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Protein

Phosphatidate cytidylyltransferase 2

Gene

Cds2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein 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.

Pathway: CDP-diacylglycerol biosynthesis

This protein is involved in step 3 of the subpathway that synthesizes CDP-diacylglycerol from sn-glycerol 3-phosphate.
Proteins known to be involved in the 3 steps of the subpathway in this organism are:
  1. Glycerol-3-phosphate acyltransferase 1, mitochondrial (Gpam), Glycerol-3-phosphate acyltransferase 4 (Agpat6), Glycerol-3-phosphate acyltransferase 3 (Agpat9), Glycerol-3-phosphate acyltransferase 2, mitochondrial (Gpat2)
  2. 1-acyl-sn-glycerol-3-phosphate acyltransferase gamma (Agpat3), 1-acyl-sn-glycerol-3-phosphate acyltransferase beta (Agpat2), 1-acyl-sn-glycerol-3-phosphate acyltransferase alpha (Agpat1), Lysocardiolipin acyltransferase 1 (Lclat1), 1-acyl-sn-glycerol-3-phosphate acyltransferase epsilon (Agpat5), 1-acyl-sn-glycerol-3-phosphate acyltransferase delta (Agpat4)
  3. Phosphatidate cytidylyltransferase, mitochondrial (Tamm41), Phosphatidate cytidylyltransferase, mitochondrial (Tamm41), Phosphatidate cytidylyltransferase (Cds2), Phosphatidate cytidylyltransferase (Cds2), Phosphatidate cytidylyltransferase 2 (Cds2), Phosphatidate cytidylyltransferase (Cds2), Phosphatidate cytidylyltransferase 1 (Cds1)
This subpathway is part of the pathway CDP-diacylglycerol biosynthesis, which is itself part of Phospholipid metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes CDP-diacylglycerol from sn-glycerol 3-phosphate, the pathway CDP-diacylglycerol biosynthesis and in Phospholipid metabolism.

GO - Molecular functioni

  • phosphatidate cytidylyltransferase activity Source: BHF-UCL

GO - Biological processi

  • CDP-diacylglycerol biosynthetic process Source: GO_Central
  • glycosylation Source: BHF-UCL
  • phosphatidylglycerol biosynthetic process Source: GO_Central
  • phototransduction Source: BHF-UCL
Complete GO annotation...

Keywords - Molecular functioni

Nucleotidyltransferase, Transferase

Keywords - Biological processi

Lipid biosynthesis, Lipid metabolism, Phospholipid biosynthesis, Phospholipid metabolism

Enzyme and pathway databases

BRENDAi2.7.7.41. 3474.
ReactomeiREACT_352856. 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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:1332236. Cds2.

Subcellular locationi

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
Transmembranei339 – 35921HelicalSequence AnalysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion inner membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 444444Phosphatidate cytidylyltransferase 2PRO_0000090717Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei20 – 201PhosphoserineBy similarity
Modified residuei30 – 301PhosphothreonineBy similarity
Modified residuei32 – 321Phosphoserine2 Publications
Modified residuei34 – 341PhosphoserineBy similarity
Modified residuei36 – 361PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ99L43.
PaxDbiQ99L43.
PRIDEiQ99L43.

PTM databases

PhosphoSiteiQ99L43.

Expressioni

Gene expression databases

BgeeiQ99L43.
ExpressionAtlasiQ99L43. baseline and differential.
GenevisibleiQ99L43. MM.

Interactioni

Protein-protein interaction databases

IntActiQ99L43. 1 interaction.
MINTiMINT-4124036.
STRINGi10090.ENSMUSP00000099470.

Structurei

3D structure databases

ProteinModelPortaliQ99L43.
SMRiQ99L43. Positions 73-383.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the CDS family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0575.
GeneTreeiENSGT00390000016175.
HOGENOMiHOG000209582.
HOVERGENiHBG002485.
InParanoidiQ99L43.
KOiK00981.
OMAiTAATEDK.
PhylomeDBiQ99L43.
TreeFamiTF313464.

Family and domain databases

InterProiIPR000374. PC_trans.
IPR016720. PC_Trfase_euk.
[Graphical view]
PIRSFiPIRSF018269. PC_trans_euk. 1 hit.
PROSITEiPS01315. CDS. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q99L43-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTELRQRVVR EDAPPEDKES ESEAKLDGET ASDSESRAET APLPTSVDDT
60 70 80 90 100
PEVLNRALSN LSSRWKNWWV RGILTLAMIA FFFIIIYLGP MVLMMIVMCV
110 120 130 140 150
QIKCFHEIIT IGYNVYHSYD LPWFRTLSWY FLLCVNYFFY GETVTDYFFT
160 170 180 190 200
LVQREEPLRI LSKYHRFISF ALYLTGFCMF 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 QSAIGWKTVR MYPFQIHSIA LSTFASLIGP
360 370 380 390 400
FGGFFASGFK RAFKIKDFAN TIPGHGGIMD RFDCQYLMAT FVNVYIASFI
410 420 430 440
RGPNPSKLIQ QFLTLRPDQQ LHIFNTLKSH LTDKGILTSA LEDE
Length:444
Mass (Da):51,314
Last modified:June 1, 2001 - v1
Checksum:i6A3568A7E90A6C53
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti43 – 431L → P in AAH69879 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY159802 mRNA. Translation: AAO17790.1.
AK036328 mRNA. Translation: BAC29384.1.
AK147541 mRNA. Translation: BAE27984.1.
AK166001 mRNA. Translation: BAE38511.1.
BC003852 mRNA. Translation: AAH03852.1.
BC069879 mRNA. Translation: AAH69879.1.
CCDSiCCDS16772.1.
RefSeqiNP_001277968.1. NM_001291039.1.
NP_619592.1. NM_138651.7.
UniGeneiMm.284503.

Genome annotation databases

EnsembliENSMUST00000103181; ENSMUSP00000099470; ENSMUSG00000058793.
GeneIDi110911.
KEGGimmu:110911.
UCSCiuc008mmo.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY159802 mRNA. Translation: AAO17790.1.
AK036328 mRNA. Translation: BAC29384.1.
AK147541 mRNA. Translation: BAE27984.1.
AK166001 mRNA. Translation: BAE38511.1.
BC003852 mRNA. Translation: AAH03852.1.
BC069879 mRNA. Translation: AAH69879.1.
CCDSiCCDS16772.1.
RefSeqiNP_001277968.1. NM_001291039.1.
NP_619592.1. NM_138651.7.
UniGeneiMm.284503.

3D structure databases

ProteinModelPortaliQ99L43.
SMRiQ99L43. Positions 73-383.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ99L43. 1 interaction.
MINTiMINT-4124036.
STRINGi10090.ENSMUSP00000099470.

PTM databases

PhosphoSiteiQ99L43.

Proteomic databases

MaxQBiQ99L43.
PaxDbiQ99L43.
PRIDEiQ99L43.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000103181; ENSMUSP00000099470; ENSMUSG00000058793.
GeneIDi110911.
KEGGimmu:110911.
UCSCiuc008mmo.1. mouse.

Organism-specific databases

CTDi8760.
MGIiMGI:1332236. Cds2.

Phylogenomic databases

eggNOGiCOG0575.
GeneTreeiENSGT00390000016175.
HOGENOMiHOG000209582.
HOVERGENiHBG002485.
InParanoidiQ99L43.
KOiK00981.
OMAiTAATEDK.
PhylomeDBiQ99L43.
TreeFamiTF313464.

Enzyme and pathway databases

UniPathwayiUPA00557; UER00614.
BRENDAi2.7.7.41. 3474.
ReactomeiREACT_352856. Synthesis of PG.

Miscellaneous databases

ChiTaRSiCds2. mouse.
NextBioi364917.
PROiQ99L43.
SOURCEiSearch...

Gene expression databases

BgeeiQ99L43.
ExpressionAtlasiQ99L43. baseline and differential.
GenevisibleiQ99L43. MM.

Family and domain databases

InterProiIPR000374. PC_trans.
IPR016720. PC_Trfase_euk.
[Graphical view]
PIRSFiPIRSF018269. PC_trans_euk. 1 hit.
PROSITEiPS01315. CDS. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation and characterization of murine Cds (CDP-diacylglycerol synthase) 1 and 2."
    Inglis S.L., Hunt D.M., Halford S.
    Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: C57BL/6J.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Cerebellum, Embryonic stem cell and Lung.
  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].
    Strain: FVB/N.
    Tissue: Embryo and Mammary tumor.
  4. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-32, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  5. "Specific phosphopeptide enrichment with immobilized titanium ion affinity chromatography adsorbent for phosphoproteome analysis."
    Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.
    J. Proteome Res. 7:3957-3967(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-32, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  6. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiCDS2_MOUSE
AccessioniPrimary (citable) accession number: Q99L43
Secondary accession number(s): Q3TMD1, Q6NSU1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: June 1, 2001
Last modified: June 24, 2015
This is version 114 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. 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.