ID CDS2_HUMAN Reviewed; 445 AA. AC O95674; B2RDC6; D3DW04; Q5TDY2; Q5TDY3; Q5TDY4; Q5TDY5; Q9BYK5; Q9NTT2; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1999, sequence version 1. DT 24-JAN-2024, entry version 186. DE RecName: Full=Phosphatidate cytidylyltransferase 2 {ECO:0000305}; DE EC=2.7.7.41 {ECO:0000269|PubMed:25375833}; 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|HGNC:HGNC:1801}; 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] (ISOFORM 1), TISSUE SPECIFICITY, AND RP 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 [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). 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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=11780052; DOI=10.1038/414865a; RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.; RT "The DNA sequence and comparative analysis of human chromosome 20."; RL Nature 414:865-871(2001). RN [4] 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 (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Brain; 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 [6] RP NUCLEOTIDE SEQUENCE [MRNA] OF 25-445 (ISOFORM 1). 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 [7] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling RT networks."; RL Cell 127:635-648(2006). RN [8] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Platelet; RX PubMed=18088087; DOI=10.1021/pr0704130; RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., RA Schuetz C., Walter U., Gambaryan S., Sickmann A.; RT "Phosphoproteome of resting human platelets."; RL J. Proteome Res. 7:526-534(2008). RN [9] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007; RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., RA Greff Z., Keri G., Stemmann O., Mann M.; RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the RT kinome across the cell cycle."; RL Mol. Cell 31:438-448(2008). RN [10] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [11] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=18318008; DOI=10.1002/pmic.200700884; RA Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., RA Zou H., Gu J.; RT "Large-scale phosphoproteome analysis of human liver tissue by enrichment RT and fractionation of phosphopeptides with strong anion exchange RT chromatography."; RL Proteomics 8:1346-1361(2008). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [13] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21; SER-33 AND SER-35, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-31 AND SER-33, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [17] 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 [18] 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 [19] 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). 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:25375833). 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 (PubMed:25375833). 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 CC (PubMed:26946540, PubMed:31548309). {ECO:0000269|PubMed:25375833, CC ECO:0000269|PubMed:26946540, ECO:0000269|PubMed:31548309}. 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:25375833}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16230; CC Evidence={ECO:0000305|PubMed:25375833}; 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 -!- ACTIVITY REGULATION: Inhibited by its anionic phospholipid end CC products, with phosphatidylinositol-(4,5)- bisphosphate (PIP2) showing CC the strongest inhibition. Inhibition is also acyl chain specific, with CC 1-stearoyl-2-arachidonoyl-snphosphatidylinositol showing the strongest CC inhibition. {ECO:0000269|PubMed:25375833}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=1.4 uM for 1-stearoyl-2-arachidonoyl-sn-phosphatidic acid CC {ECO:0000269|PubMed:25375833}; CC KM=0.9 uM for 1-stearoyl-2-linoleoyl-sn-phosphatidic acid CC {ECO:0000269|PubMed:25375833}; CC Vmax=9.3 umol/min/mg enzyme for CC 1-stearoyl-2-arachidonoyl-sn-phosphatidic acid CC {ECO:0000269|PubMed:25375833}; CC Vmax=3.5 umol/min/mg enzyme for CC 1-stearoyl-2-linoleoyl-sn-phosphatidic acid CC {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. {ECO:0000250|UniProtKB:Q91XU8}. CC -!- INTERACTION: CC O95674; Q92870-2: APBB2; NbExp=3; IntAct=EBI-3913685, EBI-21535880; CC O95674; P55212: CASP6; NbExp=3; IntAct=EBI-3913685, EBI-718729; CC O95674; P28329-3: CHAT; NbExp=3; IntAct=EBI-3913685, EBI-25837549; CC O95674; Q7Z7G2: CPLX4; NbExp=3; IntAct=EBI-3913685, EBI-18013275; CC O95674; G5E9A7: DMWD; NbExp=3; IntAct=EBI-3913685, EBI-10976677; CC O95674; Q9Y282: ERGIC3; NbExp=3; IntAct=EBI-3913685, EBI-781551; CC O95674; Q5JX71: FAM209A; NbExp=3; IntAct=EBI-3913685, EBI-18304435; CC O95674; P22607: FGFR3; NbExp=4; IntAct=EBI-3913685, EBI-348399; CC O95674; Q8TDT2: GPR152; NbExp=3; IntAct=EBI-3913685, EBI-13345167; CC O95674; Q8TED1: GPX8; NbExp=3; IntAct=EBI-3913685, EBI-11721746; CC O95674; Q14957: GRIN2C; NbExp=3; IntAct=EBI-3913685, EBI-8285963; CC O95674; P06396: GSN; NbExp=3; IntAct=EBI-3913685, EBI-351506; CC O95674; P31937: HIBADH; NbExp=3; IntAct=EBI-3913685, EBI-11427100; CC O95674; P01112: HRAS; NbExp=3; IntAct=EBI-3913685, EBI-350145; CC O95674; P42858: HTT; NbExp=9; IntAct=EBI-3913685, EBI-466029; CC O95674; Q13651: IL10RA; NbExp=3; IntAct=EBI-3913685, EBI-1031656; CC O95674; Q96MG2: JSRP1; NbExp=3; IntAct=EBI-3913685, EBI-11305455; CC O95674; P13473-2: LAMP2; NbExp=3; IntAct=EBI-3913685, EBI-21591415; CC O95674; A8MZ59: LEUTX; NbExp=3; IntAct=EBI-3913685, EBI-17490413; CC O95674; Q8TAF8: LHFPL5; NbExp=3; IntAct=EBI-3913685, EBI-2820517; CC O95674; Q95460-2: MR1; NbExp=3; IntAct=EBI-3913685, EBI-12201447; CC O95674; Q9H2K0: MTIF3; NbExp=3; IntAct=EBI-3913685, EBI-3923617; CC O95674; Q9HB07: MYG1; NbExp=3; IntAct=EBI-3913685, EBI-709754; CC O95674; O75400-2: PRPF40A; NbExp=3; IntAct=EBI-3913685, EBI-5280197; CC O95674; P62826: RAN; NbExp=3; IntAct=EBI-3913685, EBI-286642; CC O95674; Q9H9V4: RNF122; NbExp=3; IntAct=EBI-3913685, EBI-2129998; CC O95674; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-3913685, EBI-5235340; CC O95674; Q8WWF3: SSMEM1; NbExp=3; IntAct=EBI-3913685, EBI-17280858; CC O95674; P31948: STIP1; NbExp=3; IntAct=EBI-3913685, EBI-1054052; CC O95674; Q9NPL8: TIMMDC1; NbExp=3; IntAct=EBI-3913685, EBI-6268651; CC O95674; Q8IV31: TMEM139; NbExp=3; IntAct=EBI-3913685, EBI-7238458; CC O95674; Q96B21: TMEM45B; NbExp=3; IntAct=EBI-3913685, EBI-3923061; CC O95674; Q9Y320: TMX2; NbExp=3; IntAct=EBI-3913685, EBI-6447886; CC O95674; Q86WV8: TSC1; NbExp=3; IntAct=EBI-3913685, EBI-12806590; CC O95674; O95859: TSPAN12; NbExp=3; IntAct=EBI-3913685, EBI-2466403; CC O95674; Q9UMX0: UBQLN1; NbExp=3; IntAct=EBI-3913685, EBI-741480; CC O95674; Q9Y649; NbExp=3; IntAct=EBI-3913685, EBI-25900580; 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 -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=O95674-1; Sequence=Displayed; CC Name=2; CC IsoId=O95674-2; Sequence=VSP_015477, VSP_015480, VSP_015482; CC -!- TISSUE SPECIFICITY: Widely expressed. Expressed in heart, brain and CC retina, and to a lesser extent in placenta, lung, liver, skeletal CC muscle, kidney and pancreas. {ECO:0000269|PubMed:9889000}. CC -!- DEVELOPMENTAL STAGE: No expression detected at 10.5 dpc in the CC developing brain. At 12.5 dpc, expression is detected in the developing CC sentral nervous system and peripheral nervous system. At 17.5 dpc, high CC levels of expression are detected in a number of sites, including the CC dorsal root ganglia of the peripheral nervous system and the ganglion CC cell layer of the neural retina in the developing eye. At this stage, CC expression in the brain is restricted to the ventricular zone of the CC telencephalon, in particular in the basal ganglia and the cerebral CC cortex. {ECO:0000269|PubMed:9889000}. CC -!- SIMILARITY: Belongs to the CDS family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; Y16521; CAA76270.1; -; mRNA. DR EMBL; AK315489; BAG37873.1; -; mRNA. DR EMBL; AL121755; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL121924; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471133; EAX10424.1; -; Genomic_DNA. DR EMBL; CH471133; EAX10426.1; -; Genomic_DNA. DR EMBL; BC025751; AAH25751.1; -; mRNA. DR EMBL; AF069532; AAC78305.1; -; mRNA. DR CCDS; CCDS13088.1; -. [O95674-1] DR RefSeq; NP_003809.1; NM_003818.3. [O95674-1] DR AlphaFoldDB; O95674; -. DR BioGRID; 114295; 150. DR IntAct; O95674; 61. DR MINT; O95674; -. DR STRING; 9606.ENSP00000419879; -. DR SwissLipids; SLP:000001138; -. DR GlyCosmos; O95674; 1 site, 2 glycans. DR GlyGen; O95674; 2 sites, 2 N-linked glycans (1 site), 1 O-linked glycan (1 site). DR iPTMnet; O95674; -. DR PhosphoSitePlus; O95674; -. DR SwissPalm; O95674; -. DR BioMuta; CDS2; -. DR EPD; O95674; -. DR jPOST; O95674; -. DR MassIVE; O95674; -. DR MaxQB; O95674; -. DR PaxDb; 9606-ENSP00000419879; -. DR PeptideAtlas; O95674; -. DR ProteomicsDB; 50988; -. [O95674-1] DR Pumba; O95674; -. DR Antibodypedia; 8142; 163 antibodies from 23 providers. DR DNASU; 8760; -. DR Ensembl; ENST00000450570.1; ENSP00000403205.1; ENSG00000101290.14. [O95674-2] DR Ensembl; ENST00000460006.6; ENSP00000419879.1; ENSG00000101290.14. [O95674-1] DR GeneID; 8760; -. DR KEGG; hsa:8760; -. DR MANE-Select; ENST00000460006.6; ENSP00000419879.1; NM_003818.4; NP_003809.1. DR UCSC; uc002wls.4; human. [O95674-1] DR AGR; HGNC:1801; -. DR CTD; 8760; -. DR DisGeNET; 8760; -. DR GeneCards; CDS2; -. DR HGNC; HGNC:1801; CDS2. DR HPA; ENSG00000101290; Low tissue specificity. DR MIM; 603549; gene. DR neXtProt; NX_O95674; -. DR OpenTargets; ENSG00000101290; -. DR PharmGKB; PA26347; -. DR VEuPathDB; HostDB:ENSG00000101290; -. DR eggNOG; KOG1440; Eukaryota. DR GeneTree; ENSGT00940000158877; -. DR HOGENOM; CLU_023471_0_1_1; -. DR InParanoid; O95674; -. DR OMA; MPIQWHA; -. DR OrthoDB; 5481516at2759; -. DR PhylomeDB; O95674; -. DR TreeFam; TF313464; -. DR BRENDA; 2.7.7.41; 2681. DR PathwayCommons; O95674; -. DR Reactome; R-HSA-1483148; Synthesis of PG. DR SignaLink; O95674; -. DR SIGNOR; O95674; -. DR UniPathway; UPA00557; UER00614. DR BioGRID-ORCS; 8760; 184 hits in 1166 CRISPR screens. DR ChiTaRS; CDS2; human. DR GeneWiki; CDS2; -. DR GenomeRNAi; 8760; -. DR Pharos; O95674; Tbio. DR PRO; PR:O95674; -. DR Proteomes; UP000005640; Chromosome 20. DR RNAct; O95674; Protein. DR Bgee; ENSG00000101290; Expressed in lateral nuclear group of thalamus and 212 other cell types or tissues. DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0005743; C:mitochondrial inner membrane; TAS:Reactome. 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:0006655; P:phosphatidylglycerol biosynthetic process; TAS:Reactome. DR InterPro; IPR000374; PC_trans. DR InterPro; IPR016720; PC_Trfase_euk. DR PANTHER; PTHR13773; PHOSPHATIDATE CYTIDYLYLTRANSFERASE; 1. DR PANTHER; PTHR13773:SF4; PHOSPHATIDATE CYTIDYLYLTRANSFERASE 2; 1. DR Pfam; PF01148; CTP_transf_1; 1. DR PIRSF; PIRSF018269; PC_trans_euk; 1. DR PROSITE; PS01315; CDS; 1. DR Genevisible; O95674; HS. PE 1: Evidence at protein level; KW Alternative splicing; Endoplasmic reticulum; Lipid biosynthesis; KW Lipid metabolism; Membrane; Nucleotidyltransferase; KW Phospholipid biosynthesis; Phospholipid metabolism; Phosphoprotein; KW Reference proteome; Transferase; Transmembrane; Transmembrane helix. FT CHAIN 1..445 FT /note="Phosphatidate cytidylyltransferase 2" FT /id="PRO_0000090716" FT TRANSMEM 79..99 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 132..152 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 166..186 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 213..233 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 262..282 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 340..360 FT /note="Helical" FT /evidence="ECO:0000255" FT REGION 1..49 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1..35 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 21 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT MOD_RES 31 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 33 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:24275569" FT MOD_RES 35 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692" FT MOD_RES 37 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332" FT MOD_RES 51 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q99L43" FT VAR_SEQ 1..55 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000305" FT /id="VSP_015477" FT VAR_SEQ 56..64 FT /note="NRALSNLSS -> MSRLRHPRT (in isoform 2)" FT /evidence="ECO:0000305" FT /id="VSP_015480" FT VAR_SEQ 306..445 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000305" FT /id="VSP_015482" SQ SEQUENCE 445 AA; 51418 MW; 7DAD6A3C1D5587D6 CRC64; MTELRQRVAH EPVAPPEDKE SESEAKVDGE TASDSESRAE SAPLPVSADD TPEVLNRALS NLSSRWKNWW VRGILTLAMI AFFFIIIYLG PMVLMIIVMC VQIKCFHEII TIGYNVYHSY DLPWFRTLSW YFLLCVNYFF YGETVTDYFF TLVQREEPLR ILSKYHRFIS FTLYLIGFCM FVLSLVKKHY RLQFYMFGWT HVTLLIVVTQ SHLVIHNLFE GMIWFIVPIS CVICNDIMAY MFGFFFGRTP LIKLSPKKTW EGFIGGFFAT VVFGLLLSYV MSGYRCFVCP VEYNNDTNSF TVDCEPSDLF RLQEYNIPGV IQSVIGWKTV RMYPFQIHSI ALSTFASLIG PFGGFFASGF KRAFKIKDFA NTIPGHGGIM DRFDCQYLMA TFVNVYIASF IRGPNPSKLI QQFLTLRPDQ QLHIFNTLRS HLIDKGMLTS TTEDE //