LOCUS       NP_619592                444 aa            linear   ROD 10-DEC-2024
DEFINITION  phosphatidate cytidylyltransferase 2 isoform a [Mus musculus].
ACCESSION   NP_619592
VERSION     NP_619592.1
DBSOURCE    REFSEQ: accession NM_138651.7
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 444)
  AUTHORS   Collins,D.M., Janardan,V., Barneda,D., Anderson,K.E., Niewczas,I.,
            Taylor,D., Qiu,D., Jessen,H.J., Lopez-Clavijo,A.F., Walker,S.,
            Raghu,P., Clark,J., Stephens,L.R. and Hawkins,P.T.
  TITLE     CDS2 expression regulates de novo phosphatidic acid synthesis
  JOURNAL   Biochem J 481 (20), 1449-1473 (2024)
   PUBMED   39312194
REFERENCE   2  (residues 1 to 444)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   3  (residues 1 to 444)
  AUTHORS   Xu,J., Chen,S., Wang,W., Man Lam,S., Xu,Y., Zhang,S., Pan,H.,
            Liang,J., Huang,X., Wang,Y., Li,T., Jiang,Y., Wang,Y., Ding,M.,
            Shui,G., Yang,H. and Huang,X.
  TITLE     Hepatic CDP-diacylglycerol synthase 2 deficiency causes
            mitochondrial dysfunction and promotes rapid progression of NASH
            and fibrosis
  JOURNAL   Sci Bull (Beijing) 67 (3), 299-314 (2022)
   PUBMED   36546079
  REMARK    GeneRIF: Hepatic CDP-diacylglycerol synthase 2 deficiency causes
            mitochondrial dysfunction and promotes rapid progression of NASH
            and fibrosis.
REFERENCE   4  (residues 1 to 444)
  AUTHORS   Stratman,A.N., Farrelly,O.M., Mikelis,C.M., Miller,M.F., Wang,Z.,
            Pham,V.N., Davis,A.E., Burns,M.C., Pezoa,S.A., Castranova,D.,
            Yano,J.J., Kilts,T.M., Davis,G.E., Gutkind,J.S. and Weinstein,B.M.
  TITLE     Anti-angiogenic effects of VEGF stimulation on endothelium
            deficient in phosphoinositide recycling
  JOURNAL   Nat Commun 11 (1), 1204 (2020)
   PUBMED   32139674
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 444)
  AUTHORS   Zhao,W., Cao,L., Ying,H., Zhang,W., Li,D., Zhu,X., Xue,W., Wu,S.,
            Cao,M., Fu,C., Qi,H., Hao,Y., Tang,Y.C., Qin,J., Zhong,T.P.,
            Lin,X., Yu,L., Li,X., Li,L., Wu,D. and Pan,W.
  TITLE     Endothelial CDS2 deficiency causes VEGFA-mediated vascular
            regression and tumor inhibition
  JOURNAL   Cell Res 29 (11), 895-910 (2019)
   PUBMED   31501519
  REMARK    GeneRIF: Endothelial CDS2 deficiency causes VEGFA-mediated vascular
            regression and tumor inhibition.
REFERENCE   6  (residues 1 to 444)
  AUTHORS   Lee,J., Xu,Y., Chen,Y., Sprung,R., Kim,S.C., Xie,S. and Zhao,Y.
  TITLE     Mitochondrial phosphoproteome revealed by an improved IMAC method
            and MS/MS/MS
  JOURNAL   Mol Cell Proteomics 6 (4), 669-676 (2007)
   PUBMED   17208939
REFERENCE   7  (residues 1 to 444)
  AUTHORS   Munton,R.P., Tweedie-Cullen,R., Livingstone-Zatchej,M.,
            Weinandy,F., Waidelich,M., Longo,D., Gehrig,P., Potthast,F.,
            Rutishauser,D., Gerrits,B., Panse,C., Schlapbach,R. and Mansuy,I.M.
  TITLE     Qualitative and quantitative analyses of protein phosphorylation in
            naive and stimulated mouse synaptosomal preparations
  JOURNAL   Mol Cell Proteomics 6 (2), 283-293 (2007)
   PUBMED   17114649
REFERENCE   8  (residues 1 to 444)
  AUTHORS   Jenner,J., Kerst,G., Handgretinger,R. and Muller,I.
  TITLE     Increased alpha2,6-sialylation of surface proteins on tolerogenic,
            immature dendritic cells and regulatory T cells
  JOURNAL   Exp Hematol 34 (9), 1212-1218 (2006)
   PUBMED   16939814
REFERENCE   9  (residues 1 to 444)
  AUTHORS   Inglis-Broadgate,S.L., Ocaka,L., Banerjee,R., Gaasenbeek,M.,
            Chapple,J.P., Cheetham,M.E., Clark,B.J., Hunt,D.M. and Halford,S.
  TITLE     Isolation and characterization of murine Cds (CDP-diacylglycerol
            synthase) 1 and 2
  JOURNAL   Gene 356, 19-31 (2005)
   PUBMED   16023307
  REMARK    GeneRIF: Cds2 showed a ubiquitous pattern of expression and was
            mapped to chromosome 2G1.
REFERENCE   10 (residues 1 to 444)
  AUTHORS   Volta,M., Bulfone,A., Gattuso,C., Rossi,E., Mariani,M.,
            Consalez,G.G., Zuffardi,O., Ballabio,A., Banfi,S. and Franco,B.
  TITLE     Identification and characterization of CDS2, a mammalian homolog of
            the Drosophila CDP-diacylglycerol synthase gene
  JOURNAL   Genomics 55 (1), 68-77 (1999)
   PUBMED   9889000
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CJ112406.1, AK147541.1, CD351907.1, BQ572878.1, AK017677.1 and
            AI854580.1.
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longest isoform (a).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK147541.1, AK036328.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849375
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..444
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="2"
                     /map="2 64.15 cM"
     Protein         1..444
                     /product="phosphatidate cytidylyltransferase 2 isoform a"
                     /EC_number="2.7.7.41"
                     /note="phosphatidate cytidylyltransferase 2; CDP-DG
                     synthase 2; CDP-DAG synthase 2; CDP-diglyceride synthase
                     2; CDP-diglyceride pyrophosphorylase 2; CTP:phosphatidate
                     cytidylyltransferase 2; CDP-diacylglycerol synthase
                     (phosphatidate cytidylyltransferase) 2"
                     /calculated_mol_wt=51183
     Region          1..48
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99L43.1)"
     Site            20
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O95674; propagated from
                     UniProtKB/Swiss-Prot (Q99L43.1)"
     Site            30
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:O95674; propagated from
                     UniProtKB/Swiss-Prot (Q99L43.1)"
     Site            32
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17208939,
                     ECO:0007744|PubMed:17242355, ECO:0007744|PubMed:18630941,
                     ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q99L43.1)"
     Site            34
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O95674; propagated from
                     UniProtKB/Swiss-Prot (Q99L43.1)"
     Site            36
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q99L43.1)"
     Site            50
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q99L43.1)"
     Site            78..98
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99L43.1)"
     Region          105..424
                     /region_name="CTP_transf_1"
                     /note="Cytidylyltransferase family; cl21502"
                     /db_xref="CDD:451277"
     Site            129..149
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99L43.1)"
     Site            165..185
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99L43.1)"
     Site            212..232
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99L43.1)"
     Site            261..281
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99L43.1)"
     Site            339..359
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q99L43.1)"
     CDS             1..444
                     /gene="Cds2"
                     /gene_synonym="5730450N06Rik; 5730460C18Rik; D2Wsu127e"
                     /coded_by="NM_138651.7:297..1631"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS16772.1"
                     /db_xref="GeneID:110911"
                     /db_xref="MGI:MGI:1332236"
ORIGIN      
        1 mtelrqrvvr edappedkes eseakldget asdsesraet aplptsvddt pevlnralsn
       61 lssrwknwwv rgiltlamia fffiiiylgp mvlmmivmcv qikcfheiit igynvyhsyd
      121 lpwfrtlswy fllcvnyffy getvtdyfft lvqreeplri lskyhrfisf alyltgfcmf
      181 vlslvkkhyr lqfymfgwth vtllivvtqs hlvihnlfeg miwfivpisc vicndimaym
      241 fgfffgrtpl iklspkktwe gfiggffatv vfglllsyvm sgyrcfvcpv eynndtnsft
      301 vdcepsdlfr lqeynipgvi qsaigwktvr mypfqihsia lstfasligp fggffasgfk
      361 rafkikdfan tipghggimd rfdcqylmat fvnvyiasfi rgpnpskliq qfltlrpdqq
      421 lhifntlksh ltdkgiltsa lede
//
