ID A2AMQ5_MOUSE Unreviewed; 427 AA. AC A2AMQ5; DT 20-FEB-2007, integrated into UniProtKB/TrEMBL. DT 20-FEB-2007, sequence version 1. DT 08-MAY-2019, entry version 90. DE RecName: Full=Phosphatidate cytidylyltransferase {ECO:0000256|PIRNR:PIRNR018269, ECO:0000256|RuleBase:RU003938}; DE EC=2.7.7.41 {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; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; OC Muroidea; Muridae; 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 RT affinity 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., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the 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 RT 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: Provides CDP-diacylglycerol, an important precursor for CC the synthesis of phosphatidylinositol, phosphatidylglycerol, and CC cardiolipin. {ECO:0000256|PIRNR:PIRNR018269}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphate + CTP + H(+) = a CDP- CC 1,2-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: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CC CDP-diacylglycerol from sn-glycerol 3-phosphate: step 3/3. CC {ECO:0000256|PIRNR:PIRNR018269, ECO:0000256|RuleBase:RU003938}. CC -!- SIMILARITY: Belongs to the CDS family. 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 Ensembl; ENSMUST00000089461; ENSMUSP00000086886; ENSMUSG00000058793. DR GeneID; 110911; -. DR UCSC; uc029ueu.2; mouse. DR CTD; 8760; -. DR MGI; MGI:1332236; Cds2. DR eggNOG; KOG1440; Eukaryota. DR eggNOG; COG0575; LUCA. DR GeneTree; ENSGT00940000158877; -. DR HOGENOM; HOG000209582; -. DR OMA; MIVLCVQ; -. DR OrthoDB; 1072976at2759; -. DR UniPathway; UPA00557; UER00614. DR ChiTaRS; Cds2; mouse. DR Proteomes; UP000000589; Chromosome 2. DR Bgee; ENSMUSG00000058793; Expressed in 296 organ(s), highest expression level in substantia nigra. 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 Complete proteome {ECO:0000313|Proteomes:UP000000589}; KW Lipid biosynthesis {ECO:0000256|PIRNR:PIRNR018269}; KW Lipid metabolism {ECO:0000256|PIRNR:PIRNR018269}; KW Membrane {ECO:0000256|PIRNR:PIRNR018269}; KW Nucleotidyltransferase {ECO:0000256|PIRNR:PIRNR018269, KW ECO:0000256|RuleBase:RU003938}; KW Phospholipid biosynthesis {ECO:0000256|PIRNR:PIRNR018269}; KW Phospholipid metabolism {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|PIRNR:PIRNR018269, KW ECO:0000256|RuleBase:RU003938}; KW Transmembrane {ECO:0000256|PIRNR:PIRNR018269, KW ECO:0000256|RuleBase:RU003938}; KW Transmembrane helix {ECO:0000256|PIRNR:PIRNR018269}. FT TRANSMEM 106 123 Helical. {ECO:0000256|PIRNR:PIRNR018269}. FT TRANSMEM 150 168 Helical. {ECO:0000256|PIRNR:PIRNR018269}. FT TRANSMEM 175 197 Helical. {ECO:0000256|PIRNR:PIRNR018269}. FT TRANSMEM 203 229 Helical. {ECO:0000256|PIRNR:PIRNR018269}. FT TRANSMEM 241 263 Helical. {ECO:0000256|PIRNR:PIRNR018269}. FT TRANSMEM 319 339 Helical. {ECO:0000256|PIRNR:PIRNR018269}. 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 //