ID   CDS1_HUMAN              Reviewed;         461 AA.
AC   Q92903; B2RAL5; O00163;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1998, sequence version 2.
DT   24-JAN-2024, entry version 175.
DE   RecName: Full=Phosphatidate cytidylyltransferase 1 {ECO:0000305};
DE            EC=2.7.7.41 {ECO:0000269|PubMed:9407135};
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|HGNC:HGNC:1800}; Synonyms=CDS;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Neuron;
RX   PubMed=8863531; DOI=10.1046/j.1471-4159.1996.67052200.x;
RA   Heacock A.M., Uhler M.D., Agranoff B.W.;
RT   "Cloning of CDP-diacylglycerol synthase from a human neuronal cell line.";
RL   J. Neurochem. 67:2200-2203(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Leukocyte, and Placenta;
RX   PubMed=9115637; DOI=10.1089/dna.1997.16.281;
RA   Weeks R., Dowhan W., Shen H., Balantac N., Meengs B., Nudelman E.,
RA   Leung D.W.;
RT   "Isolation and expression of an isoform of human CDP-diacylglycerol
RT   synthase cDNA.";
RL   DNA Cell Biol. 16:281-289(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND TISSUE
RP   SPECIFICITY.
RC   TISSUE=Placenta;
RX   PubMed=9407135; DOI=10.1074/jbc.272.52.33402;
RA   Lykidis A., Jackson P.D., Rock C.O., Jackowski S.;
RT   "The role of CDP-diacylglycerol synthetase and phosphatidylinositol
RT   synthase activity levels in the regulation of cellular phosphatidylinositol
RT   content.";
RL   J. Biol. Chem. 272:33402-33409(1997).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Retina;
RX   PubMed=9806839; DOI=10.1006/geno.1998.5547;
RA   Halford S., Dulai K.S., Daw S.C.M., Fitzgibbon J., Hunt D.M.;
RT   "Isolation and chromosomal localization of two human CDP-diacylglycerol
RT   synthase (CDS) genes.";
RL   Genomics 54:140-144(1998).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Ovary;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Lung;
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   [8]
RP   FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, BIOPHYSICOCHEMICAL
RP   PROPERTIES, AND ACTIVITY REGULATION.
RX   PubMed=25375833; DOI=10.1021/bi501250m;
RA   D'Souza K., Kim Y.J., Balla T., Epand R.M.;
RT   "Distinct properties of the two isoforms of CDP-diacylglycerol synthase.";
RL   Biochemistry 53:7358-7367(2014).
RN   [9]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
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   [10]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=31548309; DOI=10.1074/jbc.ra119.009992;
RA   Xu Y., Mak H.Y., Lukmantara I., Li Y.E., Hoehn K.L., Huang X., Du X.,
RA   Yang H.;
RT   "CDP-DAG synthase 1 and 2 regulate lipid droplet growth through distinct
RT   mechanisms.";
RL   J. Biol. Chem. 294:16740-16755(2019).
RN   [11]
RP   VARIANT [LARGE SCALE ANALYSIS] THR-204.
RX   PubMed=16959974; DOI=10.1126/science.1133427;
RA   Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA   Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA   Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA   Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA   Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA   Velculescu V.E.;
RT   "The consensus coding sequences of human breast and colorectal cancers.";
RL   Science 314:268-274(2006).
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:9407135, PubMed:25375833). Exhibits almost no acyl chain
CC       preference for PA, showing no discrimination for the sn-1/sn-2 acyl
CC       chain composition of PAs (PubMed:25375833). Plays an important role in
CC       regulating the growth of lipid droplets which are storage organelles at
CC       the center of lipid and energy homeostasis (PubMed:26946540,
CC       PubMed:31548309). Positively regulates the differentiation and
CC       development of adipocytes (By similarity).
CC       {ECO:0000250|UniProtKB:P98191, ECO:0000269|PubMed:25375833,
CC       ECO:0000269|PubMed:26946540, ECO:0000269|PubMed:31548309,
CC       ECO:0000269|PubMed:9407135}.
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:9407135};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16230;
CC         Evidence={ECO:0000305|PubMed:9407135};
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:0000269|PubMed:25375833};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45649;
CC         Evidence={ECO:0000305|PubMed:25375833};
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:0000269|PubMed:25375833};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45661;
CC         Evidence={ECO:0000305|PubMed:25375833};
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:0000269|PubMed:25375833};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45653;
CC         Evidence={ECO:0000305|PubMed:25375833};
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:0000269|PubMed:25375833};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45657;
CC         Evidence={ECO:0000305|PubMed:25375833};
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:0000269|PubMed:25375833};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45665;
CC         Evidence={ECO:0000305|PubMed:25375833};
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:0000269|PubMed:25375833};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45669;
CC         Evidence={ECO:0000305|PubMed:25375833};
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:0000269|PubMed:25375833};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45673;
CC         Evidence={ECO:0000305|PubMed:25375833};
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:0000269|PubMed:25375833};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45677;
CC         Evidence={ECO:0000305|PubMed:25375833};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:O35052};
CC   -!- ACTIVITY REGULATION: Inhibited by its anionic phospholipid end
CC       products, with phosphatidylinositol-(4,5)- bisphosphate showing the
CC       strongest inhibition. {ECO:0000269|PubMed:25375833}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.8 uM for 1-stearoyl-2-arachidonoyl-sn-phosphatidic acid
CC         {ECO:0000269|PubMed:25375833};
CC         KM=0.6 uM for 1-stearoyl-2-linoleoyl-sn-phosphatidic acid
CC         {ECO:0000269|PubMed:25375833};
CC         Vmax=3.3 umol/min/mg enzyme for 1-stearoyl-2-arachidonoyl-sn-
CC         phosphatidic acid {ECO:0000269|PubMed:25375833};
CC         Vmax=3.6 umol/min/mg enzyme for 1-stearoyl-2-linoleoyl-sn-
CC         phosphatidic acid {ECO:0000269|PubMed:25375833};
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 (By similarity).
CC       {ECO:0000250|UniProtKB:O35052, ECO:0000250|UniProtKB:P98191}.
CC   -!- INTERACTION:
CC       Q92903; Q5JX71: FAM209A; NbExp=3; IntAct=EBI-13295305, EBI-18304435;
CC       Q92903; Q86VR2: RETREG3; NbExp=3; IntAct=EBI-13295305, EBI-10192441;
CC       Q92903; Q3KNW5: SLC10A6; NbExp=3; IntAct=EBI-13295305, EBI-18159983;
CC       Q92903; Q9UKG4: SLC13A4; NbExp=3; IntAct=EBI-13295305, EBI-12808018;
CC       Q92903; Q96Q45-2: TMEM237; NbExp=3; IntAct=EBI-13295305, EBI-10982110;
CC       Q92903; Q9Y385: UBE2J1; NbExp=3; IntAct=EBI-13295305, EBI-988826;
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000269|PubMed:25375833, ECO:0000269|PubMed:26946540,
CC       ECO:0000269|PubMed:31548309}; Multi-pass membrane protein
CC       {ECO:0000255}.
CC   -!- TISSUE SPECIFICITY: Expressed in adult tissues such as placenta, brain,
CC       small intestine, ovary, testis and prostate. Highly expressed in fetal
CC       kidney, lung and brain. Lower level in fetal liver.
CC       {ECO:0000269|PubMed:9407135}.
CC   -!- SIMILARITY: Belongs to the CDS family. {ECO:0000305}.
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DR   EMBL; U65887; AAC50735.1; -; mRNA.
DR   EMBL; U60808; AAC51184.1; -; mRNA.
DR   EMBL; AK314245; BAG36912.1; -; mRNA.
DR   EMBL; CH471057; EAX05950.1; -; Genomic_DNA.
DR   EMBL; BC074833; AAH74833.1; -; mRNA.
DR   EMBL; BC074881; AAH74881.1; -; mRNA.
DR   CCDS; CCDS3608.1; -.
DR   RefSeq; NP_001254.2; NM_001263.3.
DR   AlphaFoldDB; Q92903; -.
DR   BioGRID; 107471; 58.
DR   CORUM; Q92903; -.
DR   IntAct; Q92903; 18.
DR   STRING; 9606.ENSP00000295887; -.
DR   SwissLipids; SLP:000000532; -.
DR   iPTMnet; Q92903; -.
DR   PhosphoSitePlus; Q92903; -.
DR   SwissPalm; Q92903; -.
DR   BioMuta; CDS1; -.
DR   DMDM; 3123204; -.
DR   EPD; Q92903; -.
DR   jPOST; Q92903; -.
DR   MassIVE; Q92903; -.
DR   MaxQB; Q92903; -.
DR   PaxDb; 9606-ENSP00000295887; -.
DR   PeptideAtlas; Q92903; -.
DR   ProteomicsDB; 75588; -.
DR   Antibodypedia; 25245; 101 antibodies from 21 providers.
DR   DNASU; 1040; -.
DR   Ensembl; ENST00000295887.6; ENSP00000295887.5; ENSG00000163624.6.
DR   GeneID; 1040; -.
DR   KEGG; hsa:1040; -.
DR   MANE-Select; ENST00000295887.6; ENSP00000295887.5; NM_001263.4; NP_001254.2.
DR   UCSC; uc011ccv.3; human.
DR   AGR; HGNC:1800; -.
DR   CTD; 1040; -.
DR   DisGeNET; 1040; -.
DR   GeneCards; CDS1; -.
DR   HGNC; HGNC:1800; CDS1.
DR   HPA; ENSG00000163624; Low tissue specificity.
DR   MIM; 603548; gene.
DR   neXtProt; NX_Q92903; -.
DR   OpenTargets; ENSG00000163624; -.
DR   PharmGKB; PA26346; -.
DR   VEuPathDB; HostDB:ENSG00000163624; -.
DR   eggNOG; KOG1440; Eukaryota.
DR   GeneTree; ENSGT00940000158223; -.
DR   HOGENOM; CLU_023471_0_1_1; -.
DR   InParanoid; Q92903; -.
DR   OMA; FFAYMYF; -.
DR   OrthoDB; 5481516at2759; -.
DR   PhylomeDB; Q92903; -.
DR   TreeFam; TF313464; -.
DR   BRENDA; 2.7.7.41; 2681.
DR   PathwayCommons; Q92903; -.
DR   Reactome; R-HSA-1483226; Synthesis of PI.
DR   SignaLink; Q92903; -.
DR   SIGNOR; Q92903; -.
DR   UniPathway; UPA00557; UER00614.
DR   BioGRID-ORCS; 1040; 14 hits in 1153 CRISPR screens.
DR   ChiTaRS; CDS1; human.
DR   GeneWiki; CDS1_(gene); -.
DR   GenomeRNAi; 1040; -.
DR   Pharos; Q92903; Tbio.
DR   PRO; PR:Q92903; -.
DR   Proteomes; UP000005640; Chromosome 4.
DR   RNAct; Q92903; Protein.
DR   Bgee; ENSG00000163624; Expressed in bronchial epithelial cell and 184 other cell types or tissues.
DR   ExpressionAtlas; Q92903; baseline and differential.
DR   Genevisible; Q92903; HS.
DR   GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR   GO; GO:0016020; C:membrane; ISS:UniProtKB.
DR   GO; GO:0004142; F:diacylglycerol cholinephosphotransferase activity; NAS:UniProtKB.
DR   GO; GO:0004605; F:phosphatidate cytidylyltransferase activity; IDA:UniProtKB.
DR   GO; GO:0016024; P:CDP-diacylglycerol biosynthetic process; IDA:UniProtKB.
DR   GO; GO:0140042; P:lipid droplet formation; IMP:UniProtKB.
DR   GO; GO:0006661; P:phosphatidylinositol biosynthetic process; IDA:UniProtKB.
DR   GO; GO:0007602; P:phototransduction; NAS:UniProtKB.
DR   GO; GO:0045600; P:positive regulation of fat cell differentiation; ISS:UniProtKB.
DR   GO; GO:0007165; P:signal transduction; NAS: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_0000090713"
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..67
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        18..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:0000250|UniProtKB:P98191"
FT   MOD_RES         35
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O35052"
FT   MOD_RES         37
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P98191"
FT   VARIANT         99
FT                   /note="L -> F (in dbSNP:rs36068434)"
FT                   /id="VAR_048736"
FT   VARIANT         204
FT                   /note="K -> T (in a breast cancer sample; somatic
FT                   mutation)"
FT                   /evidence="ECO:0000269|PubMed:16959974"
FT                   /id="VAR_036129"
FT   CONFLICT        444..461
FT                   /note="TLKTHLIEKGILQPTLKV -> P (in Ref. 1; AAC50735)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   461 AA;  53304 MW;  E9D761BA285A5AB1 CRC64;
     MLELRHRGSC PGPREAVSPP HREGEAAGGD HETESTSDKE TDIDDRYGDL DSRTDSDIPE
     IPPSSDRTPE ILKKALSGLS SRWKNWWIRG ILTLTMISLF FLIIYMGSFM LMLLVLGIQV
     KCFHEIITIG YRVYHSYDLP WFRTLSWYFL LCVNYFFYGE TVADYFATFV QREEQLQFLI
     RYHRFISFAL YLAGFCMFVL SLVKKHYRLQ FYMFAWTHVT LLITVTQSHL VIQNLFEGMI
     WFLVPISSVI CNDITAYLFG FFFGRTPLIK LSPKKTWEGF IGGFFSTVVF GFIAAYVLSK
     YQYFVCPVEY RSDVNSFVTE CEPSELFQLQ TYSLPPFLKA VLRQERVSLY PFQIHSIALS
     TFASLIGPFG GFFASGFKRA FKIKDFANTI PGHGGIMDRF DCQYLMATFV HVYITSFIRG
     PNPSKVLQQL LVLQPEQQLN IYKTLKTHLI EKGILQPTLK V
//