CDSA_CAEEL
ID CDSA_CAEEL Reviewed; 465 AA.
AC P53439; G8JY50;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 03-SEP-2014, sequence version 2.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Phosphatidate cytidylyltransferase;
DE EC=2.7.7.41;
DE AltName: Full=CDP-DAG synthase;
DE AltName: Full=CDP-DG synthase;
DE AltName: Full=CDP-diacylglycerol synthase;
DE AltName: Full=CDP-diglyceride pyrophosphorylase;
DE AltName: Full=CDP-diglyceride synthase;
GN Name=cdgs-1; ORFNames=C33H5.18;
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).
RN [2]
RP DISRUPTION PHENOTYPE.
RX PubMed=24449268; DOI=10.1101/gad.230599.113;
RA Bahmanyar S., Biggs R., Schuh A.L., Desai A., Muller-Reichert T.,
RA Audhya A., Dixon J.E., Oegema K.;
RT "Spatial control of phospholipid flux restricts endoplasmic reticulum sheet
RT formation to allow nuclear envelope breakdown.";
RL Genes Dev. 28:121-126(2014).
CC -!- FUNCTION: Provides CDP-diacylglycerol, an important precursor for the
CC synthesis of phosphatidylinositol (PtdIns). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphate + CTP + H(+) = a CDP-1,2-
CC diacyl-sn-glycerol + diphosphate; Xref=Rhea:RHEA:16229,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37563,
CC ChEBI:CHEBI:58332, ChEBI:CHEBI:58608; EC=2.7.7.41;
CC -!- PATHWAY: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-
CC diacylglycerol from sn-glycerol 3-phosphate: step 3/3.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=b;
CC IsoId=P53439-1; Sequence=Displayed;
CC Name=a;
CC IsoId=P53439-2; Sequence=VSP_055417;
CC -!- DISRUPTION PHENOTYPE: Reduced levels of phosphatidylinositol. No effect
CC on two-cell stage nuclear morphology. Significant rescue of the nuclear
CC morphology defects resulting from inhibition of cnep-1 or partial
CC inhibition of lpin-1 but does not rescue the nuclear envelope
CC disassembly defects observed following depletion of npp-12.
CC {ECO:0000269|PubMed:24449268}.
CC -!- SIMILARITY: Belongs to the CDS family. {ECO:0000305}.
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DR EMBL; FO080768; CCD66581.1; -; Genomic_DNA.
DR EMBL; FO080768; CCD66582.1; -; Genomic_DNA.
DR PIR; T34155; T34155.
DR RefSeq; NP_501297.1; NM_068896.3. [P53439-2]
DR RefSeq; NP_501298.1; NM_068897.3. [P53439-1]
DR AlphaFoldDB; P53439; -.
DR BioGRID; 532364; 1.
DR IntAct; P53439; 1.
DR MINT; P53439; -.
DR STRING; 6239.C33H5.18b; -.
DR iPTMnet; P53439; -.
DR EPD; P53439; -.
DR PaxDb; P53439; -.
DR PeptideAtlas; P53439; -.
DR EnsemblMetazoa; C33H5.18a.1; C33H5.18a.1; WBGene00016384. [P53439-2]
DR EnsemblMetazoa; C33H5.18b.1; C33H5.18b.1; WBGene00016384. [P53439-1]
DR GeneID; 3565046; -.
DR KEGG; cel:CELE_C33H5.18; -.
DR UCSC; C33H5.18b; c. elegans. [P53439-1]
DR CTD; 3565046; -.
DR WormBase; C33H5.18a; CE04161; WBGene00016384; cdgs-1. [P53439-2]
DR WormBase; C33H5.18b; CE26907; WBGene00016384; cdgs-1. [P53439-1]
DR eggNOG; KOG1440; Eukaryota.
DR GeneTree; ENSGT00940000170268; -.
DR InParanoid; P53439; -.
DR OMA; FIMNNIF; -.
DR OrthoDB; 1072976at2759; -.
DR PhylomeDB; P53439; -.
DR Reactome; R-CEL-1483148; Synthesis of PG.
DR Reactome; R-CEL-1483226; Synthesis of PI.
DR UniPathway; UPA00557; UER00614.
DR PRO; PR:P53439; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00016384; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0004605; F:phosphatidate cytidylyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0016024; P:CDP-diacylglycerol biosynthetic process; IEA:UniProtKB-UniPathway.
DR InterPro; IPR000374; PC_trans.
DR InterPro; IPR016720; PC_Trfase_euk.
DR PANTHER; PTHR13773; PTHR13773; 1.
DR PIRSF; PIRSF018269; PC_trans_euk; 1.
DR PROSITE; PS01315; CDS; 1.
PE 3: Inferred from homology;
KW Alternative splicing; Lipid biosynthesis; Lipid metabolism; Membrane;
KW Nucleotidyltransferase; Phospholipid biosynthesis; Phospholipid metabolism;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..465
FT /note="Phosphatidate cytidylyltransferase"
FT /id="PRO_0000090719"
FT TRANSMEM 95..117
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 121..143
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 158..178
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 187..207
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 214..234
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 239..259
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 288..308
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 367..387
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..42
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 52..62
FT /note="SDAGSKNKEEK -> R (in isoform a)"
FT /evidence="ECO:0000305"
FT /id="VSP_055417"
SQ SEQUENCE 465 AA; 53460 MW; D02E7C5F17E9D3DD CRC64;
MSDQPPAENA DVRQRRAPES PVTERLRAPA RDDARPTSDE SDMEGILQDE DSDAGSKNKE
EKLERLTQAI PQDKGSLGVF ADSMLEALPP RWRNWVVRGL FSIIMISTFT FIVTRGATWL
MFLVFLIQFK CFQEIISIGL AVYRLYDFPW FRALSWYFLL TSNYFFFGES LIDYWGIVLK
KDNFLHFLVA YHRLVSFALY CIGFVSFVLS LRKGYYMRQF SLFAWTHLTL LLIVSQSFFI
IQNIFQGLIW FLAPVAMIIC CDIMSYMFGF FWGKTPLIKL SPKKTWEGFI GGAFSTVVFG
ILLSLALYNR PFFVCPVQHY QTDSSNCTIP LAFQLQDYPV PRPFSFVYKI LRKEPIIQLC
PFVFHSIALS LFASILGPFG GFFASGFKRA FKIKDFGDVI PGHGGLMDRF DCQLLMGTFV
MVYIHSFIRV PDASKLLKQI MTLEPQDQLN IFNLLQSELS KTGLI
