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O35052

- CDS1_RAT

UniProt

O35052 - CDS1_RAT

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Protein

Phosphatidate cytidylyltransferase 1

Gene

Cds1

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

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

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
Complete GO annotation...

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.

Topology

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

GO - Cellular componenti

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

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.

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

        10         20         30         40         50
MLELRHRGGC PGPGGAGTPP PREGEAAGGD HETESTSDKE TDIDDRYGDL
60 70 80 90 100
DARGDSDVPE VPPSSDRTPE ILKKALSGLS SRWKNWWIRG ILTLTMISLF
110 120 130 140 150
FLIIYMGSFM LMLLVLGIQV KCFQEIITIG YRVYHSYDLP WFRTLSWYFL
160 170 180 190 200
LCVNYFFYGE TVADYFATFV QREEQLQFLI RYHRFISFAL YLAGFCMFVL
210 220 230 240 250
SLVKKHYRLQ FYMFAWTHVT LLITVTQSHL VIQNLFEGMI WFLVPISSVI
260 270 280 290 300
CNDITAYLFG FFFGRTPLIK LSPKKTWEGF IGGFFSTVIF GFIAAYVLSK
310 320 330 340 350
YQYFVCPVEY RSDVNSFVTE CEPSELFQLQ NYSLPPFLQA VLSRETVSLY
360 370 380 390 400
PFQIHSIALS TFASLIGPFG GFFASGFKRA FKIKDFANTI PGHGGIMDRF
410 420 430 440 450
DCQYLMATFV HVYITSFIRG PNPSKVLQQL LVLQPEQQLN IYRTLKIHLT
460
EKGILQPTWK V
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 104 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