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O35052 (CDS1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 94. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended 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 names
Name:Cds1
Synonyms:Cds
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length461 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Catalytic activity

CTP + phosphatidate = diphosphate + CDP-diacylglycerol.

Cofactor

Magnesium.

Pathway

Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-diacylglycerol from sn-glycerol 3-phosphate: step 3/3.

Subunit structure

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

Subcellular location

Endoplasmic reticulum membrane; Multi-pass membrane protein. Note: Cytoplasmic aspect of the endoplasmic reticulum. Ref.4

Tissue specificity

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

Induction

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

Sequence similarities

Belongs to the CDS family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 461461Phosphatidate cytidylyltransferase 1
PRO_0000090715

Regions

Transmembrane96 – 11621Helical; Potential
Transmembrane149 – 16921Helical; Potential
Transmembrane183 – 20321Helical; Potential
Transmembrane230 – 25021Helical; Potential
Transmembrane279 – 29921Helical; Potential
Transmembrane357 – 37721Helical; Potential

Experimental info

Sequence conflict1721R → K in BAA28787. Ref.2
Sequence conflict299 – 30810SKYQYFVCPV → VQVSVLCGARW in BAA22085. Ref.1
Sequence conflict3261L → V in BAA28787. Ref.2

Sequences

Sequence LengthMass (Da)Tools
O35052 [UniParc].

Last modified May 30, 2000. Version 2.
Checksum: 66061B9A8AF73B3D

FASTA46152,970
        10         20         30         40         50         60 
MLELRHRGGC PGPGGAGTPP PREGEAAGGD HETESTSDKE TDIDDRYGDL DARGDSDVPE 

        70         80         90        100        110        120 
VPPSSDRTPE ILKKALSGLS SRWKNWWIRG ILTLTMISLF FLIIYMGSFM LMLLVLGIQV 

       130        140        150        160        170        180 
KCFQEIITIG YRVYHSYDLP WFRTLSWYFL LCVNYFFYGE TVADYFATFV QREEQLQFLI 

       190        200        210        220        230        240 
RYHRFISFAL YLAGFCMFVL SLVKKHYRLQ FYMFAWTHVT LLITVTQSHL VIQNLFEGMI 

       250        260        270        280        290        300 
WFLVPISSVI CNDITAYLFG FFFGRTPLIK LSPKKTWEGF IGGFFSTVIF GFIAAYVLSK 

       310        320        330        340        350        360 
YQYFVCPVEY RSDVNSFVTE CEPSELFQLQ NYSLPPFLQA VLSRETVSLY PFQIHSIALS 

       370        380        390        400        410        420 
TFASLIGPFG GFFASGFKRA FKIKDFANTI PGHGGIMDRF DCQYLMATFV HVYITSFIRG 

       430        440        450        460 
PNPSKVLQQL LVLQPEQQLN IYRTLKIHLT EKGILQPTWK V

« Hide

References

« Hide 'large scale' references
[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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AB000517 mRNA. Translation: BAA22085.1.
AB009999 mRNA. Translation: BAA28787.1.
BC127492 mRNA. Translation: AAI27493.1.
IPIIPI00326213.
RefSeqNP_112521.2. NM_031242.2.
UniGeneRn.18983.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRING10116.ENSRNOP00000002918.

PTM databases

PhosphoSiteO35052.

Proteomic databases

PaxDbO35052.
PRIDEO35052.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000002918; ENSRNOP00000002918; ENSRNOG00000002142.
GeneID81925.
KEGGrno:81925.

Organism-specific databases

CTD1040.
RGD621185. Cds1.

Phylogenomic databases

eggNOGCOG0575.
GeneTreeENSGT00390000016175.
HOGENOMHOG000209582.
HOVERGENHBG002485.
InParanoidO35052.
KOK00981.
OMAWVIRGIF.
OrthoDBEOG4V437K.

Enzyme and pathway databases

UniPathwayUPA00557; UER00614.

Gene expression databases

GenevestigatorO35052.
GermOnlineENSRNOG00000002142. Rattus norvegicus.

Family and domain databases

InterProIPR000374. PC_trans.
IPR016720. PC_Trfase_euk.
[Graphical view]
PfamPF01148. CTP_transf_1. 1 hit.
[Graphical view]
PIRSFPIRSF018269. PC_trans_euk. 1 hit.
PROSITEPS01315. CDS. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio615829.

Entry information

Entry nameCDS1_RAT
AccessionPrimary (citable) accession number: O35052
Secondary accession number(s): A0JPL6, O88208
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: May 30, 2000
Last modified: May 29, 2013
This is version 94 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents