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   03-AUG-2022, entry version 137.
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; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   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 investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
CC   -!- FUNCTION: Converts lysophosphatidic acid (LPA) into phosphatidic acid
CC       by incorporating an acyl moiety at the sn-2 position of the glycerol
CC       backbone. {ECO:0000250}.
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; Z73975; CAA98276.1; -; Genomic_DNA.
DR   PIR; T24610; T24610.
DR   RefSeq; NP_001256175.1; NM_001269246.1.
DR   AlphaFoldDB; Q22267; -.
DR   SMR; Q22267; -.
DR   STRING; 6239.T06E8.1a; -.
DR   EPD; Q22267; -.
DR   PaxDb; Q22267; -.
DR   PeptideAtlas; Q22267; -.
DR   EnsemblMetazoa; T06E8.1a.1; T06E8.1a.1; WBGene00011543.
DR   GeneID; 179398; -.
DR   KEGG; cel:CELE_T06E8.1; -.
DR   UCSC; T06E8.1.1; c. elegans.
DR   CTD; 179398; -.
DR   WormBase; T06E8.1a; CE06378; WBGene00011543; acl-2.
DR   eggNOG; KOG2848; Eukaryota.
DR   GeneTree; ENSGT00390000008726; -.
DR   HOGENOM; CLU_027938_10_1_1; -.
DR   InParanoid; Q22267; -.
DR   OMA; MASVDYC; -.
DR   OrthoDB; 1623097at2759; -.
DR   PhylomeDB; Q22267; -.
DR   Reactome; R-CEL-1483166; Synthesis of PA.
DR   Reactome; R-CEL-163765; ChREBP activates metabolic gene expression.
DR   UniPathway; UPA00557; UER00613.
DR   PRO; PR:Q22267; -.
DR   Proteomes; UP000001940; Chromosome V.
DR   Bgee; WBGene00011543; Expressed in germ line (C elegans) and 4 other tissues.
DR   ExpressionAtlas; Q22267; baseline and differential.
DR   GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0003841; F:1-acylglycerol-3-phosphate O-acyltransferase activity; IBA:GO_Central.
DR   GO; GO:0016024; P:CDP-diacylglycerol biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006654; P:phosphatidic acid biosynthetic process; IBA:GO_Central.
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   3: Inferred from homology;
KW   Acyltransferase; Lipid biosynthesis; Lipid metabolism; Membrane;
KW   Phospholipid biosynthesis; Phospholipid metabolism; Reference proteome;
KW   Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..282
FT                   /note="Putative 1-acyl-sn-glycerol-3-phosphate
FT                   acyltransferase acl-2"
FT                   /id="PRO_0000208203"
FT   TRANSMEM        4..24
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        32..52
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        122..142
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   MOTIF           98..103
FT                   /note="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