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O35052

- CDS1_RAT

UniProt

O35052 - CDS1_RAT

Protein

Phosphatidate cytidylyltransferase 1

Gene

Cds1

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 103 (01 Oct 2014)
      Sequence version 2 (30 May 2000)
      Previous versions | rss
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    Functioni

    Provides CDP-diacylglycerol, an important precursor for the synthesis of phosphatidylinositol (PtdIns), phosphatidylglycerol, and cardiolipin. Overexpression may amplify cellular signaling responses from cytokines. May also play an important role in the signal transduction mechanism of retina and neural cells By similarity. May play an important role in phosphoinositide synthesis, prefers 1-stearoyl-2-arachidonoyl phosphatidic acid as substrate.By similarity

    Catalytic activityi

    CTP + phosphatidate = diphosphate + CDP-diacylglycerol.

    Cofactori

    Magnesium.

    Pathwayi

    GO - Molecular functioni

    1. phosphatidate cytidylyltransferase activity Source: RGD

    GO - Biological processi

    1. CDP-diacylglycerol biosynthetic process Source: UniProtKB
    2. phosphatidylinositol biosynthetic process Source: UniProtKB

    Keywords - Molecular functioni

    Nucleotidyltransferase, Transferase

    Keywords - Biological processi

    Lipid biosynthesis, Lipid metabolism, Phospholipid biosynthesis, Phospholipid metabolism

    Keywords - Ligandi

    Magnesium

    Enzyme and pathway databases

    ReactomeiREACT_199142. Synthesis of PI.
    UniPathwayiUPA00557; UER00614.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Phosphatidate cytidylyltransferase 1 (EC:2.7.7.41)
    Alternative name(s):
    CDP-DAG synthase 1
    CDP-DG synthase 1
    CDP-diacylglycerol synthase 1
    Short name:
    CDS 1
    CDP-diglyceride pyrophosphorylase 1
    CDP-diglyceride synthase 1
    CTP:phosphatidate cytidylyltransferase 1
    Gene namesi
    Name:Cds1
    Synonyms:Cds
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Chromosome 14

    Organism-specific databases

    RGDi621185. Cds1.

    Subcellular locationi

    Endoplasmic reticulum membrane 1 Publication; Multi-pass membrane protein 1 Publication
    Note: Cytoplasmic aspect of the endoplasmic reticulum.

    GO - Cellular componenti

    1. endoplasmic reticulum membrane Source: RGD
    2. integral component of membrane Source: UniProtKB-KW

    Keywords - Cellular componenti

    Endoplasmic reticulum, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 461461Phosphatidate cytidylyltransferase 1PRO_0000090715Add
    BLAST

    Proteomic databases

    PaxDbiO35052.
    PRIDEiO35052.

    PTM databases

    PhosphoSiteiO35052.

    Expressioni

    Tissue specificityi

    Brain, retina and testis. Found in cerebellar Purkinje cells, pineal body, inner segment of photoreceptor cells and postmitotic spermatocytes and spermatids.

    Inductioni

    Activated by GTP. Inhibited by CDP-diacylglycerol (product inhibition).

    Gene expression databases

    GenevestigatoriO35052.

    Interactioni

    Subunit structurei

    Interacts with FOS; this interaction may enhance catalytic activity.By similarity

    Protein-protein interaction databases

    STRINGi10116.ENSRNOP00000002918.

    Structurei

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei96 – 11621HelicalSequence AnalysisAdd
    BLAST
    Transmembranei149 – 16921HelicalSequence AnalysisAdd
    BLAST
    Transmembranei183 – 20321HelicalSequence AnalysisAdd
    BLAST
    Transmembranei230 – 25021HelicalSequence AnalysisAdd
    BLAST
    Transmembranei279 – 29921HelicalSequence AnalysisAdd
    BLAST
    Transmembranei357 – 37721HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the CDS family.Curated

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG0575.
    GeneTreeiENSGT00390000016175.
    HOGENOMiHOG000209582.
    HOVERGENiHBG002485.
    InParanoidiO35052.
    KOiK00981.
    OMAiVKCFQEI.
    OrthoDBiEOG7M98G5.
    PhylomeDBiO35052.
    TreeFamiTF313464.

    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.

    O35052-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLELRHRGGC PGPGGAGTPP PREGEAAGGD HETESTSDKE TDIDDRYGDL    50
    DARGDSDVPE VPPSSDRTPE ILKKALSGLS SRWKNWWIRG ILTLTMISLF 100
    FLIIYMGSFM LMLLVLGIQV KCFQEIITIG YRVYHSYDLP WFRTLSWYFL 150
    LCVNYFFYGE TVADYFATFV QREEQLQFLI RYHRFISFAL YLAGFCMFVL 200
    SLVKKHYRLQ FYMFAWTHVT LLITVTQSHL VIQNLFEGMI WFLVPISSVI 250
    CNDITAYLFG FFFGRTPLIK LSPKKTWEGF IGGFFSTVIF GFIAAYVLSK 300
    YQYFVCPVEY RSDVNSFVTE CEPSELFQLQ NYSLPPFLQA VLSRETVSLY 350
    PFQIHSIALS TFASLIGPFG GFFASGFKRA FKIKDFANTI PGHGGIMDRF 400
    DCQYLMATFV HVYITSFIRG PNPSKVLQQL LVLQPEQQLN IYRTLKIHLT 450
    EKGILQPTWK V 461
    Length:461
    Mass (Da):52,970
    Last modified:May 30, 2000 - v2
    Checksum:i66061B9A8AF73B3D
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti172 – 1721R → K in BAA28787. 1 PublicationCurated
    Sequence conflicti299 – 30810SKYQYFVCPV → VQVSVLCGARW in BAA22085. (PubMed:9083091)Curated
    Sequence conflicti326 – 3261L → V in BAA28787. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB000517 mRNA. Translation: BAA22085.1.
    AB009999 mRNA. Translation: BAA28787.1.
    BC127492 mRNA. Translation: AAI27493.1.
    RefSeqiNP_112521.2. NM_031242.2.
    UniGeneiRn.18983.

    Genome annotation databases

    EnsembliENSRNOT00000002918; ENSRNOP00000002918; ENSRNOG00000002142.
    GeneIDi81925.
    KEGGirno:81925.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB000517 mRNA. Translation: BAA22085.1 .
    AB009999 mRNA. Translation: BAA28787.1 .
    BC127492 mRNA. Translation: AAI27493.1 .
    RefSeqi NP_112521.2. NM_031242.2.
    UniGenei Rn.18983.

    3D structure databases

    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 10116.ENSRNOP00000002918.

    PTM databases

    PhosphoSitei O35052.

    Proteomic databases

    PaxDbi O35052.
    PRIDEi O35052.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSRNOT00000002918 ; ENSRNOP00000002918 ; ENSRNOG00000002142 .
    GeneIDi 81925.
    KEGGi rno:81925.

    Organism-specific databases

    CTDi 1040.
    RGDi 621185. Cds1.

    Phylogenomic databases

    eggNOGi COG0575.
    GeneTreei ENSGT00390000016175.
    HOGENOMi HOG000209582.
    HOVERGENi HBG002485.
    InParanoidi O35052.
    KOi K00981.
    OMAi VKCFQEI.
    OrthoDBi EOG7M98G5.
    PhylomeDBi O35052.
    TreeFami TF313464.

    Enzyme and pathway databases

    UniPathwayi UPA00557 ; UER00614 .
    Reactomei REACT_199142. Synthesis of PI.

    Miscellaneous databases

    NextBioi 615829.
    PROi O35052.

    Gene expression databases

    Genevestigatori O35052.

    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. "Gene cloning and characterization of CDP-diacylglycerol synthase from rat brain."
      Saito S., Goto K., Tonosaki A., Kondo H.
      J. Biol. Chem. 272:9503-9509(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: Wistar.
      Tissue: Brain.
    2. "Rat brain CDP-diacylglycerol synthase."
      Hosaka K., Imai H., Nikawa J.
      Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: Wistar.
      Tissue: Brain.
    3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Liver.
    4. "Topography of glycerolipid synthetic enzymes. Synthesis of phosphatidylserine, phosphatidylinositol and glycerolipid intermediates occurs on the cytoplasmic surface of rat liver microsomal vesicles."
      Ballas L.M., Bell R.M.
      Biochim. Biophys. Acta 665:586-595(1981) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    5. "Extraction and stabilization of mammalian CDP-diacylglycerol synthase activity."
      Monaco M.E., Feldman M.
      Biochem. Biophys. Res. Commun. 239:166-170(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.
      Tissue: Liver.

    Entry informationi

    Entry nameiCDS1_RAT
    AccessioniPrimary (citable) accession number: O35052
    Secondary accession number(s): A0JPL6, O88208
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: May 30, 2000
    Last modified: October 1, 2014
    This is version 103 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3