ID   PLSC_LIMDO              Reviewed;         281 AA.
AC   Q42870; Q40120;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   16-JUN-2009, entry version 43.
DE   RecName: Full=1-acyl-sn-glycerol-3-phosphate acyltransferase;
DE            Short=1-AGP acyltransferase;
DE            Short=1-AGPAT;
DE            EC=2.3.1.51;
DE   AltName: Full=Lysophosphatidic acid acyltransferase;
DE            Short=LPAAT;
GN   Name=PLSC;
OS   Limnanthes douglasii (Douglas's meadowfoam).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC   rosids; eurosids II; Brassicales; Limnanthaceae; Limnanthes.
OX   NCBI_TaxID=28973;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=96028122; PubMed=7588719;
RX   DOI=10.1111/j.1432-1033.1995.806zz.x;
RA   Hanke C., Wolter F.P., Coleman J., Peterek G., Frentzen M.;
RT   "A plant acyltransferase involved in triacylglycerol biosynthesis
RT   complements an Escherichia coli sn-1-acylglycerol-3-phosphate
RT   acyltransferase mutant.";
RL   Eur. J. Biochem. 232:806-810(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=96046746; PubMed=7579178; DOI=10.1007/BF00043651;
RA   Brown A.P., Brough C.L., Kroon J., Slabas A.R.;
RT   "Identification of a cDNA that encodes a 1-acyl-sn-glycerol-3-
RT   phosphate acyltransferase from Limnanthes douglasii.";
RL   Plant Mol. Biol. 29:267-278(1995).
CC   -!- FUNCTION: Converts lysophosphatidic acid (LPA) into phosphatidic
CC       acid by incorporating acyl moiety at the 2 position. This enzyme
CC       uses erucoyl-CoA as an acyl donor.
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; X83266; CAA58239.1; -; mRNA.
DR   EMBL; Z46836; CAA86877.1; -; mRNA.
DR   PIR; S60477; S60477.
DR   BRENDA; 2.3.1.51; 263641.
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   InterPro; IPR004552; AGP_acyltrans.
DR   Pfam; PF01553; Acyltransferase; 1.
DR   SMART; SM00563; PlsC; 1.
DR   TIGRFAMs; TIGR00530; AGP_acyltrn; 1.
PE   2: Evidence at transcript level;
KW   Acyltransferase; Membrane; Phospholipid biosynthesis; Transferase;
KW   Transmembrane.
FT   CHAIN         1    281       1-acyl-sn-glycerol-3-phosphate
FT                                acyltransferase.
FT                                /FTId=PRO_0000208187.
FT   TRANSMEM     40     60       Potential.
FT   TRANSMEM     71     91       Potential.
FT   TRANSMEM    110    130       Potential.
FT   MOTIF       109    114       HXXXXD motif.
FT   CONFLICT     46     46       I -> V (in Ref. 2; CAA86877).
FT   CONFLICT    188    188       R -> G (in Ref. 2; CAA86877).
FT   CONFLICT    262    262       V -> I (in Ref. 2; CAA86877).
FT   CONFLICT    281    281       N -> K (in Ref. 2; CAA86877).
SQ   SEQUENCE   281 AA;  31717 MW;  9C880BD9E492EE2A CRC64;
     MAKTRTSSLR NRRQLKPAVA ATADDDKDGV FMVLLSCFKI FVCFAIVLIT AVAWGLIMVL
     LLPWPYMRIR LGNLYGHIIG GLVIWIYGIP IKIQGSEHTK KRAIYISNHA SPIDAFFVMW
     LAPIGTVGVA KKEVIWYPLL GQLYTLAHHI RIDRSNPAAA IQSMKEAVRV ITEKNLSLIM
     FPEGTRSRDG RLLPFKKGFV HLALQSHLPI VPMILTGTHL AWRKGTFRVR PVPITVKYLP
     PINTDDWTVD KIDDYVKMIH DVYVRNLPAS QKPLGSTNRS N
//