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 24-JAN-2024, entry version 119. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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.ENSRNOP00000069883; -. DR PhosphoSitePlus; Q924S1; -. DR PaxDb; 10116-ENSRNOP00000024213; -. DR Ensembl; ENSRNOT00000024213.5; ENSRNOP00000024213.2; ENSRNOG00000017731.5. DR Ensembl; ENSRNOT00060017012; ENSRNOP00060013254; ENSRNOG00060010052. DR Ensembl; ENSRNOT00065050998; ENSRNOP00065041945; ENSRNOG00065029526. DR GeneID; 170919; -. DR KEGG; rno:170919; -. DR AGR; RGD:619916; -. DR CTD; 56895; -. DR RGD; 619916; Agpat4. DR eggNOG; KOG1505; Eukaryota. DR GeneTree; ENSGT00950000182836; -. DR InParanoid; Q924S1; -. DR OrthoDB; 921703at2759; -. 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 cell types or tissues. DR ExpressionAtlas; Q924S1; baseline and differential. 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:0005741; C:mitochondrial outer membrane; ISO:RGD. DR GO; GO:0003841; F:1-acylglycerol-3-phosphate O-acyltransferase activity; ISS:UniProtKB. 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 CDD; cd07990; LPLAT_LCLAT1-like; 1. DR InterPro; IPR032098; Acyltransf_C. DR InterPro; IPR002123; Plipid/glycerol_acylTrfase. DR PANTHER; PTHR10983:SF8; 1-ACYL-SN-GLYCEROL-3-PHOSPHATE ACYLTRANSFERASE DELTA; 1. DR PANTHER; PTHR10983; 1-ACYLGLYCEROL-3-PHOSPHATE ACYLTRANSFERASE-RELATED; 1. DR Pfam; PF16076; Acyltransf_C; 1. DR Pfam; PF01553; Acyltransferase; 1. DR SMART; SM00563; PlsC; 1. DR SUPFAM; SSF69593; Glycerol-3-phosphate (1)-acyltransferase; 1. DR Genevisible; Q924S1; RN. 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 //