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   25-MAY-2022, entry version 67.
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' meadowfoam).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Limnanthaceae; Limnanthes.
OX   NCBI_TaxID=28973;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=7588719; 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   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-phosphate
RT   acyltransferase from Limnanthes douglasii.";
RL   Plant Mol. Biol. 29:267-278(1995).
CC   -!- FUNCTION: Converts lysophosphatidic acid (LPA) into phosphatidic acid
CC       by incorporating acyl moiety at the 2 position. This enzyme uses
CC       erucoyl-CoA as an acyl donor.
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   -!- PATHWAY: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-
CC       diacylglycerol from sn-glycerol 3-phosphate: step 2/3.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
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}.
CC   -!- SIMILARITY: Belongs to the 1-acyl-sn-glycerol-3-phosphate
CC       acyltransferase family. {ECO:0000305}.
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DR   EMBL; X83266; CAA58239.1; -; mRNA.
DR   EMBL; Z46836; CAA86877.1; -; mRNA.
DR   PIR; S60477; S60477.
DR   AlphaFoldDB; Q42870; -.
DR   SMR; Q42870; -.
DR   BRENDA; 2.3.1.51; 3028.
DR   UniPathway; UPA00557; UER00613.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0003841; F:1-acylglycerol-3-phosphate O-acyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016024; P:CDP-diacylglycerol biosynthetic process; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR004552; AGP_acyltrans.
DR   InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR   Pfam; PF01553; Acyltransferase; 1.
DR   SMART; SM00563; PlsC; 1.
DR   TIGRFAMs; TIGR00530; AGP_acyltrn; 1.
PE   2: Evidence at transcript level;
KW   Acyltransferase; Lipid biosynthesis; Lipid metabolism; Membrane;
KW   Phospholipid biosynthesis; Phospholipid metabolism; Transferase;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..281
FT                   /note="1-acyl-sn-glycerol-3-phosphate acyltransferase"
FT                   /id="PRO_0000208187"
FT   TRANSMEM        40..60
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        71..91
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        110..130
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   MOTIF           109..114
FT                   /note="HXXXXD motif"
FT   CONFLICT        46
FT                   /note="I -> V (in Ref. 2; CAA86877)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        188
FT                   /note="R -> G (in Ref. 2; CAA86877)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        262
FT                   /note="V -> I (in Ref. 2; CAA86877)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        281
FT                   /note="N -> K (in Ref. 2; CAA86877)"
FT                   /evidence="ECO:0000305"
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