PLSB_CAEEL
ID PLSB_CAEEL Reviewed; 718 AA.
AC Q22949;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Probable glycerol-3-phosphate acyltransferase, mitochondrial;
DE Short=GPAT;
DE EC=2.3.1.15;
DE Flags: Precursor;
GN Name=acl-6; ORFNames=F08F3.2;
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 -!- CATALYTIC ACTIVITY:
CC Reaction=an acyl-CoA + sn-glycerol 3-phosphate = a 1-acyl-sn-glycero-3-
CC phosphate + CoA; Xref=Rhea:RHEA:15325, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57597, ChEBI:CHEBI:57970, ChEBI:CHEBI:58342; EC=2.3.1.15;
CC -!- PATHWAY: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-
CC diacylglycerol from sn-glycerol 3-phosphate: step 1/3.
CC -!- SUBCELLULAR LOCATION: Mitochondrion membrane {ECO:0000305}; Single-pass
CC membrane 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 GPAT/DAPAT family. {ECO:0000305}.
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DR EMBL; FO080663; CCD65590.1; -; Genomic_DNA.
DR PIR; T29448; T29448.
DR RefSeq; NP_001023769.1; NM_001028598.3.
DR AlphaFoldDB; Q22949; -.
DR BioGRID; 43977; 1.
DR DIP; DIP-26239N; -.
DR STRING; 6239.F08F3.2a; -.
DR iPTMnet; Q22949; -.
DR EPD; Q22949; -.
DR PaxDb; Q22949; -.
DR PeptideAtlas; Q22949; -.
DR EnsemblMetazoa; F08F3.2a.1; F08F3.2a.1; WBGene00017261.
DR GeneID; 178928; -.
DR KEGG; cel:CELE_F08F3.2; -.
DR UCSC; F08F3.2a.1; c. elegans.
DR CTD; 178928; -.
DR WormBase; F08F3.2a; CE09258; WBGene00017261; acl-6.
DR eggNOG; KOG3729; Eukaryota.
DR GeneTree; ENSGT00520000055570; -.
DR InParanoid; Q22949; -.
DR OMA; GYQSKKT; -.
DR OrthoDB; 198209at2759; -.
DR PhylomeDB; Q22949; -.
DR Reactome; R-CEL-1483166; Synthesis of PA.
DR Reactome; R-CEL-75109; Triglyceride biosynthesis.
DR UniPathway; UPA00557; UER00612.
DR PRO; PR:Q22949; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00017261; Expressed in germ line (C elegans) and 4 other tissues.
DR ExpressionAtlas; Q22949; baseline and differential.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031966; C:mitochondrial membrane; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IDA:WormBase.
DR GO; GO:0005886; C:plasma membrane; IEA:InterPro.
DR GO; GO:0004366; F:glycerol-3-phosphate O-acyltransferase activity; IBA:GO_Central.
DR GO; GO:0102420; F:sn-1-glycerol-3-phosphate C16:0-DCA-CoA acyl transferase activity; IEA:UniProtKB-EC.
DR GO; GO:0016024; P:CDP-diacylglycerol biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006631; P:fatty acid metabolic process; IBA:GO_Central.
DR GO; GO:0006072; P:glycerol-3-phosphate metabolic process; IBA:GO_Central.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IBA:GO_Central.
DR GO; GO:0019432; P:triglyceride biosynthetic process; IBA:GO_Central.
DR CDD; cd07993; LPLAT_DHAPAT-like; 1.
DR InterPro; IPR022284; GPAT/DHAPAT.
DR InterPro; IPR041728; GPAT/DHAPAT_LPLAT.
DR InterPro; IPR045520; GPAT_C.
DR InterPro; IPR028354; GPAT_PlsB.
DR InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR PANTHER; PTHR12563; PTHR12563; 1.
DR Pfam; PF01553; Acyltransferase; 1.
DR Pfam; PF19277; GPAT_C; 1.
DR PIRSF; PIRSF500064; GPAT; 1.
DR PIRSF; PIRSF000437; GPAT_DHAPAT; 1.
DR SMART; SM00563; PlsC; 1.
PE 3: Inferred from homology;
KW Acyltransferase; Lipid biosynthesis; Lipid metabolism; Membrane;
KW Mitochondrion; Phospholipid biosynthesis; Phospholipid metabolism;
KW Reference proteome; Transferase; Transit peptide; Transmembrane;
KW Transmembrane helix.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..718
FT /note="Probable glycerol-3-phosphate acyltransferase,
FT mitochondrial"
FT /id="PRO_0000024693"
FT TRANSMEM 409..425
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOTIF 167..172
FT /note="HXXXXD motif"
SQ SEQUENCE 718 AA; 82072 MW; E0A36A4A86FC138D CRC64;
MELDVESTSI TQLRSHCETC FPLMEEVVPR RERYVDLLEF SNFNGIPYPV VDPSRKPRRF
LADFRYSWSI PLIHHYPNVE KDVLSSKRVH RVISKLKEQN DEQKNRAVQF FTEISARLSK
FICKCCSYVL YKVFRRLMDK LLVCKEEMEV LYEAEQTGIP MVYLPLHRSH LDYLLITWCN
WHFGLKLPHI ASGDNLNLSG LGWLLRATGA FFIRRRVDPD DERGKDQLYR AILHSYIEQV
LSKDMPIEFF LEGTRSRFGK ALTPKNGLIS NVVEAVQHGF IKDCYLVPVS YTYDAVVEGI
FLHELMGIPK VRESVLGVFR GIFSGFSKSK QCGVVRMHYG RPIRLTEYLA TITASLSSNH
RTRPVRMTKL STSFSYRELV PWHRTHSETV DDRTMIRAIG FHVVYEAQMM CSISPVAVVS
CLLLAKWRGK VSRSTFERDC EWLCEKIIAE GGDVVGYQSK KTKGSALVKY AFEKLESCVE
VTDEYVSPKE SHSSFITLAY NKNSVICRFS IKSVIALTIV SRPSGTKLSI DQIVEDALSL
CDWLQFEFMF CRPCDSLREL VHNVLGQKEW SDPIHGFLRS EIEDDGFLDA GGALNSGTLR
VRDAKSRETL QFFANLVRPF VQSLYLISSF VVSEKCPTEP TSDNNIIRQL CQQSLAGDID
LPFAPLLESI NSDSFKNALR VLKDKGLLQR STPNSTARSG NSRLAELISN LERVLEVK
