PLCD_PONAB
ID PLCD_PONAB Reviewed; 378 AA.
AC Q5R757;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 60.
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 Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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; CR860261; CAH92403.1; -; mRNA.
DR RefSeq; NP_001126417.1; NM_001132945.1.
DR AlphaFoldDB; Q5R757; -.
DR STRING; 9601.ENSPPYP00000019214; -.
DR GeneID; 100173400; -.
DR KEGG; pon:100173400; -.
DR CTD; 56895; -.
DR eggNOG; KOG1505; Eukaryota.
DR InParanoid; Q5R757; -.
DR UniPathway; UPA00557; UER00613.
DR Proteomes; UP000001595; Unplaced.
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; ISS:UniProtKB.
DR GO; GO:0016024; P:CDP-diacylglycerol biosynthetic process; IEA:UniProtKB-UniPathway.
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_0000293478"
FT TRANSMEM 11..31
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 125..145
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 307..327
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; 43963 MW; 91FC13D196F8CDC7 CRC64;
MDLAGLLKSQ FLCHLVFCYV FIASGLIINT IQLFTLLLWP INKQLFRKIN CRLSYCISSQ
LVMLLEWWSG TECTIFTDPR AYLKYGKENA IVVLNHKFEI DFLCGWSLSE RFGLLGGSKV
LAKKELAYVP IIGWMWYFTE MVFCSRKWEQ DRKTVATSLQ HLRDYPEKYF FLIHCEGTRF
TEKKHEISMQ VARAKGLPRL KHHLLPRTKG FAITVRSLRN VVSAVYDCTL NFRNNENPTL
LGVLNGKKYH ADLYVRRIPL EDIPEDDDEC SAWLHKLYQE KDAFQEEYYR TGTFPETPMV
PPRRPWTLVN WLFWASLVLY PFFQFLVSMI RSGSSLTLAS FILVFFVASV GVRWMIGVTE
IDKGSAYGNS GSKQKLND
