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P56079

- CDSA_DROME

UniProt

P56079 - CDSA_DROME

Protein

Phosphatidate cytidylyltransferase, photoreceptor-specific

Gene

CdsA

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 115 (01 Oct 2014)
      Sequence version 2 (01 Dec 2000)
      Previous versions | rss
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    Functioni

    Required for the regeneration of the signaling molecule phosphatidylinositol 4,5-bisphosphate (PtdInsP2) from phosphatidic acid and maintenance of its steady supply during signaling thus plays an essential role during phospholipase C-mediated transduction.

    Catalytic activityi

    CTP + phosphatidate = diphosphate + CDP-diacylglycerol.

    Pathwayi

    GO - Molecular functioni

    1. phosphatidate cytidylyltransferase activity Source: FlyBase

    GO - Biological processi

    1. CDP-diacylglycerol biosynthetic process Source: FlyBase
    2. phototransduction Source: FlyBase
    3. regulation of lipid storage Source: FlyBase
    4. rhodopsin mediated signaling pathway Source: FlyBase
    5. terminal branching, open tracheal system Source: FlyBase
    6. thermotaxis Source: FlyBase
    7. trachea morphogenesis Source: FlyBase
    8. visual perception Source: UniProtKB-KW

    Keywords - Molecular functioni

    Nucleotidyltransferase, Transferase

    Keywords - Biological processi

    Lipid biosynthesis, Lipid metabolism, Phospholipid biosynthesis, Phospholipid metabolism, Sensory transduction, Vision

    Enzyme and pathway databases

    ReactomeiREACT_180830. Synthesis of PI.
    REACT_180833. Synthesis of PG.
    UniPathwayiUPA00557; UER00614.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Phosphatidate cytidylyltransferase, photoreceptor-specific (EC:2.7.7.41)
    Alternative name(s):
    CDP-DAG synthase
    CDP-DG synthase
    CDP-diacylglycerol synthase
    Short name:
    CDS
    CDP-diglyceride pyrophosphorylase
    CDP-diglyceride synthase
    CTP:phosphatidate cytidylyltransferase
    Gene namesi
    Name:CdsA
    ORF Names:CG7962
    OrganismiDrosophila melanogaster (Fruit fly)
    Taxonomic identifieri7227 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
    ProteomesiUP000000803: Chromosome 3L

    Organism-specific databases

    FlyBaseiFBgn0010350. CdsA.

    Subcellular locationi

    GO - Cellular componenti

    1. integral component of membrane Source: UniProtKB-KW
    2. plasma membrane Source: FlyBase

    Keywords - Cellular componenti

    Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 447447Phosphatidate cytidylyltransferase, photoreceptor-specificPRO_0000090720Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei30 – 301Phosphoserine1 Publication
    Modified residuei34 – 341Phosphoserine1 Publication
    Modified residuei35 – 351Phosphoserine1 Publication
    Modified residuei40 – 401Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiP56079.

    Expressioni

    Tissue specificityi

    Retina. Localized to the photoreceptor neurons, both in the compound eyes and ocelli.

    Gene expression databases

    BgeeiP56079.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    beQ9VXZ31EBI-86600,EBI-143313
    ScampQ9VXV61EBI-86600,EBI-188862

    Protein-protein interaction databases

    BioGridi68739. 10 interactions.
    DIPiDIP-23447N.
    IntActiP56079. 3 interactions.
    MINTiMINT-801533.
    STRINGi7227.FBpp0076411.

    Structurei

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei88 – 10821HelicalSequence AnalysisAdd
    BLAST
    Transmembranei147 – 16721HelicalSequence AnalysisAdd
    BLAST
    Transmembranei180 – 20021HelicalSequence AnalysisAdd
    BLAST
    Transmembranei203 – 22321HelicalSequence AnalysisAdd
    BLAST
    Transmembranei227 – 24721HelicalSequence AnalysisAdd
    BLAST
    Transmembranei276 – 29621HelicalSequence AnalysisAdd
    BLAST
    Transmembranei350 – 37021HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the CDS family.Curated

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG0575.
    GeneTreeiENSGT00390000016175.
    InParanoidiP56079.
    KOiK00981.
    OMAiVKCFQEI.
    OrthoDBiEOG7M98G5.
    PhylomeDBiP56079.

    Family and domain databases

    InterProiIPR000374. PC_trans.
    IPR016720. PC_Trfase_euk.
    [Graphical view]
    PfamiPF01148. CTP_transf_1. 1 hit.
    [Graphical view]
    PIRSFiPIRSF018269. PC_trans_euk. 1 hit.
    PROSITEiPS01315. CDS. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P56079-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAEVRRRKGE DEPLEDTAIS GSDAANKRNS AADSSDHVDS EEEKIPEEKF    50
    VDELAKNLPQ GTDKTPEILD SALKDLPDRW KNWVIRGIFT WIMICGFALI 100
    IYGGPLALMI TTLLVQVKCF QEIISIGYQV YRIHGLPWFR SLSWYFLLTS 150
    NYFFYGENLV DYFGVVINRV EYLKFLVTYH RFLSFALYII GFVWFVLSLV 200
    KKYYIKQFSL FAWTHVSLLI VVTQSYLIIQ NIFEGLIWFI VPVSMIVCND 250
    VMAYVFGFFF GRTPLIKLSP KKTWEGFIGG GFATVLFGIL FSYVLCNYQY 300
    FICPIQYSEE QGRMTMSCVP SYLFTPQEYS LKLFGIGKTL NLYPFIWHSI 350
    SLSLFSSIIG PFGGFFASGF KRAFKIKDFG DMIPGHGGIM DRFDCQFLMA 400
    TFVNVYISSF IRTPSPAKLL TQIYNLKPDQ QYQIYQSLKD NLGDMLT 447
    Length:447
    Mass (Da):51,511
    Last modified:December 1, 2000 - v2
    Checksum:i2E690CD02D3F4187
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti444 – 4441D → H no nucleotide entry (PubMed:7816135)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE014296 Genomic DNA. Translation: AAF50483.1.
    RefSeqiNP_524661.1. NM_079922.4.
    UniGeneiDm.6770.

    Genome annotation databases

    EnsemblMetazoaiFBtr0076688; FBpp0076411; FBgn0010350.
    GeneIDi43950.
    KEGGidme:Dmel_CG7962.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE014296 Genomic DNA. Translation: AAF50483.1 .
    RefSeqi NP_524661.1. NM_079922.4.
    UniGenei Dm.6770.

    3D structure databases

    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 68739. 10 interactions.
    DIPi DIP-23447N.
    IntActi P56079. 3 interactions.
    MINTi MINT-801533.
    STRINGi 7227.FBpp0076411.

    Proteomic databases

    PaxDbi P56079.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblMetazoai FBtr0076688 ; FBpp0076411 ; FBgn0010350 .
    GeneIDi 43950.
    KEGGi dme:Dmel_CG7962.

    Organism-specific databases

    CTDi 43950.
    FlyBasei FBgn0010350. CdsA.

    Phylogenomic databases

    eggNOGi COG0575.
    GeneTreei ENSGT00390000016175.
    InParanoidi P56079.
    KOi K00981.
    OMAi VKCFQEI.
    OrthoDBi EOG7M98G5.
    PhylomeDBi P56079.

    Enzyme and pathway databases

    UniPathwayi UPA00557 ; UER00614 .
    Reactomei REACT_180830. Synthesis of PI.
    REACT_180833. Synthesis of PG.

    Miscellaneous databases

    ChiTaRSi CdsA. drosophila.
    GenomeRNAii 43950.
    NextBioi 836438.

    Gene expression databases

    Bgeei P56079.

    Family and domain databases

    InterProi IPR000374. PC_trans.
    IPR016720. PC_Trfase_euk.
    [Graphical view ]
    Pfami PF01148. CTP_transf_1. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF018269. PC_trans_euk. 1 hit.
    PROSITEi PS01315. CDS. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Regulation of PLC-mediated signalling in vivo by CDP-diacylglycerol synthase."
      Wu L., Niemeyer B., Colley N., Socolich M., Zuker C.S.
      Nature 373:216-222(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Tissue: Retina.
    2. "The genome sequence of Drosophila melanogaster."
      Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
      , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
      Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Berkeley.
    3. Cited for: GENOME REANNOTATION.
      Strain: Berkeley.
    4. "Phosphoproteome analysis of Drosophila melanogaster embryos."
      Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.
      J. Proteome Res. 7:1675-1682(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30; SER-34; SER-35 AND SER-40, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Embryo.

    Entry informationi

    Entry nameiCDSA_DROME
    AccessioniPrimary (citable) accession number: P56079
    Secondary accession number(s): Q9VSE0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: December 1, 2000
    Last modified: October 1, 2014
    This is version 115 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programDrosophila annotation project

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Drosophila
      Drosophila: entries, gene names and cross-references to FlyBase
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3