ID   PLSC_COCNU              Reviewed;         308 AA.
AC   Q42670;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   16-JUN-2009, entry version 38.
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   Cocos nucifera (Coconut).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; Liliopsida; Arecaceae; Arecoideae;
OC   Cocoseae; Attaleinae; Cocos.
OX   NCBI_TaxID=13894;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC   TISSUE=Endosperm;
RX   MEDLINE=96163190; PubMed=8552723; DOI=10.1104/pp.109.3.999;
RA   Knutzon D.S., Lardizabal K.D., Nelsen J.S., Bleibaum J.L.,
RA   Davies H.M., Metz J.G.;
RT   "Cloning of a coconut endosperm cDNA encoding a 1-acyl-sn-glycerol-3-
RT   phosphate acyltransferase that accepts medium-chain-length
RT   substrates.";
RL   Plant Physiol. 109:999-1006(1995).
CC   -!- FUNCTION: Converts lysophosphatidic acid (LPA) into phosphatidic
CC       acid by incorporating acyl moiety at the 2 position. This enzyme
CC       shows a preference for medium-chain-length fatty acyl-coenzyme a
CC       substrates.
CC   -!- CATALYTIC ACTIVITY: Acyl-CoA + 1-acyl-sn-glycerol 3-phosphate =
CC       CoA + 1,2-diacyl-sn-glycerol 3-phosphate.
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; U29657; AAC49119.1; -; mRNA.
DR   BRENDA; 2.3.1.51; 118852.
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   1: Evidence at protein level;
KW   Acyltransferase; Direct protein sequencing; Membrane;
KW   Phospholipid biosynthesis; Transferase; Transmembrane.
FT   CHAIN         1    308       1-acyl-sn-glycerol-3-phosphate
FT                                acyltransferase.
FT                                /FTId=PRO_0000208185.
FT   TRANSMEM     65     85       Potential.
FT   TRANSMEM    124    144       Potential.
FT   TRANSMEM    148    168       Potential.
FT   MOTIF       130    135       HXXXXD motif.
SQ   SEQUENCE   308 AA;  34809 MW;  3773CF8C03C3C0FE CRC64;
     MDASGASSFL RGRCLESCFK ASFGMSQPKD AAGQPSRRPA DADDFVDDDR WITVILSVVR
     IAACFLSMMV TTIVWNMIML ILLPWPYARI RQGNLYGHVT GRMLMWILGN PITIEGSEFS
     NTRAIYICNH ASLVDIFLIM WLIPKGTVTI AKKEIIWYPL FGQLYVLANH QRIDRSNPSA
     AIESIKEVAR AVVKKNLSLI IFPEGTRSKT GRLLPFKKGF IHIALQTRLP IVPMVLTGTH
     LAWRKNSLRV RPAPITVKYF SPIKTDDWEE EKINHYVEMI HALYVDHLPE SQKPLVSKGR
     DASGRSNS
//