ID   PLCD_MACFA              Reviewed;         378 AA.
AC   Q4R581;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   05-MAY-2009, entry version 18.
DE   RecName: Full=1-acyl-sn-glycerol-3-phosphate acyltransferase delta;
DE            EC=2.3.1.51;
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; ORFNames=QccE-15256;
OS   Macaca fascicularis (Crab eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   International consortium for macaque cDNA sequencing and analysis;
RT   "DNA sequences of macaque genes expressed in brain or testis and its
RT   evolutionary implications.";
RL   Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Converts lysophosphatidic acid (LPA) into phosphatidic
CC       acid by incorporating an acyl moiety at the sn-2 position of the
CC       glycerol backbone (By similarity).
CC   -!- CATALYTIC ACTIVITY: Acyl-CoA + 1-acyl-sn-glycerol 3-phosphate =
CC       CoA + 1,2-diacyl-sn-glycerol 3-phosphate.
CC   -!- PATHWAY: Phospholipid metabolism; CDP-diacylglycerol biosynthesis;
CC       CDP-diacylglycerol from sn-glycerol 3-phosphate: step 2/3.
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein
CC       (Potential).
CC   -!- DOMAIN: The HXXXXD motif is essential for acyltransferase activity
CC       and may constitute the binding site for the phosphate moiety of
CC       the glycerol-3-phosphate (By similarity).
CC   -!- SIMILARITY: Belongs to the 1-acyl-sn-glycerol-3-phosphate
CC       acyltransferase family.
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DR   EMBL; AB169663; BAE01744.1; -; mRNA.
DR   HOVERGEN; Q4R581; -.
DR   BRENDA; 2.3.1.51; 3438.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0003841; F:1-acylglycerol-3-phosphate O-acyltransferas...; IEA:EC.
DR   GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-KW.
DR   InterPro; IPR002123; Acyltransferase.
DR   Pfam; PF01553; Acyltransferase; 1.
DR   SMART; SM00563; PlsC; 1.
PE   2: Evidence at transcript level;
KW   Acyltransferase; Membrane; Phospholipid biosynthesis; Transferase;
KW   Transmembrane.
FT   CHAIN         1    378       1-acyl-sn-glycerol-3-phosphate
FT                                acyltransferase delta.
FT                                /FTId=PRO_0000293477.
FT   TRANSMEM     11     31       Potential.
FT   TRANSMEM    125    145       Potential.
FT   TRANSMEM    307    327       Potential.
FT   TRANSMEM    338    358       Potential.
FT   MOTIF        96    101       HXXXXD motif.
SQ   SEQUENCE   378 AA;  44049 MW;  5200441D0729BB67 CRC64;
     MDLAGLLKSQ FLCHLVFCYV FIASGLIINT VQLFTLLLWP INKQLFRKIN CRLSYCISSQ
     LVMLLEWWSG TECTIFTDPR AYPKYGKENA IVVLNHKFEI DFLCGWSLSE RFGLLGGSKV
     LAKKELAYVP IIGWMWYFTE MVFCSRKWEQ DRKTVATSLQ HLRDYPEKYF FLIHCEGTRF
     TEKKHEISMQ VARAKGLPRL KHHPLPRTKG FAITVRSLRN VVSAVYDCTL NFRNNENPTL
     LGVLNGKKYH ADLYVRRIPL EDIPEDDDRC SAWLHKLYQE KDAFQEEYYR TGTFPETPMV
     PPRRPWTLVN WLFWASLVLY PFFQFLVSMI RSGSSLTLAS FILVFFVASM GVRWMIGVTE
     IDKGSAYGNS DSKQKQND
//