CDS1_MOUSE
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 03-AUG-2022, entry version 148.
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_173370.3.
DR AlphaFoldDB; P98191; -.
DR STRING; 10090.ENSMUSP00000031273; -.
DR iPTMnet; P98191; -.
DR PhosphoSitePlus; P98191; -.
DR MaxQB; P98191; -.
DR PaxDb; P98191; -.
DR PeptideAtlas; P98191; -.
DR PRIDE; P98191; -.
DR ProteomicsDB; 283871; -.
DR Antibodypedia; 25245; 96 antibodies from 21 providers.
DR DNASU; 74596; -.
DR Ensembl; ENSMUST00000031273; ENSMUSP00000031273; ENSMUSG00000029330.
DR GeneID; 74596; -.
DR KEGG; mmu:74596; -.
DR UCSC; uc008yio.1; mouse.
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; FIMNNIF; -.
DR OrthoDB; 1072976at2759; -.
DR PhylomeDB; P98191; -.
DR TreeFam; TF313464; -.
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 75 CRISPR screens.
DR ChiTaRS; Cds1; mouse.
DR PRO; PR:P98191; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; P98191; protein.
DR Bgee; ENSMUSG00000029330; Expressed in urinary bladder urothelium and 224 other tissues.
DR Genevisible; P98191; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISO:MGI.
DR GO; GO:0016021; C:integral component of 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; 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; 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 25..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
