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Protein

Phosphatidate cytidylyltransferase 2

Gene

Cds2

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

Provides CDP-diacylglycerol, an important precursor for the synthesis of phosphatidylinositol, phosphatidylglycerol, and cardiolipin.By similarity

Catalytic activityi

CTP + phosphatidate = diphosphate + CDP-diacylglycerol.

Pathwayi

GO - Molecular functioni

  1. phosphatidate cytidylyltransferase activity Source: UniProtKB-EC

GO - Biological processi

  1. CDP-diacylglycerol biosynthetic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Nucleotidyltransferase, Transferase

Keywords - Biological processi

Lipid biosynthesis, Lipid metabolism, Phospholipid biosynthesis, Phospholipid metabolism

Enzyme and pathway databases

ReactomeiREACT_279858. Synthesis of PG.
UniPathwayiUPA00557; UER00614.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphatidate cytidylyltransferase 2 (EC:2.7.7.41)
Alternative name(s):
CDP-DAG synthase 2
CDP-DG synthase 2
CDP-diacylglycerol synthase 2
Short name:
CDS 2
CDP-diglyceride pyrophosphorylase 2
CDP-diglyceride synthase 2
CTP:phosphatidate cytidylyltransferase 2
Gene namesi
Name:Cds2
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494 Componenti: Unplaced

Organism-specific databases

RGDi621186. Cds2.

Subcellular locationi

  1. Mitochondrion inner membrane By similarity; Multi-pass membrane protein By similarity; Matrix side By similarity

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei78 – 9821HelicalSequence AnalysisAdd
BLAST
Transmembranei129 – 14921HelicalSequence AnalysisAdd
BLAST
Transmembranei165 – 18521HelicalSequence AnalysisAdd
BLAST
Transmembranei212 – 23221HelicalSequence AnalysisAdd
BLAST
Transmembranei261 – 28121HelicalSequence AnalysisAdd
BLAST
Transmembranei338 – 35821HelicalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. endoplasmic reticulum Source: Ensembl
  2. integral component of membrane Source: UniProtKB-KW
  3. mitochondrial inner membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion inner membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 443443Phosphatidate cytidylyltransferase 2PRO_0000090718Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei20 – 201PhosphoserineBy similarity
Modified residuei30 – 301PhosphothreonineBy similarity
Modified residuei32 – 321PhosphoserineBy similarity
Modified residuei34 – 341PhosphoserineBy similarity
Modified residuei36 – 361PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ91XU8.
PRIDEiQ91XU8.

PTM databases

PhosphoSiteiQ91XU8.

Expressioni

Gene expression databases

ExpressionAtlasiQ91XU8. baseline and differential.
GenevestigatoriQ91XU8.

Interactioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000028888.

Family & Domainsi

Sequence similaritiesi

Belongs to the CDS family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0575.
HOGENOMiHOG000209582.
HOVERGENiHBG002485.
InParanoidiQ91XU8.
KOiK00981.
PhylomeDBiQ91XU8.

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.

Q91XU8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTELRQRAVR EDAPPEDKES ESEAKLDGET ASDSESRAET APPPTSIDDT
60 70 80 90 100
PEVLNRALSN LSSRWKNWWV RGILTMAMIA FFFIIIYLGP MVLMMIVMCV
110 120 130 140 150
QIKCFHEIIT IGYNVYHSYD LPWFRTLSWY FLLCVNYFFY GETVTDYFFT
160 170 180 190 200
LVQREEPLRI LSKYHRFISF TLYLTGFCMF VLSLVKKHYR LQFYMFGWTH
210 220 230 240 250
VTLLIVVTQS HLVIHNLFEG MIWFIVPISC VICNDIMAYM FGFFFGRTPL
260 270 280 290 300
IKLSPKKTWE GFIGGFFATV VFGLLLSYVM SGYRCFVCPV EYNNDTNSFT
310 320 330 340 350
VDCEPSDLFR LQEYNIPGVI QSLVGWKTMR MYPFQIHSAL STFASLIGPF
360 370 380 390 400
GGFFASGFKR AFKIKDFANT IPGHGGIMDR FDCQYLMATF VNVYIASFIR
410 420 430 440
GPNPSKLIQQ FLTLRPDQQL HIFNTLKSHL TDKGILMSAL EEE
Length:443
Mass (Da):51,323
Last modified:December 1, 2001 - v1
Checksum:i5CA23C56AE2B043F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB052898 mRNA. Translation: BAB61043.1.
RefSeqiNP_446095.1. NM_053643.1.
UniGeneiRn.212746.

Genome annotation databases

GeneIDi114101.
KEGGirno:114101.
UCSCiRGD:621186. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB052898 mRNA. Translation: BAB61043.1.
RefSeqiNP_446095.1. NM_053643.1.
UniGeneiRn.212746.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000028888.

PTM databases

PhosphoSiteiQ91XU8.

Proteomic databases

PaxDbiQ91XU8.
PRIDEiQ91XU8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi114101.
KEGGirno:114101.
UCSCiRGD:621186. rat.

Organism-specific databases

CTDi8760.
RGDi621186. Cds2.

Phylogenomic databases

eggNOGiCOG0575.
HOGENOMiHOG000209582.
HOVERGENiHBG002485.
InParanoidiQ91XU8.
KOiK00981.
PhylomeDBiQ91XU8.

Enzyme and pathway databases

UniPathwayiUPA00557; UER00614.
ReactomeiREACT_279858. Synthesis of PG.

Miscellaneous databases

NextBioi618261.
PROiQ91XU8.

Gene expression databases

ExpressionAtlasiQ91XU8. baseline and differential.
GenevestigatoriQ91XU8.

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]
ProtoNetiSearch...

Publicationsi

  1. "Gene cloning and characterization of rat CDP-diacylglycerol synthase type 2 (CDS2)."
    Saino-Saito S.
    Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Wistar.
    Tissue: Brain.

Entry informationi

Entry nameiCDS2_RAT
AccessioniPrimary (citable) accession number: Q91XU8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: December 1, 2001
Last modified: April 1, 2015
This is version 88 of the entry and version 1 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.