPWV
PPRRPWSLVN WLFWASLLLY PFFQFLVSMV SSGSSVTLAS LVLIFCMASM GVRWMIGVTE
IDKGSAYGNI DNKRKQTD
