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Q99L43 (CDS2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 104. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:Cds2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length444 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Catalytic activity

CTP + phosphatidate = diphosphate + CDP-diacylglycerol.

Pathway

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

Subcellular location

Mitochondrion inner membrane; Multi-pass membrane protein; Matrix side Potential.

Sequence similarities

Belongs to the CDS family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 444444Phosphatidate cytidylyltransferase 2
PRO_0000090717

Regions

Transmembrane78 – 9821Helical; Potential
Transmembrane129 – 14921Helical; Potential
Transmembrane165 – 18521Helical; Potential
Transmembrane212 – 23221Helical; Potential
Transmembrane261 – 28121Helical; Potential
Transmembrane339 – 35921Helical; Potential

Amino acid modifications

Modified residue201Phosphoserine By similarity
Modified residue321Phosphoserine Ref.4 Ref.5
Modified residue341Phosphoserine By similarity
Modified residue361Phosphoserine By similarity

Experimental info

Sequence conflict431L → P in AAH69879. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q99L43 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 6A3568A7E90A6C53

FASTA44451,314
        10         20         30         40         50         60 
MTELRQRVVR EDAPPEDKES ESEAKLDGET ASDSESRAET APLPTSVDDT PEVLNRALSN 

        70         80         90        100        110        120 
LSSRWKNWWV RGILTLAMIA FFFIIIYLGP MVLMMIVMCV QIKCFHEIIT IGYNVYHSYD 

       130        140        150        160        170        180 
LPWFRTLSWY FLLCVNYFFY GETVTDYFFT LVQREEPLRI LSKYHRFISF ALYLTGFCMF 

       190        200        210        220        230        240 
VLSLVKKHYR LQFYMFGWTH VTLLIVVTQS HLVIHNLFEG MIWFIVPISC VICNDIMAYM 

       250        260        270        280        290        300 
FGFFFGRTPL IKLSPKKTWE GFIGGFFATV VFGLLLSYVM SGYRCFVCPV EYNNDTNSFT 

       310        320        330        340        350        360 
VDCEPSDLFR LQEYNIPGVI QSAIGWKTVR MYPFQIHSIA LSTFASLIGP FGGFFASGFK 

       370        380        390        400        410        420 
RAFKIKDFAN TIPGHGGIMD RFDCQYLMAT FVNVYIASFI RGPNPSKLIQ QFLTLRPDQQ 

       430        440 
LHIFNTLKSH LTDKGILTSA LEDE 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS16772.1.
RefSeqNP_001277968.1. NM_001291039.1.
NP_619592.1. NM_138651.7.
UniGeneMm.284503.

3D structure databases

ProteinModelPortalQ99L43.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ99L43. 1 interaction.
MINTMINT-4124036.

PTM databases

PhosphoSiteQ99L43.

Proteomic databases

MaxQBQ99L43.
PaxDbQ99L43.
PRIDEQ99L43.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000103181; ENSMUSP00000099470; ENSMUSG00000058793.
GeneID110911.
KEGGmmu:110911.
UCSCuc008mmo.1. mouse.

Organism-specific databases

CTD8760.
MGIMGI:1332236. Cds2.

Phylogenomic databases

eggNOGCOG0575.
GeneTreeENSGT00390000016175.
HOGENOMHOG000209582.
HOVERGENHBG002485.
InParanoidQ99L43.
KOK00981.
OMARILTYFV.
PhylomeDBQ99L43.
TreeFamTF313464.

Enzyme and pathway databases

BRENDA2.7.7.41. 3474.
UniPathwayUPA00557; UER00614.

Gene expression databases

ArrayExpressQ99L43.
BgeeQ99L43.
GenevestigatorQ99L43.

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

NextBio364917.
PROQ99L43.
SOURCESearch...

Entry information

Entry nameCDS2_MOUSE
AccessionPrimary (citable) accession number: Q99L43
Secondary accession number(s): Q3TMD1, Q6NSU1
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: June 1, 2001
Last modified: July 9, 2014
This is version 104 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot