ID   PLC2_CAEEL              Reviewed;         282 AA.
AC   Q22267;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   16-JUN-2009, entry version 53.
DE   RecName: Full=Putative 1-acyl-sn-glycerol-3-phosphate acyltransferase acl-2;
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=acl-2; ORFNames=T06E8.1;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Nematoda; Chromadorea; Rhabditida; Rhabditoidea;
OC   Rhabditidae; Peloderinae; Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   MEDLINE=99069613; PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for
RT   investigating biology.";
RL   Science 282:2012-2018(1998).
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; Z73975; CAA98276.1; -; Genomic_DNA.
DR   PIR; T24610; T24610.
DR   RefSeq; NP_505578.1; -.
DR   UniGene; Cel.36470; -.
DR   Ensembl; T06E8.1; Caenorhabditis elegans.
DR   GeneID; 179398; -.
DR   KEGG; cel:T06E8.1; -.
DR   NMPDR; fig|6239.3.peg.19283; -.
DR   WormBase; WBGene00011543; acl-2.
DR   WormPep; T06E8.1; CE06378.
DR   OMA; Q22267; ILLHGME.
DR   BRENDA; 2.3.1.51; 672.
DR   NextBio; 905224; -.
DR   ArrayExpress; Q22267; -.
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; Complete proteome; Membrane;
KW   Phospholipid biosynthesis; Transferase; Transmembrane.
FT   CHAIN         1    282       Putative 1-acyl-sn-glycerol-3-phosphate
FT                                acyltransferase acl-2.
FT                                /FTId=PRO_0000208203.
FT   TRANSMEM      4     24       Potential.
FT   TRANSMEM     32     52       Potential.
FT   TRANSMEM    122    142       Potential.
FT   MOTIF        98    103       HXXXXD motif.
SQ   SEQUENCE   282 AA;  32691 MW;  577D25A65F318C64 CRC64;
     MENFWSIVVF FLLSILFILY NISTVCHYYM RISFYYFTIL LHGMEVCVTM IPSWLNGKGA
     DYVFHSFFYW CKWTGVHTTV YGYEKTQVEG PAVVICNHQS SLDILSMASI WPKNCVVMMK
     RILAYVPFFN LGAYFSNTIF IDRYNRERAM ASVDYCASEM KNRNLKLWVF PEGTRNREGG
     FIPFKKGAFN IAVRAQIPII PVVFSDYRDF YSKPGRYFKN DGEVVIRVLD AIPTKGLTLD
     DVSELSDMCR DVMLAAYKEV TLEAQQRNAT RRGETKDGKK SE
//