PLC12_CAEEL
ID PLC12_CAEEL Reviewed; 391 AA.
AC Q11087;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 25-MAY-2022, entry version 105.
DE RecName: Full=Putative 1-acyl-sn-glycerol-3-phosphate acyltransferase acl-12;
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-12; ORFNames=C01C10.3;
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}.
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DR EMBL; FO080255; CCD62384.1; -; Genomic_DNA.
DR PIR; T15366; T15366.
DR RefSeq; NP_509260.1; NM_076859.4.
DR AlphaFoldDB; Q11087; -.
DR STRING; 6239.C01C10.3; -.
DR EPD; Q11087; -.
DR PaxDb; Q11087; -.
DR PeptideAtlas; Q11087; -.
DR EnsemblMetazoa; C01C10.3.1; C01C10.3.1; WBGene00015295.
DR GeneID; 181001; -.
DR KEGG; cel:CELE_C01C10.3; -.
DR UCSC; C01C10.3; c. elegans.
DR CTD; 181001; -.
DR WormBase; C01C10.3; CE02449; WBGene00015295; acl-12.
DR eggNOG; KOG1505; Eukaryota.
DR GeneTree; ENSGT00950000182836; -.
DR HOGENOM; CLU_046804_0_0_1; -.
DR InParanoid; Q11087; -.
DR OMA; TPLGVMW; -.
DR OrthoDB; 836124at2759; -.
DR PhylomeDB; Q11087; -.
DR UniPathway; UPA00557; UER00613.
DR PRO; PR:Q11087; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00015295; Expressed in material anatomical entity and 5 other tissues.
DR GO; GO:0012505; C:endomembrane system; IBA:GO_Central.
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; IEA:UniProtKB-EC.
DR GO; GO:0016746; F:acyltransferase activity; IBA:GO_Central.
DR GO; GO:0016024; P:CDP-diacylglycerol biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0036149; P:phosphatidylinositol acyl-chain remodeling; IBA:GO_Central.
DR InterPro; IPR032098; Acyltransf_C.
DR InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR Pfam; PF16076; Acyltransf_C; 1.
DR Pfam; PF01553; Acyltransferase; 1.
DR SMART; SM00563; PlsC; 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..391
FT /note="Putative 1-acyl-sn-glycerol-3-phosphate
FT acyltransferase acl-12"
FT /id="PRO_0000065097"
FT TRANSMEM 47..67
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 84..104
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOTIF 124..129
FT /note="HXXXXD motif"
SQ SEQUENCE 391 AA; 44718 MW; FB5C062A0172A8C1 CRC64;
MLKSGLMDTD DQKVGVRVAN IDMSERTDNV HLIEIRRIIS LVGAAYFFFM TAWVVPVACV
ITVSLLFPLM LFSTPLFNYL EHKLCAMVNA HWNAVSVFVG ATVTEYGTNL AGYAEEKCLL
LANHLGLLDH FVLMQSLNGK GSIRSRWMWV IYNIWKYTPL GVMWTSHGNF FVNGGVSKRD
SVLSSFRDHL KNSFYKYDYG WVIMYPEGSR LYLVKNSGRT FAEKNGLKPL DNCVYPRTGA
AHAVLDVLGP TDDSLSMSKC GKGEPIKYII DATIGYRKGA VPDICDVMMG DWESVEASQF
AVHYDVIPVK PEWSDENLLK EFLYERYIIK DKLLAEFYKT GHFPGDKTKV IPNNYEMMFA
QVFWGCLYYA HYVYWLRPLI VHSWTSFLSI F
