CDS2_RAT
ID CDS2_RAT Reviewed; 443 AA.
AC Q91XU8;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 25-MAY-2022, entry version 119.
DE RecName: Full=Phosphatidate cytidylyltransferase 2 {ECO:0000305};
DE EC=2.7.7.41 {ECO:0000269|PubMed:29253589};
DE AltName: Full=CDP-DAG synthase 2;
DE AltName: Full=CDP-DG synthase 2;
DE AltName: Full=CDP-diacylglycerol synthase 2;
DE Short=CDS 2;
DE AltName: Full=CDP-diglyceride pyrophosphorylase 2;
DE AltName: Full=CDP-diglyceride synthase 2;
DE AltName: Full=CTP:phosphatidate cytidylyltransferase 2;
GN Name=Cds2 {ECO:0000312|RGD:621186};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Wistar; TISSUE=Brain;
RA Saino-Saito S.;
RT "Gene cloning and characterization of rat CDP-diacylglycerol synthase type
RT 2 (CDS2).";
RL Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20; THR-30 AND SER-32, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=29253589; DOI=10.1016/j.bbalip.2017.12.005;
RA Blunsom N.J., Gomez-Espinosa E., Ashlin T.G., Cockcroft S.;
RT "Mitochondrial CDP-diacylglycerol synthase activity is due to the
RT peripheral protein, TAMM41 and not due to the integral membrane protein,
RT CDP-diacylglycerol synthase 1.";
RL Biochim. Biophys. Acta 1863:284-298(2018).
CC -!- FUNCTION: Catalyzes the conversion of phosphatidic acid (PA) to CDP-
CC diacylglycerol (CDP-DAG), an essential intermediate in the synthesis of
CC phosphatidylglycerol, cardiolipin and phosphatidylinositol
CC (PubMed:29253589). Exhibits specificity for the nature of the acyl
CC chains at the sn-1 and sn-2 positions in the substrate, PA and the
CC preferred acyl chain composition is 1-stearoyl-2-arachidonoyl-sn-
CC phosphatidic acid (By similarity). Plays an important role in
CC regulating the growth and maturation of lipid droplets which are
CC storage organelles at the center of lipid and energy homeostasis (By
CC similarity). {ECO:0000250|UniProtKB:O95674,
CC ECO:0000269|PubMed:29253589}.
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 Evidence={ECO:0000269|PubMed:29253589};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16230;
CC Evidence={ECO:0000269|PubMed:29253589};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-octadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-
CC 3-phosphate + CTP + H(+) = 1-octadecanoyl-2-(5Z,8Z,11Z,14Z-
CC eicosatetraenoyl)-sn-glycero-3-cytidine-5'-diphosphate + diphosphate;
CC Xref=Rhea:RHEA:45648, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:37563, ChEBI:CHEBI:77091, ChEBI:CHEBI:85349;
CC Evidence={ECO:0000250|UniProtKB:O95674};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45649;
CC Evidence={ECO:0000250|UniProtKB:O95674};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-octadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-
CC phosphate + CTP + H(+) = 1-octadecanoyl-2-(9Z,12Z-octadecadienoyl)-
CC sn-glycero-3-cytidine-5'-diphosphate + diphosphate;
CC Xref=Rhea:RHEA:45660, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:37563, ChEBI:CHEBI:77098, ChEBI:CHEBI:85352;
CC Evidence={ECO:0000250|UniProtKB:O95674};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45661;
CC Evidence={ECO:0000250|UniProtKB:O95674};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-
CC 3-phosphate + CTP + H(+) = 1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-
CC eicosatetraenoyl)-sn-glycero-3-cytidine-5'-diphosphate + diphosphate;
CC Xref=Rhea:RHEA:45652, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:37563, ChEBI:CHEBI:72864, ChEBI:CHEBI:85350;
CC Evidence={ECO:0000250|UniProtKB:O95674};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45653;
CC Evidence={ECO:0000250|UniProtKB:O95674};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-di-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero-3-phosphate
CC + CTP + H(+) = 1,2-di-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-
CC cytidine-5'-diphosphate + diphosphate; Xref=Rhea:RHEA:45656,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37563,
CC ChEBI:CHEBI:77126, ChEBI:CHEBI:85351;
CC Evidence={ECO:0000250|UniProtKB:O95674};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45657;
CC Evidence={ECO:0000250|UniProtKB:O95674};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-octadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphate +
CC CTP + H(+) = 1-octadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-
CC cytidine-5'-diphosphate + diphosphate; Xref=Rhea:RHEA:45664,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37563,
CC ChEBI:CHEBI:74560, ChEBI:CHEBI:85353;
CC Evidence={ECO:0000250|UniProtKB:O95674};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45665;
CC Evidence={ECO:0000250|UniProtKB:O95674};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-octadecanoyl-2-(4Z,7Z,10Z,13Z,16Z,19Z-docosahexaenoyl)-sn-
CC glycero-3-phosphate + CTP + H(+) = 1-octadecanoyl-2-
CC (4Z,7Z,10Z,13Z,16Z,19Z-docosahexaenoyl)-sn-glycero-3-cytidine-5'-
CC diphosphate + diphosphate; Xref=Rhea:RHEA:45668, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:37563, ChEBI:CHEBI:77130,
CC ChEBI:CHEBI:85354; Evidence={ECO:0000250|UniProtKB:O95674};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45669;
CC Evidence={ECO:0000250|UniProtKB:O95674};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-di-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphate + CTP +
CC H(+) = 1,2-di-(9Z,12Z-octadecadienoyl)-sn-glycero-3-cytidine-5'-
CC diphosphate + diphosphate; Xref=Rhea:RHEA:45672, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:37563, ChEBI:CHEBI:77128,
CC ChEBI:CHEBI:85355; Evidence={ECO:0000250|UniProtKB:O95674};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45673;
CC Evidence={ECO:0000250|UniProtKB:O95674};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphate + CTP + H(+) =
CC 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-cytidine-5'-diphosphate +
CC diphosphate; Xref=Rhea:RHEA:45676, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:37563, ChEBI:CHEBI:74546,
CC ChEBI:CHEBI:85356; Evidence={ECO:0000250|UniProtKB:O95674};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45677;
CC Evidence={ECO:0000250|UniProtKB:O95674};
CC -!- PATHWAY: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-
CC diacylglycerol from sn-glycerol 3-phosphate: step 3/3.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:29253589}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:29253589}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the CDS family. {ECO:0000305}.
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DR EMBL; AB052898; BAB61043.1; -; mRNA.
DR RefSeq; NP_446095.1; NM_053643.1.
DR AlphaFoldDB; Q91XU8; -.
DR BioGRID; 250280; 1.
DR STRING; 10116.ENSRNOP00000028888; -.
DR iPTMnet; Q91XU8; -.
DR PhosphoSitePlus; Q91XU8; -.
DR SwissPalm; Q91XU8; -.
DR jPOST; Q91XU8; -.
DR PaxDb; Q91XU8; -.
DR PRIDE; Q91XU8; -.
DR GeneID; 114101; -.
DR KEGG; rno:114101; -.
DR UCSC; RGD:621186; rat.
DR CTD; 8760; -.
DR RGD; 621186; Cds2.
DR eggNOG; KOG1440; Eukaryota.
DR InParanoid; Q91XU8; -.
DR OrthoDB; 1072976at2759; -.
DR PhylomeDB; Q91XU8; -.
DR Reactome; R-RNO-1483148; Synthesis of PG.
DR UniPathway; UPA00557; UER00614.
DR PRO; PR:Q91XU8; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IDA:UniProtKB.
DR GO; GO:0004605; F:phosphatidate cytidylyltransferase activity; IDA:UniProtKB.
DR GO; GO:0016024; P:CDP-diacylglycerol biosynthetic process; ISS:UniProtKB.
DR GO; GO:0140042; P:lipid droplet formation; ISS:UniProtKB.
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 1: Evidence at protein level;
KW Endoplasmic reticulum; Lipid biosynthesis; Lipid metabolism; Membrane;
KW Nucleotidyltransferase; Phospholipid biosynthesis; Phospholipid metabolism;
KW Phosphoprotein; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..443
FT /note="Phosphatidate cytidylyltransferase 2"
FT /id="PRO_0000090718"
FT TRANSMEM 78..98
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 129..149
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 165..185
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 212..232
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 261..281
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 338..358
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..34
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 20
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 30
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 32
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 34
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95674"
FT MOD_RES 36
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95674"
FT MOD_RES 50
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q99L43"
SQ SEQUENCE 443 AA; 51323 MW; 5CA23C56AE2B043F CRC64;
MTELRQRAVR EDAPPEDKES ESEAKLDGET ASDSESRAET APPPTSIDDT PEVLNRALSN
LSSRWKNWWV RGILTMAMIA FFFIIIYLGP MVLMMIVMCV QIKCFHEIIT IGYNVYHSYD
LPWFRTLSWY FLLCVNYFFY GETVTDYFFT LVQREEPLRI LSKYHRFISF TLYLTGFCMF
VLSLVKKHYR LQFYMFGWTH VTLLIVVTQS HLVIHNLFEG MIWFIVPISC VICNDIMAYM
FGFFFGRTPL IKLSPKKTWE GFIGGFFATV VFGLLLSYVM SGYRCFVCPV EYNNDTNSFT
VDCEPSDLFR LQEYNIPGVI QSLVGWKTMR MYPFQIHSAL STFASLIGPF GGFFASGFKR
AFKIKDFANT IPGHGGIMDR FDCQYLMATF VNVYIASFIR GPNPSKLIQQ FLTLRPDQQL
HIFNTLKSHL TDKGILMSAL EEE
