PLC1_CAEEL
ID PLC1_CAEEL Reviewed; 262 AA.
AC Q93841; Q93783;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 2.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Putative 1-acyl-sn-glycerol-3-phosphate acyltransferase acl-1;
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-1; ORFNames=F59F4.4;
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; Z81095; CAB03160.1; -; Genomic_DNA.
DR EMBL; Z81089; CAB03160.1; JOINED; Genomic_DNA.
DR PIR; T22599; T22599.
DR RefSeq; NP_510606.1; NM_078205.5.
DR AlphaFoldDB; Q93841; -.
DR SMR; Q93841; -.
DR STRING; 6239.F59F4.4; -.
DR EPD; Q93841; -.
DR PaxDb; Q93841; -.
DR PeptideAtlas; Q93841; -.
DR EnsemblMetazoa; F59F4.4.1; F59F4.4.1; WBGene00010339.
DR GeneID; 181671; -.
DR KEGG; cel:CELE_F59F4.4; -.
DR UCSC; F59F4.4; c. elegans.
DR CTD; 181671; -.
DR WormBase; F59F4.4; CE11552; WBGene00010339; acl-1.
DR eggNOG; KOG2848; Eukaryota.
DR GeneTree; ENSGT00390000008726; -.
DR HOGENOM; CLU_027938_10_2_1; -.
DR InParanoid; Q93841; -.
DR OMA; MYIYPEG; -.
DR OrthoDB; 1623097at2759; -.
DR PhylomeDB; Q93841; -.
DR UniPathway; UPA00557; UER00613.
DR PRO; PR:Q93841; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00010339; Expressed in larva and 4 other tissues.
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..262
FT /note="Putative 1-acyl-sn-glycerol-3-phosphate
FT acyltransferase acl-1"
FT /id="PRO_0000208202"
FT TRANSMEM 3..23
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 29..49
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 89..109
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOTIF 94..99
FT /note="HXXXXD motif"
SQ SEQUENCE 262 AA; 29638 MW; 0361FE6C9710593E CRC64;
MTFLAILFVI AVLLLLAQLP VIGFYIRAVY FGMCLIIGGF LGGLASIPFG KSPNNHFRMF
KIFQAMTWPM GVRFELRNSE ILHDKKPYII IANHQSALDV LGMSFAWPVD CVVMLKSSLK
YLPGFNLCAY LCDSVYINRF SKEKALKTVD TTLHEIVTKK RKVWIYPEGT RNAEPELLPF
KKGAFILAKQ AKIPIVPCVF SSHKFFYSHA EKRLTSGNCI IDILPEVDSS KFDSIDDLSA
HCRKIMQAHR EKLDAEAANL NI
