Reviewed, UniProtKB/Swiss-Prot O35052 (CDS1_RAT)

Names and origin

Protein names

Recommended name:
    Phosphatidate cytidylyltransferase 1
    EC=2.7.7.41
Alternative name(s):
    CDP-diglyceride pyrophosphorylase 1
    CDP-diglyceride synthetase 1
    CDP-diacylglycerol synthase 1
      Short name=CDS 1
    CTP:phosphatidate cytidylyltransferase 1
    CDP-DG synthetase 1
    CDP-DAG synthase 1

Gene names

Name:	Cds1
Synonyms:	Cds

Organism

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	461 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence 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.
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.

Ontologies

Keywords
Biological process	Phospholipid biosynthesis
Cellular component	Endoplasmic reticulum Membrane
Domain	Transmembrane
Ligand	Magnesium
Molecular function	Nucleotidyltransferase Transferase
Gene Ontology (GO)
Biological process	phospholipid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	endoplasmic reticulum membrane Ref.1 Inferred from direct assay. Source: RGD integral to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW phosphatidate cytidylyltransferase activity Ref.5 Inferred from direct assay. Source: RGD
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 461	461	Phosphatidate cytidylyltransferase 1		PRO_0000090715
Regions
	Transmembrane	96 – 116	21	Potential
	Transmembrane	149 – 169	21	Potential
	Transmembrane	183 – 203	21	Potential
	Transmembrane	230 – 250	21	Potential
	Transmembrane	279 – 299	21	Potential
	Transmembrane	357 – 377	21	Potential
Experimental info
	Sequence conflict	172	1	R → K in BAA28787. Ref.2
	Sequence conflict	299 – 308	10	SKYQYFVCPV → VQVSVLCGARW Ref.1
	Sequence conflict	326	1	L → V in BAA28787. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	O35052-1 [UniParc]. Last modified May 30, 2000. Version 2. Checksum: 66061B9A8AF73B3D	FASTA	461	52,970
	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

References

	« Hide 'large scale' referencesShow '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: 9083091] [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: 15489334] [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: 6271231] [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: 9345289] [Abstract] Cited for: CHARACTERIZATION. Tissue: Liver.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AB000517 mRNA. Translation: BAA22085.1. AB009999 mRNA. Translation: BAA28787.1. BC127492 mRNA. Translation: AAI27493.1.
IPI	IPI00326213.
RefSeq	NP_112521.2.
UniGene	Rn.18983
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	O35052.
Genome annotation databases
Ensembl	ENSRNOT00000002918; ENSRNOP00000002918; ENSRNOG00000002142; Rattus norvegicus. [Genome view]
GeneID	81925.
KEGG	rno:81925.
UCSC	NM_031242. rat.
Organism-specific databases
CTD	81925.
RGD	621185. Cds1.
Phylogenomic databases
HOVERGEN	O35052.
OMA	IEISPKK.
Enzyme and pathway databases
BRENDA	2.7.7.41. 248.
Gene expression databases
ArrayExpress	O35052.
Genevestigator	O35052.
GermOnline	ENSRNOG00000002142. Rattus norvegicus.
Family and domain databases
InterPro	IPR000374. PC_trans. IPR016720. PC_Trfase_euk. [Graphical view]
Pfam	PF01148. CTP_transf_1. 1 hit. [Graphical view]
PIRSF	PIRSF018269. PC_trans_euk. 1 hit.
PROSITE	PS01315. CDS. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	615829.

Entry information

Entry name

CDS1_RAT

Accession

Primary (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:	November 3, 2009
This is version 67 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)