ID A2AMQ5_MOUSE Unreviewed; 427 AA. AC A2AMQ5; DT 20-FEB-2007, integrated into UniProtKB/TrEMBL. DT 20-FEB-2007, sequence version 1. DT 10-FEB-2021, entry version 99. DE RecName: Full=Phosphatidate cytidylyltransferase {ECO:0000256|ARBA:ARBA00012487, ECO:0000256|PIRNR:PIRNR018269, ECO:0000256|RuleBase:RU003938}; DE EC=2.7.7.41 {ECO:0000256|ARBA:ARBA00012487, ECO:0000256|PIRNR:PIRNR018269, ECO:0000256|RuleBase:RU003938}; GN Name=Cds2 {ECO:0000313|Ensembl:ENSMUSP00000086886, GN ECO:0000313|MGI:MGI:1332236}; 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 {ECO:0000313|Ensembl:ENSMUSP00000086886, ECO:0000313|Proteomes:UP000000589}; RN [1] {ECO:0000213|PubMed:17208939} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=17208939; DOI=10.1074/mcp.M600218-MCP200; RA Lee J., Xu Y., Chen Y., Sprung R., Kim S.C., Xie S., Zhao Y.; RT "Mitochondrial phosphoproteome revealed by an improved IMAC method and RT MS/MS/MS."; RL Mol. Cell. Proteomics 6:669-676(2007). RN [2] {ECO:0000213|PubMed:17242355} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=17242355; DOI=10.1073/pnas.0609836104; RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; RT "Large-scale phosphorylation analysis of mouse liver."; RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007). RN [3] {ECO:0000213|PubMed:18630941} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=18630941; DOI=10.1021/pr800223m; RA Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.; RT "Specific phosphopeptide enrichment with immobilized titanium ion affinity RT chromatography adsorbent for phosphoproteome analysis."; RL J. Proteome Res. 7:3957-3967(2008). RN [4] {ECO:0000213|PubMed:19144319} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006; RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M., RA Thibault P.; RT "The phagosomal proteome in interferon-gamma-activated macrophages."; RL Immunity 30:143-154(2009). RN [5] {ECO:0000313|Ensembl:ENSMUSP00000086886, ECO:0000313|Proteomes:UP000000589} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000086886, RC ECO:0000313|Proteomes:UP000000589}; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S., RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., RA Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of the RT mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [6] {ECO:0000213|PubMed:21183079} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. 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 [7] {ECO:0000313|Ensembl:ENSMUSP00000086886} RP IDENTIFICATION. RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000086886}; RG Ensembl; RL Submitted (FEB-2012) to UniProtKB. 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 {ECO:0000256|PIRNR:PIRNR018269}. 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:0000256|ARBA:ARBA00001021}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45657; CC Evidence={ECO:0000256|ARBA:ARBA00001021}; 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:0000256|ARBA:ARBA00001056}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45673; CC Evidence={ECO:0000256|ARBA:ARBA00001056}; 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:0000256|ARBA:ARBA00000060}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45677; CC Evidence={ECO:0000256|ARBA:ARBA00000060}; 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:0000256|ARBA:ARBA00001617}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45653; CC Evidence={ECO:0000256|ARBA:ARBA00001617}; 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:0000256|ARBA:ARBA00000281}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45669; CC Evidence={ECO:0000256|ARBA:ARBA00000281}; 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:0000256|ARBA:ARBA00001729}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45649; CC Evidence={ECO:0000256|ARBA:ARBA00001729}; 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:0000256|ARBA:ARBA00000515}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45661; CC Evidence={ECO:0000256|ARBA:ARBA00000515}; 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:0000256|ARBA:ARBA00000859}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45665; CC Evidence={ECO:0000256|ARBA:ARBA00000859}; 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:0000256|PIRNR:PIRNR018269, CC ECO:0000256|RuleBase:RU003938}; CC -!- PATHWAY: Lipid metabolism. {ECO:0000256|ARBA:ARBA00005189}. CC -!- PATHWAY: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP- CC diacylglycerol from sn-glycerol 3-phosphate: step 3/3. CC {ECO:0000256|ARBA:ARBA00005119, ECO:0000256|PIRNR:PIRNR018269, CC ECO:0000256|RuleBase:RU003938}. CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi- CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. CC -!- SIMILARITY: Belongs to the CDS family. {ECO:0000256|ARBA:ARBA00010185, CC ECO:0000256|PIRNR:PIRNR018269, ECO:0000256|RuleBase:RU003938}. 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; AL807793; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR RefSeq; NP_001277968.1; NM_001291039.1. DR jPOST; A2AMQ5; -. DR MaxQB; A2AMQ5; -. DR PeptideAtlas; A2AMQ5; -. DR PRIDE; A2AMQ5; -. DR Antibodypedia; 8142; 140 antibodies. DR Ensembl; ENSMUST00000089461; ENSMUSP00000086886; ENSMUSG00000058793. DR GeneID; 110911; -. DR UCSC; uc029ueu.2; mouse. DR CTD; 8760; -. DR MGI; MGI:1332236; Cds2. DR GeneTree; ENSGT00940000158877; -. DR HOGENOM; CLU_023471_0_1_1; -. DR OMA; QLHIFNS; -. DR OrthoDB; 1072976at2759; -. DR UniPathway; UPA00557; UER00614. DR BioGRID-ORCS; 110911; 9 hits in 19 CRISPR screens. DR ChiTaRS; Cds2; mouse. DR Proteomes; UP000000589; Chromosome 2. DR Bgee; ENSMUSG00000058793; Expressed in substantia nigra and 313 other tissues. DR ExpressionAtlas; A2AMQ5; baseline and differential. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-UniRule. DR GO; GO:0004605; F:phosphatidate cytidylyltransferase activity; IEA:UniProtKB-UniRule. DR GO; GO:0016024; P:CDP-diacylglycerol biosynthetic process; IEA:UniProtKB-UniRule. 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 Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516, KW ECO:0000256|PIRNR:PIRNR018269}; KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098, KW ECO:0000256|PIRNR:PIRNR018269}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR018269}; KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695, KW ECO:0000256|PIRNR:PIRNR018269, ECO:0000256|RuleBase:RU003938}; KW Phospholipid biosynthesis {ECO:0000256|ARBA:ARBA00023209, KW ECO:0000256|PIRNR:PIRNR018269}; KW Phospholipid metabolism {ECO:0000256|ARBA:ARBA00023264, KW ECO:0000256|PIRNR:PIRNR018269}; KW Proteomics identification {ECO:0000213|EPD:A2AMQ5, KW ECO:0000213|MaxQB:A2AMQ5, ECO:0000213|PeptideAtlas:A2AMQ5}; KW Reference proteome {ECO:0000313|Proteomes:UP000000589}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR018269, KW ECO:0000256|RuleBase:RU003938}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, KW ECO:0000256|PIRNR:PIRNR018269, ECO:0000256|RuleBase:RU003938}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, KW ECO:0000256|PIRNR:PIRNR018269}. FT TRANSMEM 106..123 FT /note="Helical" FT /evidence="ECO:0000256|PIRNR:PIRNR018269" FT TRANSMEM 150..168 FT /note="Helical" FT /evidence="ECO:0000256|PIRNR:PIRNR018269" FT TRANSMEM 175..197 FT /note="Helical" FT /evidence="ECO:0000256|PIRNR:PIRNR018269" FT TRANSMEM 203..229 FT /note="Helical" FT /evidence="ECO:0000256|PIRNR:PIRNR018269" FT TRANSMEM 241..263 FT /note="Helical" FT /evidence="ECO:0000256|PIRNR:PIRNR018269" FT TRANSMEM 319..339 FT /note="Helical" FT /evidence="ECO:0000256|PIRNR:PIRNR018269" FT REGION 1..31 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1..17 FT /note="Polyampholyte" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 427 AA; 49294 MW; F67EF48633FAF3E0 CRC64; MESESEAKLD GETASDSESR AETAPLPTSV DDTPEVLNRA LSNLSSRWKN WWVRGILTLA MIAFFFIIIY LGPMVLMMIV MCVQIKCFHE IITIGYNVYH SYDLPWFRTL SWYFLLCVNY FFYGETVTDY FFTLVQREEP LRILSKYHRF ISFALYLTGF CMFVLSLVKK HYRLQFYMFG WTHVTLLIVV TQSHLVIHNL FEGMIWFIVP ISCVICNDIM AYMFGFFFGR TPLIKLSPKK TWEGFIGGFF ATVVFGLLLS YVMSGYRCFV CPVEYNNDTN SFTVDCEPSD LFRLQEYNIP GVIQSAIGWK TVRMYPFQIH SIALSTFASL IGPFGGFFAS GFKRAFKIKD FANTIPGHGG IMDRFDCQYL MATFVNVYIA SFIRGPNPSK LIQQFLTLRP DQQLHIFNTL KSHLTDKGIL TSALEDE //