ID   CDS1_MOUSE              Reviewed;         461 AA.
AC   P98191; Q8CGZ1;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2005, sequence version 2.
DT   02-SEP-2026, entry version 165.
DE   RecName: Full=Phosphatidate cytidylyltransferase 1 {ECO:0000305};
DE            EC=2.7.7.41 {ECO:0000250|UniProtKB:Q92903};
DE   AltName: Full=CDP-DAG synthase 1;
DE   AltName: Full=CDP-DG synthase 1;
DE   AltName: Full=CDP-diacylglycerol synthase 1;
DE            Short=CDS 1;
DE   AltName: Full=CDP-diglyceride pyrophosphorylase 1;
DE   AltName: Full=CDP-diglyceride synthase 1;
DE   AltName: Full=CTP:phosphatidate cytidylyltransferase 1;
GN   Name=Cds1 {ECO:0000312|MGI:MGI:1921846}; Synonyms=Cds;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC   STRAIN=C57BL/6J;
RX   PubMed=16023307; DOI=10.1016/j.gene.2005.04.037;
RA   Inglis-Broadgate S.L., Ocaka L., Banerjee R., Gaasenbeek M., Chapple J.P.,
RA   Cheetham M.E., Clark B.J., Hunt D.M., Halford S.;
RT   "Isolation and characterization of murine Cds (CDP-diacylglycerol synthase)
RT   1 and 2.";
RL   Gene 356:19-31(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   PubMed=9889000; DOI=10.1006/geno.1998.5610;
RA   Volta M., Bulfone A., Gattuso C., Rossi E., Mariani M., Consalez G.G.,
RA   Zuffardi O., Ballabio A., Banfi S., Franco B.;
RT   "Identification and characterization of CDS2, a mammalian homolog of the
RT   Drosophila CDP-diacylglycerol synthase gene.";
RL   Genomics 55:68-77(1999).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Kidney, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [5]
RP   INTERACTION WITH FOS.
RX   PubMed=22105363; DOI=10.1038/onc.2011.510;
RA   Ferrero G.O., Velazquez F.N., Caputto B.L.;
RT   "The kinase c-Src and the phosphatase TC45 coordinately regulate c-Fos
RT   tyrosine phosphorylation and c-Fos phospholipid synthesis activation
RT   capacity.";
RL   Oncogene 31:3381-3391(2012).
RN   [6]
RP   FUNCTION.
RX   PubMed=26946540; DOI=10.1194/jlr.m060574;
RA   Qi Y., Kapterian T.S., Du X., Ma Q., Fei W., Zhang Y., Huang X.,
RA   Dawes I.W., Yang H.;
RT   "CDP-diacylglycerol synthases regulate the growth of lipid droplets and
RT   adipocyte development.";
RL   J. Lipid Res. 57:767-780(2016).
RN   [7]
RP   METHYLATION [LARGE SCALE ANALYSIS] AT ARG-7, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain;
RX   PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA   Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA   Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA   Bedford M.T., Comb M.J.;
RT   "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT   methylation.";
RL   Mol. Cell. Proteomics 13:372-387(2014).
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 (By
CC       similarity). Exhibits almost no acyl chain preference for PA, showing
CC       no discrimination for the sn-1/sn-2 acyl chain composition of PAs (By
CC       similarity). Plays an important role in regulating the growth of lipid
CC       droplets which are storage organelles at the center of lipid and energy
CC       homeostasis (PubMed:26946540). Positively regulates the differentiation
CC       and development of adipocytes (PubMed:26946540).
CC       {ECO:0000250|UniProtKB:Q92903, ECO:0000269|PubMed:26946540}.
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:0000250|UniProtKB:Q92903};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16230;
CC         Evidence={ECO:0000250|UniProtKB:Q92903};
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:Q92903};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45649;
CC         Evidence={ECO:0000250|UniProtKB:Q92903};
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:Q92903};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45661;
CC         Evidence={ECO:0000250|UniProtKB:Q92903};
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:Q92903};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45653;
CC         Evidence={ECO:0000250|UniProtKB:Q92903};
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:Q92903};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45657;
CC         Evidence={ECO:0000250|UniProtKB:Q92903};
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:Q92903};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45665;
CC         Evidence={ECO:0000250|UniProtKB:Q92903};
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:Q92903};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45669;
CC         Evidence={ECO:0000250|UniProtKB:Q92903};
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:Q92903};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45673;
CC         Evidence={ECO:0000250|UniProtKB:Q92903};
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:Q92903};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45677;
CC         Evidence={ECO:0000250|UniProtKB:Q92903};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:O35052};
CC   -!- PATHWAY: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-
CC       diacylglycerol from sn-glycerol 3-phosphate: step 3/3.
CC   -!- SUBUNIT: Homodimer (By similarity). Interacts with FOS; this
CC       interaction may enhance catalytic activity (PubMed:22105363).
CC       {ECO:0000250|UniProtKB:O35052, ECO:0000269|PubMed:22105363}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000269|PubMed:16023307}; Multi-pass membrane protein
CC       {ECO:0000255}.
CC   -!- TISSUE SPECIFICITY: Expressed in adult brain, eye, smooth muscle and
CC       testis. Highly expressed in the inner segment of the photoreceptor
CC       layer of adult retina. {ECO:0000269|PubMed:16023307,
CC       ECO:0000269|PubMed:9889000}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in a structure probably corresponding to
CC       the thymic rudiment 12.5 dpc. No expression could be detected at
CC       earlier and later stages of embryonic development (10.5 dpc and 17.5
CC       dpc). {ECO:0000269|PubMed:9889000}.
CC   -!- SIMILARITY: Belongs to the CDS family. {ECO:0000305}.
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DR   EMBL; AF533367; AAO16167.2; -; mRNA.
DR   EMBL; BC055292; AAH55292.1; -; mRNA.
DR   CCDS; CCDS19472.1; -.
DR   RefSeq; NP_775546.2; NM_173370.4.
DR   AlphaFoldDB; P98191; -.
DR   SMR; P98191; -.
DR   FunCoup; P98191; 1963.
DR   STRING; 10090.ENSMUSP00000031273; -.
DR   GlyGen; P98191; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P98191; -.
DR   PhosphoSitePlus; P98191; -.
DR   SwissPalm; P98191; -.
DR   PaxDb; 10090-ENSMUSP00000031273; -.
DR   PeptideAtlas; P98191; -.
DR   ProteomicsDB; 283871; -.
DR   Antibodypedia; 25245; 86 antibodies from 22 providers.
DR   DNASU; 74596; -.
DR   Ensembl; ENSMUST00000031273.9; ENSMUSP00000031273.9; ENSMUSG00000029330.9.
DR   GeneID; 74596; -.
DR   KEGG; mmu:74596; -.
DR   UCSC; uc008yio.1; mouse.
DR   AGR; MGI:1921846; -.
DR   CTD; 1040; -.
DR   MGI; MGI:1921846; Cds1.
DR   VEuPathDB; HostDB:ENSMUSG00000029330; -.
DR   eggNOG; KOG1440; Eukaryota.
DR   GeneTree; ENSGT00940000158223; -.
DR   HOGENOM; CLU_023471_0_1_1; -.
DR   InParanoid; P98191; -.
DR   OMA; FFAYMYF; -.
DR   OrthoDB; 10260889at2759; -.
DR   PhylomeDB; P98191; -.
DR   BRENDA; 2.7.7.41; 3474.
DR   Reactome; R-MMU-1483226; Synthesis of PI.
DR   UniPathway; UPA00557; UER00614.
DR   BioGRID-ORCS; 74596; 3 hits in 80 CRISPR screens.
DR   PRO; PR:P98191; -.
DR   Proteomes; UP000000589; Chromosome 5.
DR   RNAct; P98191; protein.
DR   Bgee; ENSMUSG00000029330; Expressed in urinary bladder urothelium and 227 other cell types or tissues.
DR   GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; EXP:UniProtKB.
DR   GO; GO:0016020; C:membrane; ISS:UniProtKB.
DR   GO; GO:0004605; F:phosphatidate cytidylyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0016024; P:CDP-diacylglycerol biosynthetic process; ISS:UniProtKB.
DR   GO; GO:0140042; P:lipid droplet formation; IMP:UniProtKB.
DR   GO; GO:0006661; P:phosphatidylinositol biosynthetic process; ISS:UniProtKB.
DR   GO; GO:0045600; P:positive regulation of fat cell differentiation; IMP:UniProtKB.
DR   InterPro; IPR000374; PC_trans.
DR   InterPro; IPR016720; PC_Trfase_euk.
DR   PANTHER; PTHR13773; PHOSPHATIDATE CYTIDYLYLTRANSFERASE; 1.
DR   PANTHER; PTHR13773:SF16; PHOSPHATIDATE CYTIDYLYLTRANSFERASE 1; 1.
DR   Pfam; PF01148; CTP_transf_1; 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; Magnesium;
KW   Membrane; Methylation; Nucleotidyltransferase; Phospholipid biosynthesis;
KW   Phospholipid metabolism; Phosphoprotein; Reference proteome; Transferase;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..461
FT                   /note="Phosphatidate cytidylyltransferase 1"
FT                   /id="PRO_0000090714"
FT   TRANSMEM        96..116
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        149..169
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        183..203
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        230..250
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        279..299
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        357..377
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          1..68
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        22..56
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         7
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0007744|PubMed:24129315"
FT   MOD_RES         35
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O35052"
FT   MOD_RES         37
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
SQ   SEQUENCE   461 AA;  52875 MW;  B6AD0DB2124E0D71 CRC64;
     MLELRHRGGC PGPGGAGAPP PREGEAAGGD HETESTSDKE TDIDDRYGDL DARGDSDVPE
     VPPSSDRTPE ILKKALSGLS SRWKNWWIRG ILTLTMISLF FLIIYMGSFM LMLLVLGIQV
     KCFHEIITIG YRVYHSYDLP WFRTLSWYFL LCVNYFFYGE TVADYFATFV QREEQLQFLI
     RYHRFISFAL YLAGFCMFVL SLVKKHYRLQ FYMFAWTHVT LLITVTQSHL VIQNLFEGMI
     WFLVPISSVI CNDITAYLFG FFFGRTPLIK LSPKKTWEGF IGGFFSTVIF GFIAAYVLSK
     YQYFVCPVEY RSDVNSFVTE CEPSELFQLQ NYSLPPFLQA VLSRETVSLY PFQIHSIALS
     TFASLIGPFG GFFASGFKRA FKIKDFANTI PGHGGIMDRF DCQYLMATFV HVYITSFIRG
     PNPSKVLQQL LVLQPEQQLN IYRTLKIHLT EKGILQPTLK V
//