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Q99L43

- CDS2_MOUSE

UniProt

Q99L43 - CDS2_MOUSE

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Protein

Phosphatidate cytidylyltransferase 2

Gene

Cds2

Organism
Mus musculus (Mouse)
Status
Reviewed - 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.

Pathwayi

GO - Molecular functioni

  1. phosphatidate cytidylyltransferase activity Source: BHF-UCL

GO - Biological processi

  1. CDP-diacylglycerol biosynthetic process Source: UniProtKB-UniPathway
  2. glycosylation Source: BHF-UCL
  3. 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_199032. 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: Chromosome 2

Organism-specific databases

MGIiMGI:1332236. Cds2.

Subcellular locationi

GO - Cellular componenti

  1. endoplasmic reticulum Source: BHF-UCL
  2. integral component of membrane Source: UniProtKB-KW
  3. mitochondrial inner membrane Source: UniProtKB-KW
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 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.
GenevestigatoriQ99L43.

Interactioni

Protein-protein interaction databases

IntActiQ99L43. 1 interaction.
MINTiMINT-4124036.

Structurei

3D structure databases

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

Transmembrane

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

Family & Domainsi

Sequence similaritiesi

Belongs to the CDS family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

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

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.

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:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS16772.1.
RefSeqi NP_001277968.1. NM_001291039.1.
NP_619592.1. NM_138651.7.
UniGenei Mm.284503.

3D structure databases

ProteinModelPortali Q99L43.
SMRi Q99L43. Positions 73-383.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi Q99L43. 1 interaction.
MINTi MINT-4124036.

PTM databases

PhosphoSitei Q99L43.

Proteomic databases

MaxQBi Q99L43.
PaxDbi Q99L43.
PRIDEi Q99L43.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000103181 ; ENSMUSP00000099470 ; ENSMUSG00000058793 .
GeneIDi 110911.
KEGGi mmu:110911.
UCSCi uc008mmo.1. mouse.

Organism-specific databases

CTDi 8760.
MGIi MGI:1332236. Cds2.

Phylogenomic databases

eggNOGi COG0575.
GeneTreei ENSGT00390000016175.
HOGENOMi HOG000209582.
HOVERGENi HBG002485.
InParanoidi Q99L43.
KOi K00981.
OMAi RILTYFV.
PhylomeDBi Q99L43.
TreeFami TF313464.

Enzyme and pathway databases

UniPathwayi UPA00557 ; UER00614 .
BRENDAi 2.7.7.41. 3474.
Reactomei REACT_199032. Synthesis of PG.

Miscellaneous databases

NextBioi 364917.
PROi Q99L43.
SOURCEi Search...

Gene expression databases

Bgeei Q99L43.
ExpressionAtlasi Q99L43. baseline and differential.
Genevestigatori Q99L43.

Family and domain databases

InterProi IPR000374. PC_trans.
IPR016720. PC_Trfase_euk.
[Graphical view ]
Pfami PF01148. CTP_transf_1. 1 hit.
[Graphical view ]
PIRSFi PIRSF018269. PC_trans_euk. 1 hit.
PROSITEi PS01315. CDS. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: October 29, 2014
This is version 107 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