ID PLSC_LIMAL Reviewed; 281 AA. AC Q42868; DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 16-JUN-2009, entry version 39. 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; OS Limnanthes alba (White meadowfoam). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC rosids; eurosids II; Brassicales; Limnanthaceae; Limnanthes. OX NCBI_TaxID=42439; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=Alba; RX MEDLINE=96106201; PubMed=8539298; DOI=10.1104/pp.109.4.1389; RA Lassner M.W., Levering C.K., Davies H.M.D., Knutzon D.S.; RT "Lysophosphatidic acid acyltransferase from meadowfoam mediates RT insertion of erucic acid at the sn-2 position of triacylglycerol in RT transgenic rapeseed oil."; RL Plant Physiol. 109:1389-1394(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. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U32988; AAC49185.1; -; mRNA. DR BRENDA; 2.3.1.51; 295322. 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_0000208186. FT TRANSMEM 40 60 Potential. FT TRANSMEM 71 91 Potential. FT TRANSMEM 110 130 Potential. FT MOTIF 109 114 HXXXXD motif. SQ SEQUENCE 281 AA; 31665 MW; 2725B811777A6067 CRC64; MAKTRTSSLR NRRQLKTAVA ATADDDKDGI FMVLLSCFKI FVCFAIVLIT AVAWGLIMVL LLPWPYMRIR LGNLYGHIIG GLVIWLYGIP IEIQGSEHTK KRAIYISNHA SPIDAFFVMW LAPIGTVGVA KKEVIWYPLL GQLYTLAHHI RIDRSNPAAA IQSMKEAVRV ITEKNLSLIM FPEGTRSGDG RLLPFKKGFV HLALQSHLPI VPMILTGTHL AWRKGTFRVR PVPITVKYLP PINTDDWTVD KIDDYVKMIH DIYVRNLPAS QKPLGSTNRS K //